ID OBSCN_HUMAN Reviewed; 7968 AA. AC Q5VST9; Q2A664; Q5T7G8; Q5T7G9; Q5VSU2; Q86YC7; Q8NHN0; Q8NHN1; Q8NHN2; AC Q8NHN3; Q8NHN4; Q8NHN5; Q8NHN6; Q8NHN7; Q8NHN8; Q8NHN9; Q96AA2; Q9HCD3; AC Q9HCL6; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 27-MAR-2024, entry version 202. DE RecName: Full=Obscurin; DE EC=2.7.11.1 {ECO:0000250|UniProtKB:A2AAJ9}; DE AltName: Full=Obscurin-RhoGEF; DE AltName: Full=Obscurin-myosin light chain kinase; DE Short=Obscurin-MLCK; GN Name=OBSCN; Synonyms=KIAA1556, KIAA1639; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), VARIANTS THR-51; RP ARG-502; ASP-1508; THR-3300; ARG-4381; ARG-4450 AND HIS-4534, FUNCTION, AND RP INTERACTION WITH TTN AND CALMODULIN. RC TISSUE=Heart; RX PubMed=11448995; DOI=10.1083/jcb.200102110; RA Young P.W., Ehler E., Gautel M.; RT "Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor RT protein involved in sarcomere assembly."; RL J. Cell Biol. 154:123-136(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2734-4428 (ISOFORM 5), AND NUCLEOTIDE RP SEQUENCE [MRNA] OF 6009-7968 (ISOFORM 1). RC TISSUE=Cardiac myocyte; RX PubMed=16625316; DOI=10.1007/s10974-005-9025-6; RA Fukuzawa A., Idowu S., Gautel M.; RT "Complete human gene structure of obscurin: implications for isoform RT generation by differential splicing."; RL J. Muscle Res. Cell Motil. 26:427-434(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5386-7968 (ISOFORM 2), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 2726-7968 (ISOFORM 4), AND VARIANT VAL-7172. RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [5] RP INTERACTION WITH TTN. RX PubMed=11717165; DOI=10.1161/hh2301.100981; RA Bang M.-L., Centner T., Fornoff F., Geach A.J., Gotthardt M., McNabb M., RA Witt C.C., Labeit D., Gregorio C.C., Granzier H., Labeit S.; RT "The complete gene sequence of titin, expression of an unusual ~700 kDa RT titin isoform and its interaction with obscurin identify a novel Z-line to RT I-band linking system."; RL Circ. Res. 89:1065-1072(2001). RN [6] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=11814696; DOI=10.1016/s0378-1119(01)00795-8; RA Russell M.W., Raeker M.O., Korytkowski K.A., Sonneman K.J.; RT "Identification, tissue expression and chromosomal localization of human RT obscurin-MLCK, a member of the titin and Dbl families of myosin light chain RT kinases."; RL Gene 282:237-246(2002). RN [7] RP SUBCELLULAR LOCATION, AND INTERACTION WITH ANK1. RX PubMed=12527750; DOI=10.1083/jcb.200208109; RA Bagnato P., Barone V., Giacomello E., Rossi D., Sorrentino V.; RT "Binding of an ankyrin-1 isoform to obscurin suggests a molecular link RT between the sarcoplasmic reticulum and myofibrils in striated muscles."; RL J. Cell Biol. 160:245-253(2003). RN [8] RP CHROMOSOMAL TRANSLOCATION WITH PTHB1. RX PubMed=12618763; DOI=10.1038/sj.onc.1206332; RA Vernon E.G., Malik K., Reynolds P., Powlesland R., Dallosso A.R., RA Jackson S., Henthorn K., Green E.D., Brown K.W.; RT "The parathyroid hormone-responsive B1 gene is interrupted by a RT t(1;7)(q42;p15) breakpoint associated with Wilms' tumour."; RL Oncogene 22:1371-1380(2003). RN [9] RP FUNCTION. RX PubMed=16205939; DOI=10.1007/s00418-005-0069-x; RA Borisov A.B., Sutter S.B., Kontrogianni-Konstantopoulos A., Bloch R.J., RA Westfall M.V., Russell M.W.; RT "Essential role of obscurin in cardiac myofibrillogenesis and hypertrophic RT response: evidence from small interfering RNA-mediated gene silencing."; RL Histochem. Cell Biol. 125:227-238(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6831 AND SER-7244, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP PHOSPHATIDYLINOSITOL-PHOSPHATE-BINDING, AND MUTAGENESIS OF ARG-5975 AND RP ARG-5980. RX PubMed=28826662; DOI=10.1016/j.yjmcc.2017.08.004; RA Ackermann M.A., King B., Lieberman N.A.P., Bobbili P.J., Rudloff M., RA Berndsen C.E., Wright N.T., Hecker P.A., Kontrogianni-Konstantopoulos A.; RT "Novel obscurins mediate cardiomyocyte adhesion and size via the RT PI3K/AKT/mTOR signaling pathway."; RL J. Mol. Cell. Cardiol. 111:27-39(2017). RN [12] RP STRUCTURE BY NMR OF 2826-3806. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the Ig domains of human obscurin."; RL Submitted (AUG-2007) to the PDB data bank. RN [13] RP STRUCTURE BY NMR OF 5601-5668. RA Pfuhl M., Gautel M.; RT "Solution structure of the SH3 domain of obscurin."; RL Submitted (APR-2005) to the PDB data bank. RN [14] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-1136; HIS-1792; MET-1930; LYS-2090; RP PHE-2314; GLN-3983; HIS-4558; GLN-4810 AND THR-5071. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [15] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-502; SER-804; ARG-1027; SER-1086; RP THR-1090; THR-1091; PRO-1101; ARG-1121; VAL-1133; VAL-1136; GLN-1156; RP HIS-1248; VAL-1532; MET-1566; THR-1601; VAL-3389; GLU-3426; GLY-3834; RP SER-4823; GLN-5598 AND GLN-6473. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [16] RP VARIANT ARG-4492. RX PubMed=25173926; DOI=10.1161/circgenetics.113.000486; RA Girolami F., Iascone M., Tomberli B., Bardi S., Benelli M., Marseglia G., RA Pescucci C., Pezzoli L., Sana M.E., Basso C., Marziliano N., Merlini P.A., RA Fornaro A., Cecchi F., Torricelli F., Olivotto I.; RT "Novel alpha-actinin 2 variant associated with familial hypertrophic RT cardiomyopathy and juvenile atrial arrhythmias: a massively parallel RT sequencing study."; RL Circ. Cardiovasc. Genet. 7:741-750(2014). RN [17] RP VARIANTS RHABDO1 2322-TRP--ARG-7968 DEL; 3279-LYS--ARG-7968 DEL; RP 3983-ARG--ARG-7968 DEL AND 4453-CYS--ARG-7968 DEL, AND INVOLVEMENT IN RP RHABDO1. RX PubMed=34957489; DOI=10.1093/brain/awab484; RA Cabrera-Serrano M., Caccavelli L., Savarese M., Vihola A., Jokela M., RA Johari M., Capiod T., Madrange M., Bugiardini E., Brady S., Quinlivan R., RA Merve A., Scalco R., Hilton-Jones D., Houlden H., Aydin H.I., Ceylaner S., RA Drewes S., Vockley J., Taylor R.L., Folland C., Kelly A., Goullee H., RA Ylikallio E., Auranen M., Tyynismaa H., Udd B., Forrest A.R.R., Davis M.R., RA Bratkovic D., Manton N., Robertson T., O'Gorman C., McCombe P., Laing N.G., RA Phillips L., de Lonlay P., Ravenscroft G.; RT "Bi-allelic loss-of-function OBSCN variants predispose individuals to RT severe recurrent rhabdomyolysis."; RL Brain 145:3985-3998(2022). CC -!- FUNCTION: Structural component of striated muscles which plays a role CC in myofibrillogenesis. Probably involved in the assembly of myosin into CC sarcomeric A bands in striated muscle (PubMed:11448995, CC PubMed:16205939). Has serine/threonine protein kinase activity and CC phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase CC subunit ATP1B1 (By similarity). Binds (via the PH domain) strongly to CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser CC extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), CC phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5- CC phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate CC (PtdIns(3,4,5)P3) (PubMed:28826662). {ECO:0000250|UniProtKB:A2AAJ9, CC ECO:0000269|PubMed:11448995, ECO:0000269|PubMed:16205939, CC ECO:0000269|PubMed:28826662}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000250|UniProtKB:A2AAJ9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A2AAJ9}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:A2AAJ9}; CC -!- SUBUNIT: Interacts (via protein kinase domain 2) with CDH2 and (via CC protein kinase domain 1) with ATP1B1 (By similarity). Isoform 3 CC interacts with TTN/titin and calmodulin (PubMed:11448995, CC PubMed:11717165). Isoform 3 interacts with ANK1 isoform Mu17/ank1.5 CC (PubMed:12527750). {ECO:0000250|UniProtKB:A2AAJ9, CC ECO:0000269|PubMed:11448995, ECO:0000269|PubMed:11717165, CC ECO:0000269|PubMed:12527750}. CC -!- INTERACTION: CC Q5VST9; Q8WZ42: TTN; NbExp=15; IntAct=EBI-941850, EBI-681210; CC Q5VST9-3; P16157: ANK1; NbExp=3; IntAct=EBI-941921, EBI-941686; CC Q5VST9-3; P16157-17: ANK1; NbExp=8; IntAct=EBI-941921, EBI-941819; CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, myofibril, sarcomere, M CC line {ECO:0000269|PubMed:12527750}. Cytoplasm, myofibril, sarcomere, Z CC line {ECO:0000269|PubMed:12527750}. Note=In differentiating skeletal CC muscle cells, isoform 3 primarily localizes to the sarcomeric M-line CC and less frequently to the Z-disk (PubMed:12527750). Isoform 3 CC colocalizes with ANK1 isoform Mu17/ank1.5 at the M-line in CC differentiated skeletal muscle cells (PubMed:12527750). CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line CC {ECO:0000250|UniProtKB:A2AAJ9}. Cytoplasm, myofibril, sarcomere, Z line CC {ECO:0000250|UniProtKB:A2AAJ9}. Cell membrane, sarcolemma CC {ECO:0000250|UniProtKB:A2AAJ9}. Nucleus {ECO:0000250|UniProtKB:A2AAJ9}. CC Note=Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to CC intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M CC line and Z line in cardiac muscles. {ECO:0000250|UniProtKB:A2AAJ9}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=B, obscurin-MLCK giant kinase; CC IsoId=Q5VST9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VST9-2; Sequence=VSP_018436; CC Name=3; Synonyms=unc-89-like; CC IsoId=Q5VST9-3; Sequence=VSP_018437, VSP_018438; CC Name=4; CC IsoId=Q5VST9-5; Sequence=VSP_020086, VSP_020087; CC Name=5; CC IsoId=Q5VST9-6; Sequence=VSP_026970; CC -!- PTM: Autophosphorylated by protein kinase domains 1 and 2. CC {ECO:0000250|UniProtKB:A2AAJ9}. CC -!- DISEASE: Rhabdomyolysis 1 (RHABDO1) [MIM:620235]: An autosomal CC recessive disorder characterized by severe and recurrent CC rhabdomyolysis, usually with onset in the teenage years. Some of the CC episodes may be triggered by exercise or heat; others occur CC spontaneously. Rhabdomyolysis is the rapid breakdown of damaged or CC injured skeletal myofibres and may require intensive care management. CC Muscle breakdown results in release of myofibrillar content into the CC extracellular space and circulation, resulting in hyperCKemia (hyperCK) CC and myoglobinuria. RHABDO1 patients may have a history of myalgia and CC muscle cramps that precede the initial rhabdomyolysis episodes. CC {ECO:0000269|PubMed:34957489}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving OBSCN has been found CC in Wilms tumor. Translocation t(1;7)(q42;p15) with PTHB1. CC {ECO:0000269|PubMed:12618763}. CC -!- MISCELLANEOUS: [Isoform 3]: Lacks the kinase domain. Initially CC described as obscurin. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- CAUTION: Initially the name obscurin was used to describe isoform 3 CC which lacks the kinase domains. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAC85746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAC85749.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAC85750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAB13382.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ002535; CAC44768.1; -; mRNA. DR EMBL; AJ314896; CAC85745.1; -; Genomic_DNA. DR EMBL; AJ314898; CAC85746.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ314900; CAC85747.1; -; Genomic_DNA. DR EMBL; AJ314901; CAC85749.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ314903; CAC85750.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ314904; CAC85751.1; -; Genomic_DNA. DR EMBL; AJ314905; CAC85752.1; -; Genomic_DNA. DR EMBL; AJ314906; CAC85753.1; -; Genomic_DNA. DR EMBL; AJ314907; CAC85754.1; -; Genomic_DNA. DR EMBL; AJ314908; CAC85755.1; -; Genomic_DNA. DR EMBL; AL353593; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL670729; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AM231061; CAJ76912.1; -; mRNA. DR EMBL; AB046776; BAB13382.1; ALT_FRAME; mRNA. DR EMBL; AB046859; BAB13465.2; -; mRNA. DR CCDS; CCDS1570.2; -. [Q5VST9-3] DR CCDS; CCDS58065.1; -. [Q5VST9-1] DR RefSeq; NP_001092093.2; NM_001098623.2. [Q5VST9-1] DR RefSeq; NP_443075.3; NM_052843.3. [Q5VST9-3] DR PDB; 1V1C; NMR; -; A=5601-5668. DR PDB; 2CR6; NMR; -; A=2999-3100. DR PDB; 2DKU; NMR; -; A=2915-3004. DR PDB; 2DM7; NMR; -; A=3551-3631. DR PDB; 2E7B; NMR; -; A=3184-3273. DR PDB; 2EDF; NMR; -; A=2826-2915. DR PDB; 2EDH; NMR; -; A=3614-3713. DR PDB; 2EDL; NMR; -; A=3801-3887. DR PDB; 2EDQ; NMR; -; A=3713-3806. DR PDB; 2EDR; NMR; -; A=3361-3449. DR PDB; 2EDT; NMR; -; A=3449-3537. DR PDB; 2EDW; NMR; -; A=3537-3630. DR PDB; 2ENY; NMR; -; A=2735-2825. DR PDB; 2EO1; NMR; -; A=1623-1712. DR PDB; 2GQH; NMR; -; A=3450-3543. DR PDB; 2MWC; NMR; -; A=4337-4429. DR PDB; 2N56; NMR; -; A=4430-4524. DR PDB; 2YZ8; X-ray; 2.00 A; A=3184-3273. DR PDB; 4C4K; X-ray; 1.95 A; O=9-103. DR PDB; 4RSV; X-ray; 2.41 A; A=4337-4429. DR PDB; 4UOW; X-ray; 3.30 A; 0/2/4/6/8/A/C/E/G/I/K/M/O/Q/S/U/W/Y=110-203. DR PDB; 5TZM; X-ray; 1.18 A; A=4431-4521. DR PDB; 6MG9; NMR; -; A=4247-4338. DR PDB; 7R67; NMR; -; A=1161-1254. DR PDB; 7R68; NMR; -; A=1071-1162. DR PDBsum; 1V1C; -. DR PDBsum; 2CR6; -. DR PDBsum; 2DKU; -. DR PDBsum; 2DM7; -. DR PDBsum; 2E7B; -. DR PDBsum; 2EDF; -. DR PDBsum; 2EDH; -. DR PDBsum; 2EDL; -. DR PDBsum; 2EDQ; -. DR PDBsum; 2EDR; -. DR PDBsum; 2EDT; -. DR PDBsum; 2EDW; -. DR PDBsum; 2ENY; -. DR PDBsum; 2EO1; -. DR PDBsum; 2GQH; -. DR PDBsum; 2MWC; -. DR PDBsum; 2N56; -. DR PDBsum; 2YZ8; -. DR PDBsum; 4C4K; -. DR PDBsum; 4RSV; -. DR PDBsum; 4UOW; -. DR PDBsum; 5TZM; -. DR PDBsum; 6MG9; -. DR PDBsum; 7R67; -. DR PDBsum; 7R68; -. DR SASBDB; Q5VST9; -. DR SMR; Q5VST9; -. DR BioGRID; 123847; 65. DR DIP; DIP-35727N; -. DR IntAct; Q5VST9; 40. DR MINT; Q5VST9; -. DR STRING; 9606.ENSP00000455507; -. DR GlyCosmos; Q5VST9; 1 site, 1 glycan. DR GlyGen; Q5VST9; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; Q5VST9; -. DR MetOSite; Q5VST9; -. DR PhosphoSitePlus; Q5VST9; -. DR SwissPalm; Q5VST9; -. DR BioMuta; OBSCN; -. DR DMDM; 215274225; -. DR EPD; Q5VST9; -. DR jPOST; Q5VST9; -. DR MassIVE; Q5VST9; -. DR MaxQB; Q5VST9; -. DR PeptideAtlas; Q5VST9; -. DR ProteomicsDB; 65280; -. [Q5VST9-1] DR ProteomicsDB; 65281; -. [Q5VST9-2] DR ProteomicsDB; 65282; -. [Q5VST9-3] DR ProteomicsDB; 65283; -. [Q5VST9-5] DR ProteomicsDB; 65284; -. [Q5VST9-6] DR Pumba; Q5VST9; -. DR Antibodypedia; 11615; 58 antibodies from 16 providers. DR DNASU; 84033; -. DR Ensembl; ENST00000284548.16; ENSP00000284548.11; ENSG00000154358.23. [Q5VST9-3] DR Ensembl; ENST00000422127.5; ENSP00000409493.1; ENSG00000154358.23. [Q5VST9-1] DR Ensembl; ENST00000636476.2; ENSP00000489816.2; ENSG00000154358.23. [Q5VST9-2] DR Ensembl; ENST00000662438.1; ENSP00000499633.1; ENSG00000154358.23. [Q5VST9-6] DR GeneID; 84033; -. DR KEGG; hsa:84033; -. DR UCSC; uc001hsn.4; human. [Q5VST9-1] DR AGR; HGNC:15719; -. DR CTD; 84033; -. DR DisGeNET; 84033; -. DR GeneCards; OBSCN; -. DR HGNC; HGNC:15719; OBSCN. DR HPA; ENSG00000154358; Tissue enriched (skeletal). DR MalaCards; OBSCN; -. DR MIM; 608616; gene. DR MIM; 620235; phenotype. DR neXtProt; NX_Q5VST9; -. DR OpenTargets; ENSG00000154358; -. DR Orphanet; 99845; Genetic recurrent myoglobinuria. DR PharmGKB; PA31888; -. DR VEuPathDB; HostDB:ENSG00000154358; -. DR GeneTree; ENSGT00940000154756; -. DR HOGENOM; CLU_000031_0_0_1; -. DR InParanoid; Q5VST9; -. DR OrthoDB; 4633043at2759; -. DR PhylomeDB; Q5VST9; -. DR PathwayCommons; Q5VST9; -. DR Reactome; R-HSA-193648; NRAGE signals death through JNK. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR SignaLink; Q5VST9; -. DR SIGNOR; Q5VST9; -. DR BioGRID-ORCS; 84033; 14 hits in 1186 CRISPR screens. DR ChiTaRS; OBSCN; human. DR EvolutionaryTrace; Q5VST9; -. DR GeneWiki; OBSCN; -. DR GeneWiki; Obscurin; -. DR GenomeRNAi; 84033; -. DR Pharos; Q5VST9; Tbio. DR PRO; PR:Q5VST9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5VST9; Protein. DR Bgee; ENSG00000154358; Expressed in hindlimb stylopod muscle and 120 other cell types or tissues. DR ExpressionAtlas; Q5VST9; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031430; C:M band; ISS:BHF-UCL. DR GO; GO:0030016; C:myofibril; NAS:BHF-UCL. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell. DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL. DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB. DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0008307; F:structural constituent of muscle; NAS:BHF-UCL. DR GO; GO:0031432; F:titin binding; IPI:BHF-UCL. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0036309; P:protein localization to M-band; ISS:BHF-UCL. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0045214; P:sarcomere organization; TAS:BHF-UCL. DR CDD; cd00063; FN3; 2. DR CDD; cd00096; Ig; 4. DR CDD; cd20971; IgI_1_Titin-A168_like; 1. DR CDD; cd20967; IgI_C2_MyBP-C-like; 1. DR CDD; cd13239; PH_Obscurin; 1. DR CDD; cd12025; SH3_Obscurin_like; 1. DR CDD; cd14107; STKc_obscurin_rpt1; 1. DR CDD; cd14110; STKc_obscurin_rpt2; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 61. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR035526; Obscurin_SH3. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR35971:SF4; OBSCURIN; 1. DR PANTHER; PTHR35971; SI:DKEY-31G6.6; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF07679; I-set; 51. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00069; Pkinase; 2. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00060; FN3; 3. DR SMART; SM00409; IG; 56. DR SMART; SM00408; IGc2; 49. DR SMART; SM00406; IGv; 14. DR SMART; SM00015; IQ; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SMART; SM00220; S_TKc; 2. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF49265; Fibronectin type III; 3. DR SUPFAM; SSF48726; Immunoglobulin; 57. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS50835; IG_LIKE; 47. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q5VST9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding; KW Cell membrane; Chromosomal rearrangement; Cytoplasm; Developmental protein; KW Differentiation; Disease variant; Disulfide bond; Immunoglobulin domain; KW Kinase; Lipid-binding; Magnesium; Membrane; Metal-binding; Muscle protein; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; SH3 domain; Transferase. FT CHAIN 1..7968 FT /note="Obscurin" FT /id="PRO_0000235298" FT DOMAIN 10..100 FT /note="Ig-like 1" FT DOMAIN 110..202 FT /note="Ig-like 2" FT DOMAIN 236..322 FT /note="Ig-like 3" FT DOMAIN 331..414 FT /note="Ig-like 4" FT DOMAIN 420..508 FT /note="Ig-like 5" FT DOMAIN 515..612 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 619..698 FT /note="Ig-like 6" FT DOMAIN 701..790 FT /note="Ig-like 7" FT DOMAIN 798..884 FT /note="Ig-like 8" FT DOMAIN 886..977 FT /note="Ig-like 9" FT DOMAIN 978..1066 FT /note="Ig-like 10" FT DOMAIN 1070..1161 FT /note="Ig-like 11" FT DOMAIN 1162..1252 FT /note="Ig-like 12" FT DOMAIN 1254..1345 FT /note="Ig-like 13" FT DOMAIN 1346..1432 FT /note="Ig-like 14" FT DOMAIN 1438..1524 FT /note="Ig-like 15" FT DOMAIN 1530..1621 FT /note="Ig-like 16" FT DOMAIN 1622..1719 FT /note="Ig-like 17" FT DOMAIN 1731..1808 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1809..1894 FT /note="Ig-like 18" FT DOMAIN 1896..1982 FT /note="Ig-like 19" FT DOMAIN 1987..2071 FT /note="Ig-like 20" FT DOMAIN 2077..2162 FT /note="Ig-like 21" FT DOMAIN 2165..2249 FT /note="Ig-like 22" FT DOMAIN 2289..2380 FT /note="Ig-like 23" FT DOMAIN 2468..2559 FT /note="Ig-like 24" FT DOMAIN 2564..2643 FT /note="Ig-like 25" FT DOMAIN 2646..2730 FT /note="Ig-like 26" FT DOMAIN 2736..2823 FT /note="Ig-like 27" FT DOMAIN 2826..2908 FT /note="Ig-like 28" FT DOMAIN 2920..2999 FT /note="Ig-like 29" FT DOMAIN 3003..3092 FT /note="Ig-like 30" FT DOMAIN 3095..3183 FT /note="Ig-like 31" FT DOMAIN 3184..3268 FT /note="Ig-like 32" FT DOMAIN 3273..3356 FT /note="Ig-like 33" FT DOMAIN 3359..3444 FT /note="Ig-like 34" FT DOMAIN 3449..3532 FT /note="Ig-like 35" FT DOMAIN 3537..3620 FT /note="Ig-like 36" FT DOMAIN 3625..3708 FT /note="Ig-like 37" FT DOMAIN 3713..3796 FT /note="Ig-like 38" FT DOMAIN 3801..3884 FT /note="Ig-like 39" FT DOMAIN 3890..3973 FT /note="Ig-like 40" FT DOMAIN 3978..4062 FT /note="Ig-like 41" FT DOMAIN 4068..4160 FT /note="Ig-like 42" FT DOMAIN 4171..4239 FT /note="Ig-like 43" FT DOMAIN 4248..4337 FT /note="Ig-like 44" FT DOMAIN 4340..4427 FT /note="Ig-like 45" FT DOMAIN 4430..4518 FT /note="Ig-like 46" FT DOMAIN 4525..4619 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 4624..4714 FT /note="Ig-like 47" FT DOMAIN 4872..4901 FT /note="IQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 4898..4989 FT /note="Ig-like 48" FT DOMAIN 5126..5215 FT /note="Ig-like 49" FT DOMAIN 5260..5349 FT /note="Ig-like 50" FT DOMAIN 5371..5467 FT /note="Ig-like 51" FT DOMAIN 5600..5667 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 5693..5877 FT /note="DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 5895..6004 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 6014..6097 FT /note="Ig-like 52" FT DOMAIN 6108..6200 FT /note="Ig-like 53" FT DOMAIN 6357..6445 FT /note="Ig-like 54" FT DOMAIN 6468..6721 FT /note="Protein kinase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 7463..7552 FT /note="Ig-like 55" FT DOMAIN 7557..7649 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 7672..7924 FT /note="Protein kinase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 228..249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4749..4785 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4820..4860 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 5238..5257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 5554..5596 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 6237..6296 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 6777..6863 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 6952..7176 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7217..7272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4749..4774 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 5574..5590 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 6785..6801 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7050..7064 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7077..7091 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7115..7142 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7155..7173 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 6587 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 7791 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 5975 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:58456" FT /evidence="ECO:0000269|PubMed:28826662" FT BINDING 5980 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:57658" FT /evidence="ECO:0000269|PubMed:28826662" FT BINDING 6474..6482 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 6497 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 7678..7686 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 7701 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 2889 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 4015 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 4750 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 4754 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 4757 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 4788 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 4805 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 5563 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 5569 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 5571 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 5573 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AAJ9" FT MOD_RES 6831 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 7244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT DISULFID 31..82 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 259..311 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 354..404 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 819..870 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 912..962 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1004..1054 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1096..1146 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1188..1238 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1280..1330 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1372..1422 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1464..1514 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1556..1606 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1648..1698 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1723..1791 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1830..1880 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2187..2237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2311..2361 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2490..2540 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2668..2718 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2848..2898 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2937..2987 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3117..3167 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3206..3256 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3295..3344 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3383..3432 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3471..3520 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3559..3608 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3647..3696 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3735..3784 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3823..3872 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 3911..3961 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 4000..4050 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 4089..4141 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 4453..4508 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 4919..4971 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 5147..5199 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 6035..6087 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 6129..6182 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 7484..7536 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 3886 FT /note="R -> RALPARFTQDLKTKEASEGATATLQCELSKVAPVEWKKGPETLRDGG FT RYSLKQDGTRCELQIHDLSVADAGEYSCMCGQERTSATLTVRALPARFTEGLRNEEAME FT GATATLQCELSKAAPVEWRKGLEALRDGDKYSLRQDGAVCELQIHGLAMADNGVYSCVC FT GQERTSATLTVRALPARFIEDMRNQKATEGATVTLQCKLRKAAPVEWRKGPNTLKDGDR FT YSLKQDGTSCELQIRGLVIADAGEYSCICEQERTSATLTVRALPARFIEDVRNHEATEG FT ATAVLQCELSKAAPVEWRKGSETLRDGDRYSLRQDGTRCELQIRGLAVEDTGEYLCVCG FT QERTSATLTVRALPARFIDNMTNQEAREGATATLHCELSKVAPVEWRKGPETLRDGDRH FT SLRQDGTRCELQIRGLSVADAGEYSCVCGQERTSATLTIREATEGATAMLQCELSKVAP FT VEWRKGPETLRDGDRYNLRQDGTRCELQIHGLSVADTGEYSCVCGQEKTSATLTVK FT (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_026970" FT VAR_SEQ 3888..3913 FT /note="PQPVFREPLQSLQAEEGSTATLQCEL -> LPARIHSRSEDQGGLRRGHSYT FT AV (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10997877" FT /id="VSP_020086" FT VAR_SEQ 3914..7968 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10997877" FT /id="VSP_020087" FT VAR_SEQ 5753 FT /note="S -> SS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10997877" FT /id="VSP_018436" FT VAR_SEQ 6221..6620 FT /note="DTTLERADQEVTSVLKRLLGPKAPGPSTGDLTGPGPCPRGAPALQETGSQPP FT VTGTSEAPAVPPRVPQPLLHEGPEQEPEAIARAQEWTVPIRMEGAAWPGAGTGELLWDV FT HSHVVRETTQRTYTYQAIDTHTARPPSMQVTIEDVQAQTGGTAQFEAIIEGDPQPSVTW FT YKDSVQLVDSTRLSQQQEGTTYSLVLRHVASKDAGVYTCLAQNTGGQVLCKAELLVLGG FT DNEPDSEKQSHRRKLHSFYEVKEEIGRGVFGFVKRVQHKGNKILCAAKFIPLRSRTRAQ FT AYRERDILAALSHPLVTGLLDQFETRKTLILILELCSSEELLDRLYRKGVVTEAEVKVY FT IQQLVEGLHYLHSHGVLHLDIKPSNILMVHPAREDIKICDFGFAQNITPAELQ -> VT FT EQETKVPKKTVIIEETITTVVKSPRGQRRSPSKSPSRSPSRCSASPLRPGLLAPDLLYL FT PGAGQPRRPEAEPGQKPVVPTLYVTEAEAHSPALPGLSGPQPKWVEVEETIEVRVKKMG FT PQGVSPTTEVPRSSSGHLFTLPGATPGGDPNSNNSNNKLLAQEAWAQGTAMVGVREPLV FT FRVDARGSVDWAASGMGSLEEEGTMEEAGEEEGEDGDAFVTEESQDTHSLGDRDPKILT FT HNGRMLTLADLEDYVPGEGETFHCGGPGPGAPDDPPCEVSVIQREIGEPTVGQPVLLSV FT GHALGPRGPLGLFRPEPRGASPPGPQVRSLEGTSFLLREAPARPVGSAPWTQSFCTRIR FT RSADSGQSSFTTELSTQTVNFGTVGETVTLHICPDRDGDEAAQP (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:11448995" FT /id="VSP_018437" FT VAR_SEQ 6621..7968 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11448995" FT /id="VSP_018438" FT VARIANT 51 FT /note="A -> T (in dbSNP:rs1771487)" FT /evidence="ECO:0000269|PubMed:11448995" FT /id="VAR_026409" FT VARIANT 502 FT /note="Q -> R (in dbSNP:rs1771487)" FT /evidence="ECO:0000269|PubMed:11448995, FT ECO:0000269|PubMed:17344846" FT /id="VAR_034618" FT VARIANT 804 FT /note="G -> S (in dbSNP:rs55950009)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042276" FT VARIANT 908 FT /note="A -> T (in dbSNP:rs1757153)" FT /id="VAR_047743" FT VARIANT 1027 FT /note="K -> R (in dbSNP:rs55760713)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042277" FT VARIANT 1086 FT /note="A -> S (in dbSNP:rs117147433)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042278" FT VARIANT 1090 FT /note="A -> T (in dbSNP:rs752906025)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042279" FT VARIANT 1091 FT /note="S -> T (in dbSNP:rs965007403)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042280" FT VARIANT 1101 FT /note="A -> P (in dbSNP:rs780907202)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042281" FT VARIANT 1121 FT /note="G -> R" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042282" FT VARIANT 1133 FT /note="L -> V (in dbSNP:rs777214598)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042283" FT VARIANT 1136 FT /note="A -> V (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs950055015)" FT /evidence="ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:17344846" FT /id="VAR_035530" FT VARIANT 1156 FT /note="H -> Q" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042284" FT VARIANT 1248 FT /note="Q -> H (in dbSNP:rs199523598)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042285" FT VARIANT 1508 FT /note="V -> D (in dbSNP:rs7532342)" FT /evidence="ECO:0000269|PubMed:11448995" FT /id="VAR_034619" FT VARIANT 1532 FT /note="A -> V (in dbSNP:rs453140)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042286" FT VARIANT 1566 FT /note="T -> M (in dbSNP:rs56217040)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042287" FT VARIANT 1601 FT /note="A -> T (in dbSNP:rs55706639)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042288" FT VARIANT 1792 FT /note="R -> H (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs750681123)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035531" FT VARIANT 1930 FT /note="V -> M (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs545316651)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035532" FT VARIANT 2090 FT /note="E -> K (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035533" FT VARIANT 2106 FT /note="D -> E (in dbSNP:rs1188721)" FT /id="VAR_047744" FT VARIANT 2116 FT /note="F -> L (in dbSNP:rs1188722)" FT /id="VAR_047745" FT VARIANT 2314 FT /note="S -> F (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035534" FT VARIANT 2322..7968 FT /note="Missing (risk factor for RHABDO1)" FT /evidence="ECO:0000269|PubMed:34957489" FT /id="VAR_088090" FT VARIANT 2529 FT /note="R -> Q (in dbSNP:rs3795783)" FT /id="VAR_047746" FT VARIANT 2720 FT /note="V -> M (in dbSNP:rs1188697)" FT /id="VAR_047747" FT VARIANT 2812 FT /note="R -> W (in dbSNP:rs3795785)" FT /id="VAR_047748" FT VARIANT 3279..7968 FT /note="Missing (risk factor for RHABDO1)" FT /evidence="ECO:0000269|PubMed:34957489" FT /id="VAR_088091" FT VARIANT 3300 FT /note="A -> T (in dbSNP:rs437129)" FT /evidence="ECO:0000269|PubMed:11448995" FT /id="VAR_034620" FT VARIANT 3372 FT /note="E -> D (in dbSNP:rs3795789)" FT /id="VAR_047749" FT VARIANT 3373 FT /note="S -> C (in dbSNP:rs3795790)" FT /id="VAR_047750" FT VARIANT 3389 FT /note="A -> V (in dbSNP:rs770177081)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042289" FT VARIANT 3426 FT /note="D -> E" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042290" FT VARIANT 3834 FT /note="R -> G" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042291" FT VARIANT 3983..7968 FT /note="Missing (risk factor for RHABDO1)" FT /evidence="ECO:0000269|PubMed:34957489" FT /id="VAR_088092" FT VARIANT 3983 FT /note="R -> Q (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs539154039)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035535" FT VARIANT 4039 FT /note="G -> R (in dbSNP:rs435776)" FT /id="VAR_047751" FT VARIANT 4381 FT /note="H -> R (in dbSNP:rs1150912)" FT /evidence="ECO:0000269|PubMed:11448995" FT /id="VAR_034621" FT VARIANT 4450 FT /note="C -> R (in dbSNP:rs1188732)" FT /evidence="ECO:0000269|PubMed:11448995" FT /id="VAR_034622" FT VARIANT 4453..7968 FT /note="Missing (risk factor for RHABDO1; greatly reduced FT protein levels detected by Wester blot in skeletal muscle FT from a homozygous patient)" FT /evidence="ECO:0000269|PubMed:34957489" FT /id="VAR_088093" FT VARIANT 4492 FT /note="L -> R (in dbSNP:rs369570923)" FT /evidence="ECO:0000269|PubMed:25173926" FT /id="VAR_074295" FT VARIANT 4516 FT /note="R -> W (in dbSNP:rs11810627)" FT /id="VAR_059429" FT VARIANT 4534 FT /note="R -> H (in dbSNP:rs4653942)" FT /evidence="ECO:0000269|PubMed:11448995" FT /id="VAR_026410" FT VARIANT 4558 FT /note="R -> H (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs199865640)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035536" FT VARIANT 4642 FT /note="S -> C (in dbSNP:rs1188729)" FT /id="VAR_056102" FT VARIANT 4662 FT /note="R -> C (in dbSNP:rs3795800)" FT /id="VAR_056103" FT VARIANT 4666 FT /note="G -> S (in dbSNP:rs3795801)" FT /id="VAR_056104" FT VARIANT 4810 FT /note="R -> Q (in a breast cancer sample; somatic mutation; FT dbSNP:rs570805670)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035537" FT VARIANT 4823 FT /note="A -> S" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042292" FT VARIANT 4962 FT /note="D -> G (in dbSNP:rs373610)" FT /id="VAR_056105" FT VARIANT 5071 FT /note="A -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035538" FT VARIANT 5269 FT /note="L -> V (in dbSNP:rs369909)" FT /id="VAR_056106" FT VARIANT 5575 FT /note="R -> H (in dbSNP:rs3795809)" FT /id="VAR_056107" FT VARIANT 5598 FT /note="R -> Q (in dbSNP:rs867550675)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042293" FT VARIANT 5891 FT /note="Q -> E (in dbSNP:rs1188710)" FT /id="VAR_056108" FT VARIANT 6473 FT /note="E -> Q" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042294" FT VARIANT 7172 FT /note="A -> V (in dbSNP:rs500049)" FT /evidence="ECO:0000269|PubMed:10997877" FT /id="VAR_056109" FT MUTAGEN 5975 FT /note="R->A: Reduced binding to phosphatidylinositol FT 4,5-bisphosphate." FT /evidence="ECO:0000269|PubMed:28826662" FT MUTAGEN 5980 FT /note="R->A: Reduced binding to phosphatidylinositol FT 3,4-bisphosphate." FT /evidence="ECO:0000269|PubMed:28826662" FT CONFLICT 888 FT /note="V -> A (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 895 FT /note="L -> P (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 897 FT /note="R -> C (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 899..900 FT /note="KL -> EV (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 904 FT /note="A -> V (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 917 FT /note="A -> D (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 919 FT /note="T -> M (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 937..938 FT /note="CM -> HV (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 941 FT /note="T -> V (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 944 FT /note="T -> M (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 952 FT /note="A -> V (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 957 FT /note="A -> S (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 965 FT /note="G -> R (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 969 FT /note="L -> V (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 972 FT /note="H -> R (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 999 FT /note="S -> N (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 1011 FT /note="T -> A (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 1348 FT /note="A -> V (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1355 FT /note="L -> P (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1357 FT /note="H -> R (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1359 FT /note="K -> E (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1360 FT /note="V -> L (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1367 FT /note="I -> S (in Ref. 1; CAC85746/CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1394 FT /note="S -> L (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1397..1398 FT /note="RM -> HV (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1397 FT /note="R -> C (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1401 FT /note="V -> A (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1401 FT /note="V -> T (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1413 FT /note="C -> G (in Ref. 1; CAC85746/CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1417 FT /note="T -> A (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1428 FT /note="R -> Q (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1432 FT /note="S -> H (in Ref. 1; CAC85746)" FT /evidence="ECO:0000305" FT CONFLICT 1445 FT /note="E -> D (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1455 FT /note="Q -> E (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1458 FT /note="A -> T (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1461 FT /note="T -> M (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1524 FT /note="H -> R (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1526 FT /note="H -> Q (in Ref. 1; CAC85749)" FT /evidence="ECO:0000305" FT CONFLICT 1580..1582 FT /note="VRM -> MRV (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1607 FT /note="K -> E (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1610 FT /note="D -> G (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1633 FT /note="H -> C (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1653..1655 FT /note="AQT -> GQM (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1673..1674 FT /note="RV -> HM (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1677..1679 FT /note="VGC -> SGY (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1692 FT /note="E -> D (in Ref. 1; CAC44768/CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1704 FT /note="Q -> R (in Ref. 1; CAC44768/CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1710 FT /note="Q -> H (in Ref. 1; CAC44768/CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 1848 FT /note="L -> P (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 2014 FT /note="P -> A (in Ref. 1; CAC85750)" FT /evidence="ECO:0000305" FT CONFLICT 3126 FT /note="V -> M (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 4155 FT /note="T -> TG (in Ref. 3; CAC85752)" FT /evidence="ECO:0000305" FT CONFLICT 4489 FT /note="H -> Q (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 4959 FT /note="T -> A (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 5243 FT /note="S -> ST (in Ref. 1; CAC85753)" FT /evidence="ECO:0000305" FT CONFLICT 5391 FT /note="S -> F (in Ref. 4; BAB13465)" FT /evidence="ECO:0000305" FT CONFLICT 5499..5500 FT /note="LE -> FQ (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 6115 FT /note="R -> L (in Ref. 1; CAC44768)" FT /evidence="ECO:0000305" FT CONFLICT 6570 FT /note="Q -> E (in Ref. 3; CAJ76912)" FT /evidence="ECO:0000305" FT CONFLICT 6710..6711 FT /note="PS -> SG (in Ref. 3; CAJ76912)" FT /evidence="ECO:0000305" FT STRAND 9..14 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 27..37 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 53..61 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:4C4K" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 78..85 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 87..97 FT /evidence="ECO:0007829|PDB:4C4K" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 125..137 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 154..162 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 164..171 FT /evidence="ECO:0007829|PDB:4UOW" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 180..188 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 191..202 FT /evidence="ECO:0007829|PDB:4UOW" FT STRAND 1082..1086 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1090..1096 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1099..1101 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1106..1111 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1116..1124 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1126..1136 FT /evidence="ECO:0007829|PDB:7R68" FT HELIX 1138..1140 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1142..1147 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1152..1159 FT /evidence="ECO:0007829|PDB:7R68" FT STRAND 1164..1167 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1174..1178 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1182..1186 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1198..1201 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1210..1217 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1220..1227 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1237..1239 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1248..1251 FT /evidence="ECO:0007829|PDB:7R67" FT STRAND 1634..1639 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1644..1646 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1653..1655 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1658..1661 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1670..1677 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1680..1685 FT /evidence="ECO:0007829|PDB:2EO1" FT TURN 1690..1692 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1696..1700 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 1707..1712 FT /evidence="ECO:0007829|PDB:2EO1" FT STRAND 2745..2750 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2753..2758 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2771..2776 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2784..2788 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2791..2796 FT /evidence="ECO:0007829|PDB:2ENY" FT TURN 2801..2803 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2807..2811 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2814..2818 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2820..2823 FT /evidence="ECO:0007829|PDB:2ENY" FT STRAND 2829..2831 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2836..2838 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2844..2846 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2849..2854 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2859..2863 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2869..2877 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2880..2887 FT /evidence="ECO:0007829|PDB:2EDF" FT TURN 2890..2892 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2894..2899 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2904..2911 FT /evidence="ECO:0007829|PDB:2EDF" FT STRAND 2925..2928 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 2931..2938 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 2947..2952 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 2957..2966 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 2969..2976 FT /evidence="ECO:0007829|PDB:2DKU" FT TURN 2979..2981 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 2983..2988 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 2996..3001 FT /evidence="ECO:0007829|PDB:2DKU" FT STRAND 3006..3009 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3013..3017 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3027..3030 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3037..3042 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3048..3050 FT /evidence="ECO:0007829|PDB:2CR6" FT TURN 3057..3059 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3063..3065 FT /evidence="ECO:0007829|PDB:2CR6" FT TURN 3070..3072 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3074..3080 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3087..3092 FT /evidence="ECO:0007829|PDB:2CR6" FT STRAND 3187..3189 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3194..3197 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3202..3210 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3216..3219 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3227..3235 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3238..3243 FT /evidence="ECO:0007829|PDB:2YZ8" FT HELIX 3248..3250 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3252..3258 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3261..3270 FT /evidence="ECO:0007829|PDB:2YZ8" FT STRAND 3371..3374 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3386..3388 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3392..3397 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3402..3405 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3407..3410 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3412..3421 FT /evidence="ECO:0007829|PDB:2EDR" FT TURN 3424..3426 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3430..3433 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3438..3441 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3443..3446 FT /evidence="ECO:0007829|PDB:2EDR" FT STRAND 3452..3454 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3459..3462 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3467..3475 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3480..3483 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3490..3509 FT /evidence="ECO:0007829|PDB:2EDT" FT TURN 3512..3514 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3516..3522 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3525..3534 FT /evidence="ECO:0007829|PDB:2EDT" FT STRAND 3548..3550 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3555..3564 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3568..3575 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3578..3581 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3583..3587 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3590..3597 FT /evidence="ECO:0007829|PDB:2DM7" FT TURN 3600..3602 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3604..3610 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3613..3618 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3620..3622 FT /evidence="ECO:0007829|PDB:2DM7" FT STRAND 3628..3630 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3643..3651 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3656..3663 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3667..3675 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3678..3683 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3692..3698 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3701..3709 FT /evidence="ECO:0007829|PDB:2EDH" FT STRAND 3716..3718 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3723..3726 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3731..3739 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3744..3751 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3754..3757 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3759..3763 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3766..3773 FT /evidence="ECO:0007829|PDB:2EDQ" FT TURN 3776..3778 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3780..3788 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3790..3798 FT /evidence="ECO:0007829|PDB:2EDQ" FT STRAND 3811..3814 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3820..3824 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3826..3828 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3831..3837 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3842..3848 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3852..3861 FT /evidence="ECO:0007829|PDB:2EDL" FT HELIX 3864..3866 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3870..3874 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3877..3880 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 3883..3886 FT /evidence="ECO:0007829|PDB:2EDL" FT STRAND 4257..4262 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4267..4272 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4282..4285 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4294..4301 FT /evidence="ECO:0007829|PDB:6MG9" FT TURN 4302..4304 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4305..4310 FT /evidence="ECO:0007829|PDB:6MG9" FT TURN 4315..4317 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4319..4324 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4329..4337 FT /evidence="ECO:0007829|PDB:6MG9" FT STRAND 4342..4344 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4349..4351 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4353..4365 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4369..4375 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4386..4391 FT /evidence="ECO:0007829|PDB:4RSV" FT HELIX 4392..4394 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4396..4403 FT /evidence="ECO:0007829|PDB:4RSV" FT HELIX 4406..4408 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4410..4416 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4419..4427 FT /evidence="ECO:0007829|PDB:4RSV" FT STRAND 4434..4436 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4441..4444 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4449..4457 FT /evidence="ECO:0007829|PDB:5TZM" FT HELIX 4461..4463 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4464..4468 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4478..4485 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4488..4495 FT /evidence="ECO:0007829|PDB:5TZM" FT HELIX 4498..4500 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4502..4508 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 4511..4520 FT /evidence="ECO:0007829|PDB:5TZM" FT STRAND 5604..5609 FT /evidence="ECO:0007829|PDB:1V1C" FT STRAND 5628..5636 FT /evidence="ECO:0007829|PDB:1V1C" FT STRAND 5639..5644 FT /evidence="ECO:0007829|PDB:1V1C" FT STRAND 5654..5657 FT /evidence="ECO:0007829|PDB:1V1C" FT HELIX 5659..5661 FT /evidence="ECO:0007829|PDB:1V1C" FT STRAND 5662..5665 FT /evidence="ECO:0007829|PDB:1V1C" SQ SEQUENCE 7968 AA; 868484 MW; 46550B34565CAC76 CRC64; MDQPQFSGAP RFLTRPKAFV VSVGKDATLS CQIVGNPTPQ VSWEKDQQPV AAGARFRLAQ DGDLYRLTIL DLALGDSGQY VCRARNAIGE AFAAVGLQVD AEAACAEQAP HFLLRPTSIR VREGSEATFR CRVGGSPRPA VSWSKDGRRL GEPDGPRVRV EELGEASALR IRAARPRDGG TYEVRAENPL GAASAAAALV VDSDAADTAS RPGTSTAALL AHLQRRREAM RAEGAPASPP STGTRTCTVT EGKHARLSCY VTGEPKPETV WKKDGQLVTE GRRHVVYEDA QENFVLKILF CKQSDRGLYT CTASNLVGQT YSSVLVVVRE PAVPFKKRLQ DLEVREKESA TFLCEVPQPS TEAAWFKEET RLWASAKYGI EEEGTERRLT VRNVSADDDA VYICETPEGS RTVAELAVQG NLLRKLPRKT AVRVGDTAMF CVELAVPVGP VHWLRNQEEV VAGGRVAISA EGTRHTLTIS QCCLEDVGQV AFMAGDCQTS TQFCVSAPRK PPLQPPVDPV VKARMESSVI LSWSPPPHGE RPVTIDGYLV EKKKLGTYTW IRCHEAEWVA TPELTVADVA EEGNFQFRVS ALNSFGQSPY LEFPGTVHLA PKLAVRTPLK AVQAVEGGEV TFSVDLTVAS AGEWFLDGQA LKASSVYEIH CDRTRHTLTI REVPASLHGA QLKFVANGIE SSIRMEVRAA PGLTANKPPA AAAREVLARL HEEAQLLAEL SDQAAAVTWL KDGRTLSPGP KYEVQASAGR RVLLVRDVAR DDAGLYECVS RGGRIAYQLS VQGLARFLHK DMAGSCVDAV AGGPAQFECE TSEAHVHVHW YKDGMELGHS GERFLQEDVG TRHRLVAATV TRQDEGTYSC RVGEDSVDFR LRVSEPKVVF AKEQLARRKL QAEAGASATL SCEVAQAQTE VTWYKDGKKL SSSSKVCMEA TGCTRRLVVQ QAGQADAGEY SCEAGGQRLS FHLDVKEPKV VFAKDQVAHS EVQAEAGASA TLSCEVAQAQ TEVMWYKDGK KLSSSLKVHV EAKGCRRRLV VQQAGKTDAG DYSCEARGQR VSFRLHITEP KMMFAKEQSV HNEVQAEAGA SAMLSCEVAQ AQTEVTWYKD GKKLSSSSKV GMEVKGCTRR LVLPQAGKAD AGEYSCEAGG QRVSFHLHIT EPKGVFAKEQ SVHNEVQAEA GTTAMLSCEV AQPQTEVTWY KDGKKLSSSS KVRMEVKGCT RRLVVQQVGK ADAGEYSCEA GGQRVSFQLH ITEPKAVFAK EQLVHNEVRT EAGASATLSC EVAQAQTEVT WYKDGKKLSS SSKVRIEAAG CMRQLVVQQA GQADAGEYTC EAGGQRLSFH LDVSEPKAVF AKEQLAHRKV QAEAGAIATL SCEVAQAQTE VTWYKDGKKL SSSSKVRMEA VGCTRRLVVQ QACQADTGEY SCEAGGQRLS FSLDVAEPKV VFAKEQPVHR EVQAQAGAST TLSCEVAQAQ TEVMWYKDGK KLSFSSKVRM EAVGCTRRLV VQQAGQAVAG EYSCEAGSQR LSFHLHVAEP KAVFAKEQPA SREVQAEAGT SATLSCEVAQ AQTEVTWYKD GKKLSSSSKV RMEAVGCTRR LVVQEAGQAD AGEYSCKAGD QRLSFHLHVA EPKVVFAKEQ PAHREVQAEA GASATLSCEV AQAQTEVTWY KDGKKLSSSS KVRVEAVGCT RRLVVQQAGQ AEAGEYSCEA GGQQLSFRLQ VAELEPQISE RPCRREPLVV KEHEDIILTA TLATPSAATV TWLKDGVEIR RSKRHETASQ GDTHTLTVHG AQVLDSAIYS CRVGAEGQDF PVQVEEVAAK FCRLLEPVCG ELGGTVTLAC ELSPACAEVV WRCGNTQLRV GKRFQMVAEG PVRSLTVLGL RAEDAGEYVC ESRDDHTSAQ LTVSVPRVVK FMSGLSTVVA EEGGEATFQC VVSPSDVAVV WFRDGALLQP SEKFAISQSG ASHSLTISDL VLEDAGQITV EAEGASSSAA LRVREAPVLF KKKLEPQTVE ERSSVTLEVE LTRPWPELRW TRNATALAPG KNVEIHAEGA RHRLVLHNVG FADRGFFGCE TPDDKTQAKL TVEMRQVRLV RGLQAVEARE QGTATMEVQL SHADVDGSWT RDGLRFQQGP TCHLAVRGPM HTLTLSGLRP EDSGLMVFKA EGVHTSARLV VTELPVSFSR PLQDVVTTEK EKVTLECELS RPNVDVRWLK DGVELRAGKT MAIAAQGACR SLTIYRCEFA DQGVYVCDAH DAQSSASVKV QGRTYTLIYR RVLAEDAGEI QFVAENAESR AQLRVKELPV TLVRPLRDKI AMEKHRGVLE CQVSRASAQV RWFKGSQELQ PGPKYELVSD GLYRKLIISD VHAEDEDTYT CDAGDVKTSA QFFVEEQSIT IVRGLQDVTV MEPAPAWFEC ETSIPSVRPP KWLLGKTVLQ AGGNVGLEQE GTVHRLMLRR TCSTMTGPVH FTVGKSRSSA RLVVSDIPVV LTRPLEPKTG RELQSVVLSC DFRPAPKAVQ WYKDDTPLSP SEKFKMSLEG QMAELRILRL MPADAGVYRC QAGSAHSSTE VTVEAREVTV TGPLQDAEAT EEGWASFSCE LSHEDEEVEW SLNGMPLYND SFHEISHKGR RHTLVLKSIQ RADAGIVRAS SLKVSTSARL EVRVKPVVFL KALDDLSAEE RGTLALQCEV SDPEAHVVWR KDGVQLGPSD KYDFLHTAGT RGLVVHDVSP EDAGLYTCHV GSEETRARVR VHDLHVGITK RLKTMEVLEG ESCSFECVLS HESASDPAMW TVGGKTVGSS SRFQATRQGR KYILVVREAA PSDAGEVVFS VRGLTSKASL IVRERPAAII KPLEDQWVAP GEDVELRCEL SRAGTPVHWL KDRKAIRKSQ KYDVVCEGTM AMLVIRGASL KDAGEYTCEV EASKSTASLH VEEKANCFTE ELTNLQVEEK GTAVFTCKTE HPAATVTWRK GLLELRASGK HQPSQEGLTL RLTISALEKA DSDTYTCDIG QAQSRAQLLV QGRRVHIIED LEDVDVQEGS SATFRCRISP ANYEPVHWFL DKTPLHANEL NEIDAQPGGY HVLTLRQLAL KDSGTIYFEA GDQRASAALR VTEKPSVFSR ELTDATITEG EDLTLVCETS TCDIPVCWTK DGKTLRGSAR CQLSHEGHRA QLLITGATLQ DSGRYKCEAG GACSSSIVRV HARPVRFQEA LKDLEVLEGG AATLRCVLSS VAAPVKWCYG NNVLRPGDKY SLRQEGAMLE LVVRNLRPQD SGRYSCSFGD QTTSATLTVT ALPAQFIGKL RNKEATEGAT ATLRCELSKA APVEWRKGSE TLRDGDRYCL RQDGAMCELQ IRGLAMVDAA EYSCVCGEER TSASLTIRPM PAHFIGRLRH QESIEGATAT LRCELSKAAP VEWRKGRESL RDGDRHSLRQ DGAVCELQIC GLAVADAGEY SCVCGEERTS ATLTVKALPA KFTEGLRNEE AVEGATAMLW CELSKVAPVE WRKGPENLRD GDRYILRQEG TRCELQICGL AMADAGEYLC VCGQERTSAT LTIRALPARF IEDVKNQEAR EGATAVLQCE LNSAAPVEWR KGSETLRDGD RYSLRQDGTK CELQIRGLAM ADTGEYSCVC GQERTSAMLT VRALPIKFTE GLRNEEATEG ATAVLRCELS KMAPVEWWKG HETLRDGDRH SLRQDGARCE LQIRGLVAED AGEYLCMCGK ERTSAMLTVR AMPSKFIEGL RNEEATEGDT ATLWCELSKA APVEWRKGHE TLRDGDRHSL RQDGSRCELQ IRGLAVVDAG EYSCVCGQER TSATLTVRAL PARFIEDVKN QEAREGATAV LQCELSKAAP VEWRKGSETL RGGDRYSLRQ DGTRCELQIH GLSVADTGEY SCVCGQERTS ATLTVRAPQP VFREPLQSLQ AEEGSTATLQ CELSEPTATV VWSKGGLQLQ ANGRREPRLQ GCTAELVLQD LQREDTGEYT CTCGSQATSA TLTVTAAPVR FLRELQHQEV DEGGTAHLCC ELSRAGASVE WRKGSLQLFP CAKYQMVQDG AAAELLVRGV EQEDAGDYTC DTGHTQSMAS LSVRVPRPKF KTRLQSLEQE TGDIARLCCQ LSDAESGAVV QWLKEGVELH AGPKYEMRSQ GATRELLIHQ LEAKDTGEYA CVTGGQKTAA SLRVTEPEVT IVRGLVDAEV TADEDVEFSC EVSRAGATGV QWCLQGLPLQ SNEVTEVAVR DGRIHTLRLK GVTPEDAGTV SFHLGNHASS AQLTVRAPEV TILEPLQDVQ LSEGQDASFQ CRLSRASGQE ARWALGGVPL QANEMNDITV EQGTLHLLTL HKVTLEDAGT VSFHVGTCSS EAQLKVTAKN TVVRGLENVE ALEGGEALFE CQLSQPEVAA HTWLLDDEPV HTSENAEVVF FENGLRHLLL LKNLRPQDSC RVTFLAGDMV TSAFLTVRGW RLEILEPLKN AAVRAGAQAC FTCTLSEAVP VGEASWYING AAVQPDDSDW TVTADGSHHA LLLRSAQPHH AGEVTFACRD AVASARLTVL GLPDPPEDAE VVARSSHTVT LSWAAPMSDG GGGLCGYRVE VKEGATGQWR LCHELVPGPE CVVDGLAPGE TYRFRVAAVG PVGAGEPVHL PQTVRLAEPP KPVPPQPSAP ESRQVAAGED VSLELEVVAE AGEVIWHKGM ERIQPGGRFE VVSQGRQQML VIKGFTAEDQ GEYHCGLAQG SICPAAATFQ VALSPASVDE APQPSLPPEA AQEGDLHLLW EALARKRRMS REPTLDSISE LPEEDGRSQR LPQEAEEVAP DLSEGYSTAD ELARTGDADL SHTSSDDESR AGTPSLVTYL KKAGRPGTSP LASKVGAPAA PSVKPQQQQE PLAAVRPPLG DLSTKDLGDP SMDKAAVKIQ AAFKGYKVRK EMKQQEGPMF SHTFGDTEAQ VGDALRLECV VASKADVRAR WLKDGVELTD GRHHHIDQLG DGTCSLLITG LDRADAGCYT CQVSNKFGQV THSACVVVSG SESEAESSSG GELDDAFRRA ARRLHRLFRT KSPAEVSDEE LFLSADEGPA EPEEPADWQT YREDEHFICI RFEALTEARQ AVTRFQEMFA TLGIGVEIKL VEQGPRRVEM CISKETPAPV VPPEPLPSLL TSDAAPVFLT ELQNQEVQDG YPVSFDCVVT GQPMPSVRWF KDGKLLEEDD HYMINEDQQG GHQLIITAVV PADMGVYRCL AENSMGVSST KAELRVDLTS TDYDTAADAT ESSSYFSAQG YLSSREQEGT ESTTDEGQLP QVVEELRDLQ VAPGTRLAKF QLKVKGYPAP RLYWFKDGQP LTASAHIRMT DKKILHTLEI ISVTREDSGQ YAAYISNAMG AAYSSARLLV RGPDEPEEKP ASDVHEQLVP PRMLERFTPK KVKKGSSITF SVKVEGRPVP TVHWLREEAE RGVLWIGPDT PGYTVASSAQ QHSLVLLDVG RQHQGTYTCI ASNAAGQALC SASLHVSGLP KVEEQEKVKE ALISTFLQGT TQAISAQGLE TASFADLGGQ RKEEPLAAKE ALGHLSLAEV GTEEFLQKLT SQITEMVSAK ITQAKLQVPG GDSDEDSKTP SASPRHGRSR PSSSIQESSS ESEDGDARGE IFDIYVVTAD YLPLGAEQDA ITLREGQYVE VLDAAHPLRW LVRTKPTKSS PSRQGWVSPA YLDRRLKLSP EWGAAEAPEF PGEAVSEDEY KARLSSVIQE LLSSEQAFVE ELQFLQSHHL QHLERCPHVP IAVAGQKAVI FRNVRDIGRF HSSFLQELQQ CDTDDDVAMC FIKNQAAFEQ YLEFLVGRVQ AESVVVSTAI QEFYKKYAEE ALLAGDPSQP PPPPLQHYLE QPVERVQRYQ ALLKELIRNK ARNRQNCALL EQAYAVVSAL PQRAENKLHV SLMENYPGTL QALGEPIRQG HFIVWEGAPG ARMPWKGHNR HVFLFRNHLV ICKPRRDSRT DTVSYVFRNM MKLSSIDLND QVEGDDRAFE VWQEREDSVR KYLLQARTAI IKSSWVKEIC GIQQRLALPV WRPPDFEEEL ADCTAELGET VKLACRVTGT PKPVISWYKD GKAVQVDPHH ILIEDPDGSC ALILDSLTGV DSGQYMCFAA SAAGNCSTLG KILVQVPPRF VNKVRASPFV EGEDAQFTCT IEGAPYPQIR WYKDGALLTT GNKFQTLSEP RSGLLVLVIR AASKEDLGLY ECELVNRLGS ARASAELRIQ SPMLQAQEQC HREQLVAAVE DTTLERADQE VTSVLKRLLG PKAPGPSTGD LTGPGPCPRG APALQETGSQ PPVTGTSEAP AVPPRVPQPL LHEGPEQEPE AIARAQEWTV PIRMEGAAWP GAGTGELLWD VHSHVVRETT QRTYTYQAID THTARPPSMQ VTIEDVQAQT GGTAQFEAII EGDPQPSVTW YKDSVQLVDS TRLSQQQEGT TYSLVLRHVA SKDAGVYTCL AQNTGGQVLC KAELLVLGGD NEPDSEKQSH RRKLHSFYEV KEEIGRGVFG FVKRVQHKGN KILCAAKFIP LRSRTRAQAY RERDILAALS HPLVTGLLDQ FETRKTLILI LELCSSEELL DRLYRKGVVT EAEVKVYIQQ LVEGLHYLHS HGVLHLDIKP SNILMVHPAR EDIKICDFGF AQNITPAELQ FSQYGSPEFV SPEIIQQNPV SEASDIWAMG VISYLSLTCS SPFAGESDRA TLLNVLEGRV SWSSPMAAHL SEDAKDFIKA TLQRAPQARP SAAQCLSHPW FLKSMPAEEA HFINTKQLKF LLARSRWQRS LMSYKSILVM RSIPELLRGP PDSPSLGVAR HLCRDTGGSS SSSSSSDNEL APFARAKSLP PSPVTHSPLL HPRGFLRPSA SLPEEAEASE RSTEAPAPPA SPEGAGPPAA QGCVPRHSVI RSLFYHQAGE SPEHGALAPG SRRHPARRRH LLKGGYIAGA LPGLREPLME HRVLEEEAAR EEQATLLAKA PSFETALRLP ASGTHLAPGH SHSLEHDSPS TPRPSSEACG EAQRLPSAPS GGAPIRDMGH PQGSKQLPST GGHPGTAQPE RPSPDSPWGQ PAPFCHPKQG SAPQEGCSPH PAVAPCPPGS FPPGSCKEAP LVPSSPFLGQ PQAPPAPAKA SPPLDSKMGP GDISLPGRPK PGPCSSPGSA SQASSSQVSS LRVGSSQVGT EPGPSLDAEG WTQEAEDLSD STPTLQRPQE QATMRKFSLG GRGGYAGVAG YGTFAFGGDA GGMLGQGPMW ARIAWAVSQS EEEEQEEARA ESQSEEQQEA RAESPLPQVS ARPVPEVGRA PTRSSPEPTP WEDIGQVSLV QIRDLSGDAE AADTISLDIS EVDPAYLNLS DLYDIKYLPF EFMIFRKVPK SAQPEPPSPM AEEELAEFPE PTWPWPGELG PHAGLEITEE SEDVDALLAE AAVGRKRKWS SPSRSLFHFP GRHLPLDEPA ELGLRERVKA SVEHISRILK GRPEGLEKEG PPRKKPGLAS FRLSGLKSWD RAPTFLRELS DETVVLGQSV TLACQVSAQP AAQATWSKDG APLESSSRVL ISATLKNFQL LTILVVVAED LGVYTCSVSN ALGTVTTTGV LRKAERPSSS PCPDIGEVYA DGVLLVWKPV ESYGPVTYIV QCSLEGGSWT TLASDIFDCC YLTSKLSRGG TYTFRTACVS KAGMGPYSSP SEQVLLGGPS HLASEEESQG RSAQPLPSTK TFAFQTQIQR GRFSVVRQCW EKASGRALAA KIIPYHPKDK TAVLREYEAL KGLRHPHLAQ LHAAYLSPRH LVLILELCSG PELLPCLAER ASYSESEVKD YLWQMLSATQ YLHNQHILHL DLRSENMIIT EYNLLKVVDL GNAQSLSQEK VLPSDKFKDY LETMAPELLE GQGAVPQTDI WAIGVTAFIM LSAEYPVSSE GARDLQRGLR KGLVRLSRCY AGLSGGAVAF LRSTLCAQPW GRPCASSCLQ CPWLTEEGPA CSRPAPVTFP TARLRVFVRN REKRRALLYK RHNLAQVR //