ID SPEG_HUMAN Reviewed; 3267 AA. AC Q15772; A8K0G6; A8MRU0; Q27J74; Q695L1; Q6FGA6; Q6ZQW1; Q6ZTL8; Q9P2P9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 4. DT 27-MAR-2024, entry version 202. DE RecName: Full=Striated muscle preferentially expressed protein kinase; DE EC=2.7.11.1; DE AltName: Full=Aortic preferentially expressed protein 1; DE Short=APEG-1; GN Name=SPEG; Synonyms=APEG1, KIAA1297; 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] (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, AND INDUCTION. RX PubMed=8663449; DOI=10.1074/jbc.271.29.17354; RA Hsieh C.-M., Yoshizumi M., Endege W.O., Kho C.-J., Jain M.K., Kashiki S., RA de Los Santos R., Lee W.-S., Perrella M.A., Lee M.-E.; RT "APEG-1, a novel gene preferentially expressed in aortic smooth muscle RT cells, is down-regulated by vascular injury."; RL J. Biol. Chem. 271:17354-17359(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-129 (ISOFORM 1), AND ALTERNATIVE PROMOTER RP USAGE. RX PubMed=16545539; DOI=10.1016/j.ygeno.2006.01.009; RA Tam J.L.Y., Triantaphyllopoulos K., Todd H., Raguz S., de Wit T., RA Morgan J.E., Partridge T.A., Makrinou E., Grosveld F., Antoniou M.; RT "The human desmin locus: gene organization and LCR-mediated transcriptional RT control."; RL Genomics 87:733-746(2006). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-3267 (ISOFORM 1), TISSUE SPECIFICITY, AND RP VARIANT THR-2687. RX PubMed=15185077; DOI=10.1007/s00427-004-0413-5; RA Sutter S.B., Raeker M.O., Borisov A.B., Russell M.W.; RT "Orthologous relationship of obscurin and Unc-89: phylogeny of a novel RT family of tandem myosin light chain kinases."; RL Dev. Genes Evol. 214:352-359(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 982-3267 (ISOFORM 1), AND VARIANT RP THR-2687. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY RP 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 X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) OF 864-962, AND SUBUNIT. RX PubMed=16354304; DOI=10.1186/1472-6807-5-21; RA Manjasetty B.A., Niesen F.H., Scheich C., Roske Y., Goetz F., Behlke J., RA Sievert V., Heinemann U., Bussow K.; RT "X-ray structure of engineered human aortic preferentially expressed RT protein-1 (APEG-1)."; RL BMC Struct. Biol. 5:21-21(2005). RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] HIS-206; CYS-934; GLN-966; LEU-1103; RP VAL-1135; ASP-1178; TRP-1234; GLN-1340; CYS-1621; TRP-1903; THR-2687; RP MET-2742 AND ARG-3079. 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 [13] RP INTERACTION WITH MTM1, INVOLVEMENT IN CNM5, AND VARIANT CNM5 VAL-2757. RX PubMed=25087613; DOI=10.1016/j.ajhg.2014.07.004; RA Agrawal P.B., Pierson C.R., Joshi M., Liu X., Ravenscroft G., RA Moghadaszadeh B., Talabere T., Viola M., Swanson L.C., Haliloglu G., RA Talim B., Yau K.S., Allcock R.J., Laing N.G., Perrella M.A., Beggs A.H.; RT "SPEG interacts with myotubularin, and its deficiency causes centronuclear RT myopathy with dilated cardiomyopathy."; RL Am. J. Hum. Genet. 95:218-226(2014). CC -!- FUNCTION: Isoform 3 may have a role in regulating the growth and CC differentiation of arterial smooth muscle cells. 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 -!- 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; CC -!- SUBUNIT: Interacts with MTM1. Isoform 3 is found as a monomer or CC homodimer. {ECO:0000269|PubMed:16354304, ECO:0000269|PubMed:25087613}. CC -!- INTERACTION: CC Q15772; Q99873: PRMT1; NbExp=3; IntAct=EBI-1384196, EBI-78738; CC Q15772-4; O75031: HSF2BP; NbExp=3; IntAct=EBI-12175897, EBI-7116203; CC Q15772-4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12175897, EBI-16439278; CC Q15772-4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12175897, EBI-79165; CC Q15772-4; Q99873-3: PRMT1; NbExp=3; IntAct=EBI-12175897, EBI-17165527; CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4; CC Name=4; CC IsoId=Q15772-5; Sequence=Displayed; CC Name=2; CC IsoId=Q15772-3; Sequence=VSP_018259, VSP_018261, VSP_018262; CC Name=3; Synonyms=APEG1; CC IsoId=Q15772-4; Sequence=VSP_018258, VSP_018261, VSP_018262; CC Name=1; Synonyms=SPEG; CC IsoId=Q15772-1; Sequence=VSP_036071; CC -!- TISSUE SPECIFICITY: Isoform 1 is preferentially expressed in striated CC muscle. Non-kinase form such as isoform 3 is predominantly expressed in CC the aorta. Isoform 3 appears to be expressed only in highly CC differentiated ASMC in normal vessel walls and down-regulated in CC dedifferentiated ASMC in vivo. In response to vascular injuries ASMC CC dedifferentiate and change from a quiescent and contractile phenotype CC to a proliferative and synthetic phenotype. This proliferation of CC vascular smooth muscle cells is one of the most prominent features of CC atherosclerosis. {ECO:0000269|PubMed:15185077, CC ECO:0000269|PubMed:8663449}. CC -!- INDUCTION: Isoform 3 is quickly down-regulated in response to vascular CC injury, when ASMC cells change from a quiescent to a proliferative CC phenotype. {ECO:0000269|PubMed:8663449}. CC -!- PTM: May be autophosphorylated. CC -!- DISEASE: Myopathy, centronuclear, 5 (CNM5) [MIM:615959]: A form of CC centronuclear myopathy, a congenital muscle disorder characterized by CC progressive muscular weakness and wasting involving mainly limb girdle, CC trunk, and neck muscles. It may also affect distal muscles. Weakness CC may be present during childhood or adolescence or may not become CC evident until the third decade of life. Ptosis is a frequent clinical CC feature. The most prominent histopathologic features include high CC frequency of centrally located nuclei in muscle fibers not secondary to CC regeneration, radial arrangement of sarcoplasmic strands around the CC central nuclei, and predominance and hypotrophy of type 1 fibers. CNM5 CC features include severe neonatal hypotonia with respiratory CC insufficiency, difficulty feeding, and delayed motor development. Some CC patients die in infancy, and some develop dilated cardiomyopathy. CC {ECO:0000269|PubMed:25087613}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Expression is under the tight control of the locus CC control region (LCRs). CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAY15052.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=ABD61734.1; 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; U57099; AAC50599.1; -; mRNA. DR EMBL; AK126500; BAC86568.1; -; mRNA. DR EMBL; AK289531; BAF82220.1; -; mRNA. DR EMBL; CR542201; CAG46998.1; -; mRNA. DR EMBL; AC053503; AAY15052.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471063; EAW70747.1; -; Genomic_DNA. DR EMBL; BC006346; AAH06346.1; -; mRNA. DR EMBL; DQ395348; ABD61734.1; ALT_FRAME; mRNA. DR EMBL; AY603755; AAT80901.1; -; mRNA. DR EMBL; AB037718; BAA92535.1; -; mRNA. DR CCDS; CCDS42824.1; -. [Q15772-5] DR CCDS; CCDS54432.1; -. [Q15772-4] DR RefSeq; NP_001166947.1; NM_001173476.1. [Q15772-4] DR RefSeq; NP_005867.3; NM_005876.4. [Q15772-5] DR RefSeq; XP_016858651.1; XM_017003162.1. DR PDB; 1U2H; X-ray; 0.96 A; A=864-960. DR PDBsum; 1U2H; -. DR SMR; Q15772; -. DR BioGRID; 115579; 17. DR IntAct; Q15772; 5. DR STRING; 9606.ENSP00000311684; -. DR GlyCosmos; Q15772; 1 site, 1 glycan. DR GlyGen; Q15772; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15772; -. DR PhosphoSitePlus; Q15772; -. DR BioMuta; SPEG; -. DR DMDM; 218512143; -. DR EPD; Q15772; -. DR jPOST; Q15772; -. DR MassIVE; Q15772; -. DR MaxQB; Q15772; -. DR PaxDb; 9606-ENSP00000311684; -. DR PeptideAtlas; Q15772; -. DR ProteomicsDB; 60751; -. [Q15772-5] DR ProteomicsDB; 60752; -. [Q15772-1] DR ProteomicsDB; 60753; -. [Q15772-3] DR ProteomicsDB; 60754; -. [Q15772-4] DR Pumba; Q15772; -. DR Antibodypedia; 11575; 83 antibodies from 23 providers. DR DNASU; 10290; -. DR Ensembl; ENST00000312358.12; ENSP00000311684.7; ENSG00000072195.15. [Q15772-5] DR Ensembl; ENST00000396686.5; ENSP00000379917.1; ENSG00000072195.15. [Q15772-4] DR Ensembl; ENST00000396688.5; ENSP00000379919.1; ENSG00000072195.15. [Q15772-4] DR Ensembl; ENST00000396689.2; ENSP00000379920.2; ENSG00000072195.15. [Q15772-4] DR GeneID; 10290; -. DR KEGG; hsa:10290; -. DR MANE-Select; ENST00000312358.12; ENSP00000311684.7; NM_005876.5; NP_005867.3. DR UCSC; uc002vlq.4; human. [Q15772-5] DR AGR; HGNC:16901; -. DR CTD; 10290; -. DR DisGeNET; 10290; -. DR GeneCards; SPEG; -. DR HGNC; HGNC:16901; SPEG. DR HPA; ENSG00000072195; Tissue enhanced (intestine). DR MalaCards; SPEG; -. DR MIM; 615950; gene. DR MIM; 615959; phenotype. DR neXtProt; NX_Q15772; -. DR OpenTargets; ENSG00000072195; -. DR Orphanet; 169186; Autosomal recessive centronuclear myopathy. DR PharmGKB; PA142672598; -. DR VEuPathDB; HostDB:ENSG00000072195; -. DR eggNOG; KOG0032; Eukaryota. DR eggNOG; KOG0613; Eukaryota. DR GeneTree; ENSGT00940000161126; -. DR HOGENOM; CLU_000381_0_0_1; -. DR InParanoid; Q15772; -. DR OrthoDB; 4215065at2759; -. DR PhylomeDB; Q15772; -. DR TreeFam; TF331962; -. DR PathwayCommons; Q15772; -. DR SignaLink; Q15772; -. DR BioGRID-ORCS; 10290; 9 hits in 1166 CRISPR screens. DR ChiTaRS; SPEG; human. DR EvolutionaryTrace; Q15772; -. DR GeneWiki; SPEG; -. DR GenomeRNAi; 10290; -. DR Pharos; Q15772; Tbio. DR PRO; PR:Q15772; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q15772; Protein. DR Bgee; ENSG00000072195; Expressed in popliteal artery and 171 other cell types or tissues. DR ExpressionAtlas; Q15772; baseline and differential. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central. 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:0042692; P:muscle cell differentiation; IBA:GO_Central. DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00063; FN3; 2. DR CDD; cd20975; IgI_APEG-1_like; 1. DR CDD; cd14108; STKc_SPEG_rpt1; 1. DR CDD; cd14111; STKc_SPEG_rpt2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 11. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. 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; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1. DR Pfam; PF07679; I-set; 9. DR Pfam; PF00069; Pkinase; 2. DR Pfam; PF16650; SPEG_u2; 1. DR SMART; SM00060; FN3; 2. DR SMART; SM00409; IG; 9. DR SMART; SM00408; IGc2; 9. DR SMART; SM00220; S_TKc; 2. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 9. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS50835; IG_LIKE; 8. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2. DR Genevisible; Q15772; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative promoter usage; Alternative splicing; KW ATP-binding; Differentiation; Disease variant; Disulfide bond; KW Immunoglobulin domain; Kinase; Methylation; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..3267 FT /note="Striated muscle preferentially expressed protein FT kinase" FT /id="PRO_0000072666" FT DOMAIN 43..124 FT /note="Ig-like 1" FT DOMAIN 722..810 FT /note="Ig-like 2" FT DOMAIN 869..958 FT /note="Ig-like 3" FT DOMAIN 963..1057 FT /note="Ig-like 4" FT DOMAIN 1064..1152 FT /note="Ig-like 5" FT DOMAIN 1188..1278 FT /note="Ig-like 6" FT DOMAIN 1285..1382 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1384..1480 FT /note="Ig-like 7" FT DOMAIN 1485..1573 FT /note="Ig-like 8" FT DOMAIN 1601..1854 FT /note="Protein kinase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 2583..2673 FT /note="Ig-like 9" FT DOMAIN 2680..2774 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 2966..3218 FT /note="Protein kinase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 132..227 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 276..714 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 812..872 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1157..1180 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1906..2060 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2074..2239 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2253..2325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2339..2399 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2411..2452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2466..2564 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2771..2896 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2909..2966 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 157..199 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 295..331 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 340..359 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 361..381 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 402..418 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..487 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 495..516 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 538..556 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 585..599 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 661..683 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 812..828 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 848..868 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2164..2178 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2199..2237 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2353..2371 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2466..2481 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2512..2540 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2798..2828 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2882..2896 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2909..2927 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2928..2962 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1719 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 3085 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 1607..1615 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 1630 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 2972..2980 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 2995 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 364 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 371 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 375 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 378 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 381 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 449 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 453 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 506 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 526 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 549 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 1128 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 1172 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 1988 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2014 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2015 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2037 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2055 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2055 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2109 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2130 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2139 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2177 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2376 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2380 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2410 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2414 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2438 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2439 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2444 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2448 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2521 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2524 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2559 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2771 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT MOD_RES 2774 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63638" FT MOD_RES 2949 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62407" FT DISULFID 989..1041 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 2605..2657 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..849 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8663449, ECO:0000303|Ref.3" FT /id="VSP_018258" FT VAR_SEQ 1..792 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_018259" FT VAR_SEQ 961..962 FT /note="AH -> GE (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8663449, FT ECO:0000303|Ref.3" FT /id="VSP_018261" FT VAR_SEQ 963..3267 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8663449, FT ECO:0000303|Ref.3" FT /id="VSP_018262" FT VAR_SEQ 3209..3267 FT /note="LQDCLAHPWLQDAYLMKLRRQTLTFTTNRLKEFLGEQRRRRAEAATRHKVLL FT RSYPGGP -> SCLSVCHKEIKMASS (in isoform 1)" FT /evidence="ECO:0000303|PubMed:10718198, FT ECO:0000303|PubMed:15185077, ECO:0000303|PubMed:16545539" FT /id="VSP_036071" FT VARIANT 206 FT /note="R -> H (in dbSNP:rs55821435)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041101" FT VARIANT 934 FT /note="R -> C (in dbSNP:rs34398769)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041102" FT VARIANT 966 FT /note="R -> Q (in dbSNP:rs34861443)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041103" FT VARIANT 1103 FT /note="P -> L (in dbSNP:rs56334571)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041104" FT VARIANT 1135 FT /note="A -> V (in dbSNP:rs55670811)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041105" FT VARIANT 1178 FT /note="E -> D (in a gastric adenocarcinoma sample; somatic FT mutation; dbSNP:rs757589345)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041106" FT VARIANT 1234 FT /note="R -> W (in dbSNP:rs55916864)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041107" FT VARIANT 1340 FT /note="R -> Q (in dbSNP:rs34994343)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041108" FT VARIANT 1621 FT /note="R -> C (in dbSNP:rs55646900)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041109" FT VARIANT 1903 FT /note="R -> W (in an ovarian mucinous carcinoma sample; FT somatic mutation; dbSNP:rs762000831)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041110" FT VARIANT 2189 FT /note="P -> L (in dbSNP:rs10755037)" FT /id="VAR_059769" FT VARIANT 2687 FT /note="P -> T (in dbSNP:rs13026308)" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:15185077, ECO:0000269|PubMed:17344846" FT /id="VAR_041111" FT VARIANT 2742 FT /note="V -> M (in a gastric adenocarcinoma sample; somatic FT mutation; dbSNP:rs566841339)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041112" FT VARIANT 2757 FT /note="G -> V (in CNM5; dbSNP:rs587777676)" FT /evidence="ECO:0000269|PubMed:25087613" FT /id="VAR_071808" FT VARIANT 3079 FT /note="H -> R (in dbSNP:rs12464085)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041113" FT CONFLICT 71 FT /note="Q -> H (in Ref. 7; ABD61734)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="S -> I (in Ref. 7; ABD61734)" FT /evidence="ECO:0000305" FT CONFLICT 2047 FT /note="S -> G (in Ref. 8; AAT80901 and 9; BAA92535)" FT /evidence="ECO:0000305" FT CONFLICT 3005 FT /note="R -> P (in Ref. 8; AAT80901 and 9; BAA92535)" FT /evidence="ECO:0000305" FT STRAND 867..873 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 878..881 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 886..896 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 899..904 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 915..919 FT /evidence="ECO:0007829|PDB:1U2H" FT HELIX 921..923 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 924..931 FT /evidence="ECO:0007829|PDB:1U2H" FT HELIX 934..936 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 938..946 FT /evidence="ECO:0007829|PDB:1U2H" FT STRAND 949..960 FT /evidence="ECO:0007829|PDB:1U2H" SQ SEQUENCE 3267 AA; 354289 MW; E67BEB5624144233 CRC64; MQKARGTRGE DAGTRAPPSP GVPPKRAKVG AGGGAPVAVA GAPVFLRPLK NAAVCAGSDV RLRVVVSGTP QPSLRWFRDG QLLPAPAPEP SCLWLRRCGA QDAGVYSCMA QNERGRASCE AVLTVLEVGD SETAEDDISD VQGTQRLELR DDGAFSTPTG GSDTLVGTSL DTPPTSVTGT SEEQVSWWGS GQTVLEQEAG SGGGTRRLPG SPRQAQATGA GPRHLGVEPL VRASRANLVG ASWGSEDSLS VASDLYGSAF SLYRGRALSI HVSVPQSGLR REEPDLQPQL ASEAPRRPAQ PPPSKSALLP PPSPRVGKRS PPGPPAQPAA TPTSPHRRTQ EPVLPEDTTT EEKRGKKSKS SGPSLAGTAE SRPQTPLSEA SGRLSALGRS PRLVRAGSRI LDKLQFFEER RRSLERSDSP PAPLRPWVPL RKARSLEQPK SERGAPWGTP GASQEELRAP GSVAERRRLF QQKAASLDER TRQRSPASDL ELRFAQELGR IRRSTSREEL VRSHESLRAT LQRAPSPREP GEPPLFSRPS TPKTSRAVSP AAAQPPSPSS AEKPGDEPGR PRSRGPAGRT EPGEGPQQEV RRRDQFPLTR SRAIQECRSP VPPPAADPPE ARTKAPPGRK REPPAQAVRF LPWATPGLEG AAVPQTLEKN RAGPEAEKRL RRGPEEDGPW GPWDRRGARS QGKGRRARPT SPELESSDDS YVSAGEEPLE APVFEIPLQN VVVAPGADVL LKCIITANPP PQVSWHKDGS ALRSEGRLLL RAEGERHTLL LREARAADAG SYMATATNEL GQATCAASLT VRPGGSTSPF SSPITSDEEY LSPPEEFPEP GETWPRTPTM KPSPSQNRRS SDTGSKAPPT FKVSLMDQSV REGQDVIMSI RVQGEPKPVV SWLRNRQPVR PDQRRFAEEA EGGLCRLRIL AAERGDAGFY TCKAVNEYGA RQCEARLEVR AHPESRSLAV LAPLQDVDVG AGEMALFECL VAGPTDVEVD WLCRGRLLQP ALLKCKMHFD GRKCKLLLTS VHEDDSGVYT CKLSTAKDEL TCSARLTVRP SLAPLFTRLL EDVEVLEGRA ARFDCKISGT PPPVVTWTHF GCPMEESENL RLRQDGGLHS LHIAHVGSED EGLYAVSAVN THGQAHCSAQ LYVEEPRTAA SGPSSKLEKM PSIPEEPEQG ELERLSIPDF LRPLQDLEVG LAKEAMLECQ VTGLPYPTIS WFHNGHRIQS SDDRRMTQYR DVHRLVFPAV GPQHAGVYKS VIANKLGKAA CYAHLYVTDV VPGPPDGAPQ VVAVTGRMVT LTWNPPRSLD MAIDPDSLTY TVQHQVLGSD QWTALVTGLR EPGWAATGLR KGVQHIFRVL STTVKSSSKP SPPSEPVQLL EHGPTLEEAP AMLDKPDIVY VVEGQPASVT VTFNHVEAQV VWRSCRGALL EARAGVYELS QPDDDQYCLR ICRVSRRDMG ALTCTARNRH GTQTCSVTLE LAEAPRFESI MEDVEVGAGE TARFAVVVEG KPLPDIMWYK DEVLLTESSH VSFVYEENEC SLVVLSTGAQ DGGVYTCTAQ NLAGEVSCKA ELAVHSAQTA MEVEGVGEDE DHRGRRLSDF YDIHQEIGRG AFSYLRRIVE RSSGLEFAAK FIPSQAKPKA SARREARLLA RLQHDCVLYF HEAFERRRGL VIVTELCTEE LLERIARKPT VCESEIRAYM RQVLEGIHYL HQSHVLHLDV KPENLLVWDG AAGEQQVRIC DFGNAQELTP GEPQYCQYGT PEFVAPEIVN QSPVSGVTDI WPVGVVAFLC LTGISPFVGE NDRTTLMNIR NYNVAFEETT FLSLSREARG FLIKVLVQDR LRPTAEETLE HPWFKTQAKG AEVSTDHLKL FLSRRRWQRS QISYKCHLVL RPIPELLRAP PERVWVTMPR RPPPSGGLSS SSDSEEEELE ELPSVPRPLQ PEFSGSRVSL TDIPTEDEAL GTPETGAATP MDWQEQGRAP SQDQEAPSPE ALPSPGQEPA AGASPRRGEL RRGSSAESAL PRAGPRELGR GLHKAASVEL PQRRSPSPGA TRLARGGLGE GEYAQRLQAL RQRLLRGGPE DGKVSGLRGP LLESLGGRAR DPRMARAASS EAAPHHQPPL ENRGLQKSSS FSQGEAEPRG RHRRAGAPLE IPVARLGARR LQESPSLSAL SEAQPSSPAR PSAPKPSTPK SAEPSATTPS DAPQPPAPQP AQDKAPEPRP EPVRASKPAP PPQALQTLAL PLTPYAQIIQ SLQLSGHAQG PSQGPAAPPS EPKPHAAVFA RVASPPPGAP EKRVPSAGGP PVLAEKARVP TVPPRPGSSL SSSIENLESE AVFEAKFKRS RESPLSLGLR LLSRSRSEER GPFRGAEEED GIYRPSPAGT PLELVRRPER SRSVQDLRAV GEPGLVRRLS LSLSQRLRRT PPAQRHPAWE ARGGDGESSE GGSSARGSPV LAMRRRLSFT LERLSSRLQR SGSSEDSGGA SGRSTPLFGR LRRATSEGES LRRLGLPHNQ LAAQAGATTP SAESLGSEAS ATSGSSAPGE SRSRLRWGFS RPRKDKGLSP PNLSASVQEE LGHQYVRSES DFPPVFHIKL KDQVLLEGEA ATLLCLPAAC PAPHISWMKD KKSLRSEPSV IIVSCKDGRQ LLSIPRAGKR HAGLYECSAT NVLGSITSSC TVAVARVPGK LAPPEVPQTY QDTALVLWKP GDSRAPCTYT LERRVDGESV WHPVSSGIPD CYYNVTHLPV GVTVRFRVAC ANRAGQGPFS NSSEKVFVRG TQDSSAVPSA AHQEAPVTSR PARARPPDSP TSLAPPLAPA APTPPSVTVS PSSPPTPPSQ ALSSLKAVGP PPQTPPRRHR GLQAARPAEP TLPSTHVTPS EPKPFVLDTG TPIPASTPQG VKPVSSSTPV YVVTSFVSAP PAPEPPAPEP PPEPTKVTVQ SLSPAKEVVS SPGSSPRSSP RPEGTTLRQG PPQKPYTFLE EKARGRFGVV RACRENATGR TFVAKIVPYA AEGKRRVLQE YEVLRTLHHE RIMSLHEAYI TPRYLVLIAE SCGNRELLCG LSDRFRYSED DVATYMVQLL QGLDYLHGHH VLHLDIKPDN LLLAPDNALK IVDFGSAQPY NPQALRPLGH RTGTLEFMAP EMVKGEPIGS ATDIWGAGVL TYIMLSGRSP FYEPDPQETE ARIVGGRFDA FQLYPNTSQS ATLFLRKVLS VHPWSRPSLQ DCLAHPWLQD AYLMKLRRQT LTFTTNRLKE FLGEQRRRRA EAATRHKVLL RSYPGGP //