ID SPEG_RAT Reviewed; 3259 AA.
AC Q63638;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Striated muscle-specific serine/threonine-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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-368; SER-375;
RP THR-379; SER-385; SER-423; THR-453; SER-457; SER-463; SER-493; SER-511;
RP SER-554; SER-1177; SER-2004; SER-2019; SER-2020; SER-2042; SER-2114;
RP SER-2135; SER-2182; SER-2207; SER-2410; SER-2414; SER-2438; SER-2439;
RP SER-2448; SER-2559 AND SER-2774, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Isoform 2 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q15772}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SPEG;
CC IsoId=Q63638-1; Sequence=Displayed;
CC Name=2; Synonyms=APEG1;
CC IsoId=Q63638-2; Sequence=VSP_018269, VSP_018270, VSP_018271;
CC -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in differentiated
CC arterial smooth muscle cells (ASMC) in the medial layer of the aorta.
CC Weakly detected in brain and testis and to a lesser extent in organs
CC rich in striated muscle or visceral smooth muscle.
CC -!- PTM: May be autophosphorylated.
CC -!- MISCELLANEOUS: Expression is under the tight control of the locus
CC control region (LCRs).
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AABR03067996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U57097; AAC52667.1; -; mRNA.
DR RefSeq; NP_001102272.1; NM_001108802.1. [Q63638-1]
DR RefSeq; NP_037037.1; NM_012905.2. [Q63638-2]
DR IntAct; Q63638; 1.
DR STRING; 10116.ENSRNOP00000026941; -.
DR CarbonylDB; Q63638; -.
DR iPTMnet; Q63638; -.
DR PhosphoSitePlus; Q63638; -.
DR PaxDb; 10116-ENSRNOP00000026941; -.
DR Ensembl; ENSRNOT00000026941.8; ENSRNOP00000026941.4; ENSRNOG00000019850.9. [Q63638-1]
DR Ensembl; ENSRNOT00000098450.1; ENSRNOP00000084140.1; ENSRNOG00000019850.9. [Q63638-2]
DR GeneID; 363256; -.
DR KEGG; rno:363256; -.
DR UCSC; RGD:2124; rat. [Q63638-1]
DR AGR; RGD:2124; -.
DR CTD; 10290; -.
DR RGD; 2124; Speg.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000161126; -.
DR HOGENOM; CLU_000381_0_0_1; -.
DR InParanoid; Q63638; -.
DR OrthoDB; 4215065at2759; -.
DR PhylomeDB; Q63638; -.
DR TreeFam; TF331962; -.
DR PRO; PR:Q63638; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019850; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR Genevisible; Q63638; RN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0072359; P:circulatory system development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0042692; P:muscle cell differentiation; IEP:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060541; P:respiratory system development; ISO:RGD.
DR CDD; cd00063; FN3; 2.
DR CDD; cd20975; IgI_APEG-1_like; 1.
DR CDD; cd14108; STKc_SPEG_rpt1; 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; 8.
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; 8.
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; 3.
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 Alternative promoter usage; Alternative splicing; ATP-binding;
KW Differentiation; Disulfide bond; Immunoglobulin domain; Kinase;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..3259
FT /note="Striated muscle-specific serine/threonine-protein
FT kinase"
FT /id="PRO_0000072668"
FT DOMAIN 45..126
FT /note="Ig-like 1"
FT DOMAIN 727..817
FT /note="Ig-like 2"
FT DOMAIN 874..963
FT /note="Ig-like 3"
FT DOMAIN 968..1056
FT /note="Ig-like 4"
FT DOMAIN 1069..1157
FT /note="Ig-like 5"
FT DOMAIN 1193..1283
FT /note="Ig-like 6"
FT DOMAIN 1290..1387
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1490..1578
FT /note="Ig-like 7"
FT DOMAIN 1606..1859
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 2583..2673
FT /note="Ig-like 8"
FT DOMAIN 2680..2774
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2859..2965
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2958..3210
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..2244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2336..2451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2463..2562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2771..2829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2855..2957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2204..2232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2463..2481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2507..2540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2789..2807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2808..2829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2857..2905
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 2934..2954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1724
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 3077
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 1612..1620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2964..2972
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2987
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 33
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 2004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2060
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 2060
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 2114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 2182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 2414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 2448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 2771
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT MOD_RES 2774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62407"
FT DISULFID 994..1046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2605..2657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..854
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8663449"
FT /id="VSP_018269"
FT VAR_SEQ 966..967
FT /note="AH -> GE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8663449"
FT /id="VSP_018270"
FT VAR_SEQ 968..3259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8663449"
FT /id="VSP_018271"
SQ SEQUENCE 3259 AA; 354166 MW; 59915197FF5DADCC CRC64;
MQKARGTRGE DAGTRAPPSP GVPPKRAKVG AGRGVLVTGA GAGAPVFLRP LKNAAVCAGS
DVRLRVVVSG TPEPSLSWFR DGQLLPTPVP EPSCLWLRNC GAQDAGVYSC SAQNERGKAS
CEAVLTVLEV RDSETAEDDI SDVPGTQRLE LRDDRAFSTP TGGSDTLVGT SLDTPPTSVT
GTSEEQVSWW GSGQTVLEQE AGSGGGTRPL PGSPRQAQTT GAGPRHLGVE PLVRASRANL
VGASWGSEDS LSVASDLYGS AFSLYRGRAL SIHVSIPPSG LRREEPDLQP QPASDALRPR
PALPPPSKSA LLPPPSPRVG KRALPGSSAQ PPATPTSPHR CTQEPSLPED ITTTEEKRGK
KPKSSGPSLA GTVESRPQTP LSEASGRLSA LGRSPRLVRA GSRILDKLQF FEERRRSLER
SDSPPAPLRP WVPLRKARSL EQPKSEGGAA WDTPGASQEE LRSPRGSVAE RRRLFQQKAA
SLDERTRQRS ATSDLELRFA QELGRIRRST SREELVRSHE SLRATLQRAP SPREPGEPPL
FSRPSIPKTS RAVSPAATQP PPPSGAGKSG DETGRPRSRG PVGRTEPGEG PQQEIKRRDQ
FPLTRSRAIQ ECRSPVPPFT ADPPESRTKA PSARKREPPA QAVRFLPWAT PGVEDSVLPQ
TLEKNRAGPE AEKRLRRGPE EDGPWGAWDR RGTRSQGKGR RARPTSPELE SSDDSYVSAG
EEPLEAPVFE IPLQNMVVAP GADVLLKCII TANPPPQVSW KKDGSVLHSE GRLLIRAEGE
RHTLLLREAQ AADAGSYTAT ATNELGQASC ASSLAVRPGA STSPFSSPIT SDEEYLSPPE
EFPEPGETWS RTPTMKPSPS QDRDSSDSSS KAPPTFKVSL MDQSVREGQD VIMSIRVQGE
PKPVVSWLRN RQPVRPDQRR FAEEAEGGLC RLRILAAERG DAGFYTCKAV NEYGARQCEA
RLEVRAHPES RSLAVLAPLQ DVDVGAGEMA LFECLVAGPA DVEVDWLCRG RLLQPALLKC
KMHFDGRKCK LLLTSVHEDD SGVYTCKLST VKDELTCSAR LTVRPSLAPL FTRLLEDVEV
LEGRAARLDC KISGTPPPSV TWTHFGHPVN ESENLRLRQD GGLHSLHIAR VGSEDEGLYE
VSATNTHGQA HCSAQLYVEE PRTAASGPSS KLEKMPSIPE EPEHGDLERL SIPDFLRPLQ
DLEVGLAKEA MLECQVTGLP YPTISWFHNG HRIQSSDDRR MTQYRDIHRL VFPAVGPQHA
GVYKSVIANK LGKAACYAHL YVTDVVPGPP DGAPQVVAVT GRMVTLSWNP PRSLDMAIDP
DSLTYTVQHQ VLGSDQWTAL VTGLREPEWA ATGLKKGLHH IFRVLSSSGK SSSKPSAPSE
PVQLLEHGPP LEEAPAVLDK QDIVYVVEGQ PACVTVTFNH VEAQVVWRSC RGALLEPRTG
VYELSQPDDD QYCLRICRVS RRDLGPLTCS ARNRHGTKAC SITLELAEAP RFESIMEDVE
VGPGETARFA VVVEGKPLPD IMWYKDEVLL AESNHVSFVY EENECSLVVL SAGSQDGGVY
TCTARNLAGE VSCKAELSVH SAQTAMEVEG VGEDEEHRGR RLSDYYDIHQ EIGRGAFSYL
RRVVERSSGL EFAAKFIPSQ AKPKASARRE ARLLARLQHD CVLYFHEAFE RRRGLVIVTE
LCTEELLERM ARKPTVCESE TRTYMRQVLE GIGYLHQSHV LHLDVKPENL LVWDGAGGEE
QVRICDFGNA QELTPGEPQY CQFGTPEFVA PEIVNQSPVS GVTDIWPVGV VAFLCLTGIS
PFVGENDRTT LMNIRNYNVA FEETTFLSLS REARGFLIKV LVQDRLRPTA EETLEHPWFK
TEAKGAEVST DHLKLFLSRR RWQRSQISYK CHLVLRPIPE LLRAPPERVW VAMPRRQPPS
GGLSSSSDSE EEELEELPSV PRPLQPEFSG SRVSLTDIPT EDEALGTPEA GAATPMDWQE
QGRAPSKDQE APSPEALPSP GQESPDGPSP RRPELRRGSS AESALPRVGS REPGRSLHKA
ASVELPQRRS PSPGATRLTR GGLGEGEYAQ RLQALRQRLL RGGPEDGKVS GLRGPLLESL
GGRARDPRMA RAASSEAAPH HQPPPESRGL QKSSSFSQGE AEPRGRHRRA GAPLEIPVAR
LGARRLQESP SLSALSETQP PSPALPSAPK PSITKSPEPS AATSRDSPQP PAPQPVPEKI
PEPKPEPVRA AKPAQPPLAL QMPAQSLTPY AQIMQSLQLS SPTLSPQVPP SEPKPHAAVF
ARVASPPPGA SEKRVPSARI PPVLAEKVRV PTVPPRPGSS LSGSIENLES EAVFEAKFKR
SRESPLSRGL RLLSRSRSEE RGPFRGAEDD GIYRPSPAGT PLELVRRPER SRSVQDLRVA
GEPGLVRRLS LSLSQKLRRT PPGQRHPAWE SRSGDGESSE GGSSARGSPV LAVRRRLSST
LERLSSRLQR SGSSEDSGGA SGRSTPLFGR LRRATSEGES LRRLGVPHNQ LASQTGATTP
SAESLGSEAS GTSGSSAPGE SRSRHRWGLS RLRKDKGLSQ PNLSASVQED LGHQYVPSES
DFPPVFHIKL KDQVLLEGEA ATLLCLPAAC PTPRISWMKD KQSLRSEPSV VIVSCKDGRQ
LLSIPRASKR HAGLYECSAT NVLGSITSSC TVAVARTPGK LAPPEVPQTY CDTALVLWKP
GDSRAPCTYT LERRVDGESV WHPVSSGIPD CYYNVTQLPV GVTVRFRVAC SNRAGQGPFS
NPSEKVFIRG TQDSPAQSAA APRDAPVTSG PTRAPPPDSP TSLVPTPPLA PQVSQASTLS
PSTSSMSANQ ALSSLKAVGP PPATPPRKHR GLLATQQAEP SPPSILVTPS EHKSFVPDTG
TLTPTSSPQG VKPAPSSSSL YMVTSFVSAP PDPQPPAPEP PPEPTKVTVR SLSPAKEVVS
SPTPESTTLR QGPPQKPYTF LEEKARGRFG VVRSCRENAT GRTFVAKIVP YAAEGKRRVL
QEYEVLRTLH HERLMSLHEA YITPRYLVLI AESCGNRELL CGLSDRFRYS EDDVATYVVQ
LLQGLDYLHG RHVLHLDIKP DNLLLAADNA LKIVDFGSAQ PYNPQALKPL GHRTGTLEFM
APEMVRGDPI GSATDIWGAG VLTYIMLSGY SPFYEPDPQE TEARIVGGRF DAFQLYPNTS
QSATLFLRKV LSVHPWSRPS LQDCLAHPWL QDAYLMKLRR QTLTFTTNRL KEFLGEQRRR
RAEAATRHKV LLRSYPGSP
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