SPEG_HUMAN
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 03-AUG-2022, entry version 193.
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. [Q15772-3]
DR PDB; 1U2H; X-ray; 0.96 A; A=864-960.
DR PDBsum; 1U2H; -.
DR SMR; Q15772; -.
DR BioGRID; 115579; 14.
DR IntAct; Q15772; 7.
DR STRING; 9606.ENSP00000311684; -.
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; Q15772; -.
DR PeptideAtlas; Q15772; -.
DR PRIDE; Q15772; -.
DR ProteomicsDB; 60751; -. [Q15772-5]
DR ProteomicsDB; 60752; -. [Q15772-1]
DR ProteomicsDB; 60753; -. [Q15772-3]
DR ProteomicsDB; 60754; -. [Q15772-4]
DR Antibodypedia; 11575; 80 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 CTD; 10290; -.
DR DisGeNET; 10290; -.
DR GeneCards; SPEG; -.
DR HGNC; HGNC:16901; SPEG.
DR HPA; ENSG00000072195; Tissue enhanced (intestine, skeletal muscle).
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; 7796at2759; -.
DR PhylomeDB; Q15772; -.
DR TreeFam; TF331962; -.
DR PathwayCommons; Q15772; -.
DR SignaLink; Q15772; -.
DR BioGRID-ORCS; 10290; 7 hits in 1088 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 169 other tissues.
DR ExpressionAtlas; Q15772; baseline and differential.
DR Genevisible; Q15772; HS.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 11.
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; IPR015726; Ser/Thr_kin_striated-sp.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47633:SF3; PTHR47633:SF3; 3.
DR Pfam; PF07679; I-set; 9.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF48726; SSF48726; 9.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
