ID INSRR_HUMAN Reviewed; 1297 AA. AC P14616; O60724; Q5VZS3; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 27-MAR-2024, entry version 212. DE RecName: Full=Insulin receptor-related protein; DE Short=IRR; DE EC=2.7.10.1; DE AltName: Full=IR-related receptor; DE Contains: DE RecName: Full=Insulin receptor-related protein alpha chain; DE Contains: DE RecName: Full=Insulin receptor-related protein beta chain; DE Flags: Precursor; GN Name=INSRR; Synonyms=IRR; 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 [MRNA]. RC TISSUE=Kidney; RX PubMed=10226785; DOI=10.1055/s-2007-978702; RA Haenze J., Berthold A., Klammt J., Gallaher B., Siebler T., Kratzsch J., RA Elmlinger M., Kiess W.; RT "Cloning and sequencing of the complete cDNA encoding the human insulin RT receptor related receptor."; RL Horm. Metab. Res. 31:77-79(1999). 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 [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-1297. RX PubMed=2768234; DOI=10.1016/s0021-9258(18)63737-8; RA Shier P., Watt V.M.; RT "Primary structure of a putative receptor for a ligand of the insulin RT family."; RL J. Biol. Chem. 264:14605-14608(1989). RN [5] RP VARIANTS [LARGE SCALE ANALYSIS] GLU-127; VAL-161; HIS-244; ARG-246; RP GLN-278; CYS-554; LEU-928 AND GLU-1065. 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 [6] RP FUNCTION, MUTAGENESIS OF 1145-TYR-TYR-1146, AND AUTOPHOSPHORYLATION. RX PubMed=21641549; DOI=10.1016/j.cmet.2011.03.022; RA Deyev I.E., Sohet F., Vassilenko K.P., Serova O.V., Popova N.V., RA Zozulya S.A., Burova E.B., Houillier P., Rzhevsky D.I., Berchatova A.A., RA Murashev A.N., Chugunov A.O., Efremov R.G., Nikol'sky N.N., Bertelli E., RA Eladari D., Petrenko A.G.; RT "Insulin receptor-related receptor as an extracellular alkali sensor."; RL Cell Metab. 13:679-689(2011). CC -!- FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as CC a pH sensing receptor which is activated by increased extracellular pH. CC Activates an intracellular signaling pathway that involves IRS1 and CC AKT1/PKB. {ECO:0000269|PubMed:21641549}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBUNIT: Probable tetramer of 2 alpha and 2 beta chains linked by CC disulfide bonds. The alpha chains contribute to the formation of the CC ligand-binding domain, while the beta chains carry the kinase domain. CC -!- INTERACTION: CC P14616; P08238: HSP90AB1; NbExp=3; IntAct=EBI-6424336, EBI-352572; CC P14616; P06213: INSR; NbExp=4; IntAct=EBI-6424336, EBI-475899; CC P14616; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6424336, EBI-16439278; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- DOMAIN: The extracellular domain is required for sensing alterations in CC external pH. CC -!- PTM: Autophosphorylated on tyrosine residues between pH 7.9 and pH CC 10.5. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. 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; AF064078; AAC17167.1; -; mRNA. DR EMBL; AL158169; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52903.1; -; Genomic_DNA. DR EMBL; J05046; AAC31759.1; -; mRNA. DR CCDS; CCDS1160.1; -. DR PIR; B36502; B36502. DR RefSeq; NP_055030.1; NM_014215.2. DR PDB; 7PL4; NMR; -; A=918-948. DR PDB; 7TYJ; EM; 3.30 A; A/B=1-1297. DR PDB; 7TYK; EM; 3.50 A; A/B=1-1297. DR PDB; 7TYM; EM; 3.40 A; A/B=1-1297. DR PDBsum; 7PL4; -. DR PDBsum; 7TYJ; -. DR PDBsum; 7TYK; -. DR PDBsum; 7TYM; -. DR AlphaFoldDB; P14616; -. DR EMDB; EMD-26181; -. DR EMDB; EMD-26183; -. DR EMDB; EMD-26185; -. DR SASBDB; P14616; -. DR SMR; P14616; -. DR BioGRID; 109856; 97. DR IntAct; P14616; 39. DR MINT; P14616; -. DR STRING; 9606.ENSP00000357178; -. DR BindingDB; P14616; -. DR ChEMBL; CHEMBL5483; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; P14616; -. DR GuidetoPHARMACOLOGY; 1802; -. DR GlyCosmos; P14616; 10 sites, No reported glycans. DR GlyGen; P14616; 10 sites. DR iPTMnet; P14616; -. DR PhosphoSitePlus; P14616; -. DR BioMuta; INSRR; -. DR DMDM; 12644000; -. DR EPD; P14616; -. DR jPOST; P14616; -. DR MassIVE; P14616; -. DR MaxQB; P14616; -. DR PaxDb; 9606-ENSP00000357178; -. DR PeptideAtlas; P14616; -. DR Antibodypedia; 20446; 438 antibodies from 34 providers. DR DNASU; 3645; -. DR Ensembl; ENST00000368195.4; ENSP00000357178.3; ENSG00000027644.5. DR GeneID; 3645; -. DR KEGG; hsa:3645; -. DR MANE-Select; ENST00000368195.4; ENSP00000357178.3; NM_014215.3; NP_055030.1. DR UCSC; uc010pht.3; human. DR AGR; HGNC:6093; -. DR CTD; 3645; -. DR DisGeNET; 3645; -. DR GeneCards; INSRR; -. DR HGNC; HGNC:6093; INSRR. DR HPA; ENSG00000027644; Tissue enhanced (kidney, testis). DR MIM; 147671; gene. DR neXtProt; NX_P14616; -. DR OpenTargets; ENSG00000027644; -. DR PharmGKB; PA29899; -. DR VEuPathDB; HostDB:ENSG00000027644; -. DR eggNOG; KOG1095; Eukaryota. DR eggNOG; KOG4258; Eukaryota. DR GeneTree; ENSGT00940000160437; -. DR HOGENOM; CLU_000288_166_0_1; -. DR InParanoid; P14616; -. DR OMA; IQRGHVY; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P14616; -. DR TreeFam; TF351636; -. DR BRENDA; 2.7.10.1; 2681. DR PathwayCommons; P14616; -. DR SignaLink; P14616; -. DR BioGRID-ORCS; 3645; 12 hits in 1175 CRISPR screens. DR GeneWiki; INSRR; -. DR GenomeRNAi; 3645; -. DR Pharos; P14616; Tchem. DR PRO; PR:P14616; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P14616; Protein. DR Bgee; ENSG00000027644; Expressed in adult mammalian kidney and 60 other cell types or tissues. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0005899; C:insulin receptor complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; NAS:UniProtKB. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005009; F:insulin receptor activity; IBA:GO_Central. DR GO; GO:0043560; F:insulin receptor substrate binding; IBA:GO_Central. DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0071469; P:cellular response to alkaline pH; IDA:UniProtKB. DR GO; GO:0030238; P:male sex determination; IEA:Ensembl. DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR CDD; cd00063; FN3; 3. DR CDD; cd00064; FU; 1. DR CDD; cd05032; PTKc_InsR_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR Gene3D; 3.80.20.20; Receptor L-domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR006211; Furin-like_Cys-rich_dom. DR InterPro; IPR006212; Furin_repeat. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR000494; Rcpt_L-dom. DR InterPro; IPR036941; Rcpt_L-dom_sf. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt. DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS. DR PANTHER; PTHR24416:SF338; INSULIN RECEPTOR-RELATED PROTEIN; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF00757; Furin-like; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF01030; Recep_L_domain; 2. DR PIRSF; PIRSF000620; Insulin_receptor; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00060; FN3; 3. DR SMART; SM00261; FU; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF49265; Fibronectin type III; 3. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF52058; L domain-like; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. DR Genevisible; P14616; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cleavage on pair of basic residues; KW Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase; KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..1297 FT /note="Insulin receptor-related protein" FT /id="PRO_0000016701" FT CHAIN 27..742 FT /note="Insulin receptor-related protein alpha chain" FT /evidence="ECO:0000305" FT /id="PRO_0000016702" FT CHAIN 747..1297 FT /note="Insulin receptor-related protein beta chain" FT /evidence="ECO:0000305" FT /id="PRO_0000016703" FT TOPO_DOM 747..921 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 922..943 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 944..1297 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 483..603 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 607..707 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 818..913 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 979..1254 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 666..687 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 732..758 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1267..1297 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1275..1289 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1115 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 985..993 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 1013 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 1145 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000305" FT MOD_RES 1146 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000305" FT CARBOHYD 47 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 411 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 492 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 616 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 634 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 756 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 885 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 898 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 214..222 FT /evidence="ECO:0000250" FT DISULFID 216..228 FT /evidence="ECO:0000250" FT DISULFID 229..237 FT /evidence="ECO:0000250" FT DISULFID 233..246 FT /evidence="ECO:0000250" FT DISULFID 249..258 FT /evidence="ECO:0000250" FT DISULFID 262..274 FT /evidence="ECO:0000250" FT DISULFID 280..300 FT /evidence="ECO:0000250" FT DISULFID 304..317 FT /evidence="ECO:0000250" FT DISULFID 320..324 FT /evidence="ECO:0000250" FT DISULFID 657..864 FT /note="Interchain (between alpha and beta chains)" FT /evidence="ECO:0000255" FT VARIANT 127 FT /note="A -> E (in dbSNP:rs55757706)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041434" FT VARIANT 161 FT /note="A -> V (in dbSNP:rs55971900)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041435" FT VARIANT 244 FT /note="R -> H (in dbSNP:rs55951840)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041436" FT VARIANT 246 FT /note="C -> R (in dbSNP:rs56377825)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041437" FT VARIANT 278 FT /note="E -> Q (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041438" FT VARIANT 554 FT /note="R -> C (in dbSNP:rs56068937)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041439" FT VARIANT 928 FT /note="P -> L (in dbSNP:rs56252149)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041440" FT VARIANT 1065 FT /note="G -> E (in a glioblastoma multiforme sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041441" FT MUTAGEN 1145..1146 FT /note="YY->FF: Abolishes autophosphorylation." FT /evidence="ECO:0000269|PubMed:21641549" FT STRAND 31..37 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 40..45 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 51..60 FT /evidence="ECO:0007829|PDB:7TYJ" FT TURN 65..70 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:7TYJ" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:7TYJ" FT TURN 173..175 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 193..198 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:7TYK" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 247..253 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:7TYJ" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 277..282 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 311..315 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 327..335 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 338..341 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 349..356 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 365..371 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 382..386 FT /evidence="ECO:0007829|PDB:7TYJ" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 412..417 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 430..432 FT /evidence="ECO:0007829|PDB:7TYK" FT STRAND 437..444 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 450..460 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:7TYM" FT TURN 468..470 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 473..476 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 489..494 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 496..503 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 509..512 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 516..523 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 547..549 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 552..556 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 560..564 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 570..577 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 596..599 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 609..617 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 620..626 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 637..645 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 649..651 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 657..659 FT /evidence="ECO:0007829|PDB:7TYM" FT HELIX 704..718 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 763..776 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 782..792 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 794..797 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 805..808 FT /evidence="ECO:0007829|PDB:7TYJ" FT TURN 813..816 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 823..827 FT /evidence="ECO:0007829|PDB:7TYM" FT TURN 828..830 FT /evidence="ECO:0007829|PDB:7TYM" FT STRAND 832..835 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 846..858 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 861..866 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 867..873 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 874..878 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 883..896 FT /evidence="ECO:0007829|PDB:7TYJ" FT STRAND 905..909 FT /evidence="ECO:0007829|PDB:7TYJ" FT HELIX 920..926 FT /evidence="ECO:0007829|PDB:7PL4" FT HELIX 928..946 FT /evidence="ECO:0007829|PDB:7PL4" SQ SEQUENCE 1297 AA; 143720 MW; BB22C7FF61E3065D CRC64; MAVPSLWPWG ACLPVIFLSL GFGLDTVEVC PSLDIRSEVA ELRQLENCSV VEGHLQILLM FTATGEDFRG LSFPRLTQVT DYLLLFRVYG LESLRDLFPN LAVIRGTRLF LGYALVIFEM PHLRDVALPA LGAVLRGAVR VEKNQELCHL STIDWGLLQP APGANHIVGN KLGEECADVC PGVLGAAGEP CAKTTFSGHT DYRCWTSSHC QRVCPCPHGM ACTARGECCH TECLGGCSQP EDPRACVACR HLYFQGACLW ACPPGTYQYE SWRCVTAERC ASLHSVPGRA STFGIHQGSC LAQCPSGFTR NSSSIFCHKC EGLCPKECKV GTKTIDSIQA AQDLVGCTHV EGSLILNLRQ GYNLEPQLQH SLGLVETITG FLKIKHSFAL VSLGFFKNLK LIRGDAMVDG NYTLYVLDNQ NLQQLGSWVA AGLTIPVGKI YFAFNPRLCL EHIYRLEEVT GTRGRQNKAE INPRTNGDRA ACQTRTLRFV SNVTEADRIL LRWERYEPLE ARDLLSFIVY YKESPFQNAT EHVGPDACGT QSWNLLDVEL PLSRTQEPGV TLASLKPWTQ YAVFVRAITL TTEEDSPHQG AQSPIVYLRT LPAAPTVPQD VISTSNSSSH LLVRWKPPTQ RNGNLTYYLV LWQRLAEDGD LYLNDYCHRG LRLPTSNNDP RFDGEDGDPE AEMESDCCPC QHPPPGQVLP PLEAQEASFQ KKFENFLHNA ITIPISPWKV TSINKSPQRD SGRHRRAAGP LRLGGNSSDF EIQEDKVPRE RAVLSGLRHF TEYRIDIHAC NHAAHTVGCS AATFVFARTM PHREADGIPG KVAWEASSKN SVLLRWLEPP DPNGLILKYE IKYRRLGEEA TVLCVSRLRY AKFGGVHLAL LPPGNYSARV RATSLAGNGS WTDSVAFYIL GPEEEDAGGL HVLLTATPVG LTLLIVLAAL GFFYGKKRNR TLYASVNPEY FSASDMYVPD EWEVPREQIS IIRELGQGSF GMVYEGLARG LEAGEESTPV ALKTVNELAS PRECIEFLKE ASVMKAFKCH HVVRLLGVVS QGQPTLVIME LMTRGDLKSH LRSLRPEAEN NPGLPQPALG EMIQMAGEIA DGMAYLAANK FVHRDLAARN CMVSQDFTVK IGDFGMTRDV YETDYYRKGG KGLLPVRWMA PESLKDGIFT THSDVWSFGV VLWEIVTLAE QPYQGLSNEQ VLKFVMDGGV LEELEGCPLQ LQELMSRCWQ PNPRLRPSFT HILDSIQEEL RPSFRLLSFY YSPECRGARG SLPTTDAEPD SSPTPRDCSP QNGGPGH //