CSPG2_MOUSE
ID CSPG2_MOUSE Reviewed; 3357 AA.
AC Q62059; Q62058; Q9CUU0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 180.
DE RecName: Full=Versican core protein;
DE AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE Short=Chondroitin sulfate proteoglycan 2;
DE AltName: Full=Large fibroblast proteoglycan;
DE AltName: Full=PG-M;
DE Flags: Precursor;
GN Name=Vcan; Synonyms=Cspg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1 AND V2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J, and Swiss Webster; TISSUE=Brain, and Endothelial cell;
RX PubMed=7822336; DOI=10.1074/jbc.270.2.958;
RA Ito K., Shinomura T., Zako M., Ujita M., Kimata K.;
RT "Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan
RT generated by alternative splicing.";
RL J. Biol. Chem. 270:958-965(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
RC STRAIN=C57BL/6J; TISSUE=Endothelial cell;
RX PubMed=7876137; DOI=10.1074/jbc.270.8.3914;
RA Zako M., Shinomura T., Ujita M., Ito K., Kimata K.;
RT "Expression of PG-M(V3), an alternatively spliced form of PG-M without a
RT chondroitin sulfate attachment in region in mouse and human tissues.";
RL J. Biol. Chem. 270:3914-3918(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1691 (ISOFORM V1).
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PROTEIN SEQUENCE OF 277-288, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH FBLN1.
RX PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT versican.";
RL J. Biol. Chem. 274:20444-20449(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2585 AND SER-2586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP DEVELOPMENTAL STAGE, AND CLEAVAGE BY ADAMTS5.
RX PubMed=23233679; DOI=10.1074/jbc.m112.429647;
RA Stupka N., Kintakas C., White J.D., Fraser F.W., Hanciu M.,
RA Aramaki-Hattori N., Martin S., Coles C., Collier F., Ward A.C., Apte S.S.,
RA McCulloch D.R.;
RT "Versican processing by a disintegrin-like and metalloproteinase domain
RT with thrombospondin-1 repeats proteinases-5 and -15 facilitates myoblast
RT fusion.";
RL J. Biol. Chem. 288:1907-1917(2013).
RN [9]
RP CLEAVAGE BY ADAMTS15.
RX PubMed=24220035; DOI=10.1074/jbc.m112.418624;
RA Dancevic C.M., Fraser F.W., Smith A.D., Stupka N., Ward A.C.,
RA McCulloch D.R.;
RT "Biosynthesis and expression of a disintegrin-like and metalloproteinase
RT domain with thrombospondin-1 repeats-15: a novel versican-cleaving
RT proteoglycanase.";
RL J. Biol. Chem. 288:37267-37276(2013).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA Lako M.;
RT "Extracellular matrix component expression in human pluripotent stem cell-
RT derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT an important role for IMPG1 and CD44 in the development of photoreceptors
RT and interphotoreceptor matrix.";
RL Acta Biomater. 74:207-221(2018).
CC -!- FUNCTION: May play a role in intercellular signaling and in connecting
CC cells with the extracellular matrix. May take part in the regulation of
CC cell motility, growth and differentiation. Binds hyaluronic acid.
CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000269|PubMed:10400671}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:29777959}. Secreted,
CC extracellular space, extracellular matrix, interphotoreceptor matrix
CC {ECO:0000269|PubMed:29777959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=V0;
CC IsoId=Q62059-1; Sequence=Displayed;
CC Name=V1;
CC IsoId=Q62059-2; Sequence=VSP_003087, VSP_003088;
CC Name=V2;
CC IsoId=Q62059-3; Sequence=VSP_003089;
CC Name=V3;
CC IsoId=Q62059-4; Sequence=VSP_003087, VSP_003090;
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC (PubMed:29777959). Isoform V2: Only expressed in brain
CC (PubMed:7822336). {ECO:0000269|PubMed:29777959,
CC ECO:0000269|PubMed:7822336}.
CC -!- DEVELOPMENTAL STAGE: In embryonic skeletal muscle, significantly up-
CC regulated from 12.5 dpc to 15.5 dpc (PubMed:23233679). Decreased levels
CC in postnatal skeletal muscle (PubMed:23233679). In myoblasts,
CC dramatically up-regulated when myoblasts reach confluence and contact
CC inhibition, remaining high throughout the differentiation process
CC (PubMed:23233679). Disappears after the cartilage development.
CC {ECO:0000269|PubMed:23233679}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P13611}.
CC -!- PTM: Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
CC pericellular matrix surrounding myoblasts, facilitating myoblast
CC contact and fusion which is required for skeletal muscle development
CC and regeneration. {ECO:0000269|PubMed:23233679,
CC ECO:0000269|PubMed:24220035}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Versican;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_157";
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; D16263; BAA03796.1; -; mRNA.
DR EMBL; D28599; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; D32040; BAA06802.1; -; mRNA.
DR EMBL; AK014525; BAB29411.3; -; mRNA.
DR PIR; A55535; A55535.
DR SMR; Q62059; -.
DR IntAct; Q62059; 2.
DR MINT; Q62059; -.
DR STRING; 10090.ENSMUSP00000105173; -.
DR GlyConnect; 2818; 2 N-Linked glycans (1 site).
DR GlyGen; Q62059; 17 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q62059; -.
DR PhosphoSitePlus; Q62059; -.
DR jPOST; Q62059; -.
DR MaxQB; Q62059; -.
DR PaxDb; Q62059; -.
DR PeptideAtlas; Q62059; -.
DR PRIDE; Q62059; -.
DR ProteomicsDB; 284036; -. [Q62059-1]
DR ProteomicsDB; 284037; -. [Q62059-2]
DR ProteomicsDB; 284038; -. [Q62059-3]
DR ProteomicsDB; 284039; -. [Q62059-4]
DR ABCD; Q62059; 2 sequenced antibodies.
DR MGI; MGI:102889; Vcan.
DR eggNOG; ENOG502QRBE; Eukaryota.
DR InParanoid; Q62059; -.
DR PhylomeDB; Q62059; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR ChiTaRS; Vcan; mouse.
DR PRO; PR:Q62059; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62059; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0072534; C:perineuronal net; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008347; P:glial cell migration; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033987; CSPG_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 3.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS01241; LINK_1; 2.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell projection; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Hyaluronic acid; Immunoglobulin domain; Lectin; Phosphoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..3357
FT /note="Versican core protein"
FT /id="PRO_0000017523"
FT DOMAIN 24..146
FT /note="Ig-like V-type"
FT DOMAIN 150..245
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 251..347
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 3051..3087
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3089..3125
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3138..3252
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 3256..3316
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 348..1308
FT /note="GAG-alpha (glucosaminoglycan attachment domain)"
FT REGION 625..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..3051
FT /note="GAG-beta"
FT REGION 1396..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1926..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2308..2374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2475..2494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2853..2908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3331..3357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2330..2344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2351..2374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2870..2888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3340..3357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1401..1402
FT /note="Cleavage; by ADAMTS15"
FT /evidence="ECO:0000269|PubMed:24220035"
FT MOD_RES 2585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..130
FT /evidence="ECO:0000250"
FT DISULFID 172..243
FT /evidence="ECO:0000250"
FT DISULFID 196..217
FT /evidence="ECO:0000250"
FT DISULFID 270..333
FT /evidence="ECO:0000250"
FT DISULFID 294..315
FT /evidence="ECO:0000250"
FT DISULFID 3055..3066
FT /evidence="ECO:0000250"
FT DISULFID 3060..3075
FT /evidence="ECO:0000250"
FT DISULFID 3077..3086
FT /evidence="ECO:0000250"
FT DISULFID 3093..3104
FT /evidence="ECO:0000250"
FT DISULFID 3098..3113
FT /evidence="ECO:0000250"
FT DISULFID 3115..3124
FT /evidence="ECO:0000250"
FT DISULFID 3131..3142
FT /evidence="ECO:0000250"
FT DISULFID 3159..3251
FT /evidence="ECO:0000250"
FT DISULFID 3227..3243
FT /evidence="ECO:0000250"
FT DISULFID 3258..3301
FT /evidence="ECO:0000250"
FT DISULFID 3287..3314
FT /evidence="ECO:0000250"
FT VAR_SEQ 348
FT /note="P -> R (in isoform V1 and isoform V3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:7822336, ECO:0000303|PubMed:7876137"
FT /id="VSP_003087"
FT VAR_SEQ 349..3051
FT /note="Missing (in isoform V3)"
FT /evidence="ECO:0000303|PubMed:7876137"
FT /id="VSP_003090"
FT VAR_SEQ 349..1308
FT /note="Missing (in isoform V1)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:7822336"
FT /id="VSP_003088"
FT VAR_SEQ 1309..3051
FT /note="Missing (in isoform V2)"
FT /evidence="ECO:0000303|PubMed:7822336"
FT /id="VSP_003089"
FT CONFLICT 126
FT /note="A -> G (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1657
FT /note="I -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1673..1679
FT /note="TVWNSNS -> QFGIQTA (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3357 AA; 366787 MW; AE82A0D942B8323A CRC64;
MLINMKGILW MCSTLLLTHA LHQAKMETSP PVKGSLSGKV VLPCHFSTLP TLPPNYNTSE
FLRIKWSKME VDKNGKDIKE TTVLVAQNGN IKIGQDYKGR VSVPTHPDDV GDASLTMVKL
RASDAAVYRC DVMYGIEDTQ DTMSLAVDGV VFHYRAATSR YTLNFAAAQQ ACLDIGAVIA
SPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPQETYD
VYCYVDHLDG DVFHITAPSK FTFEEAEAEC TSRDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTCFPLPDSR FDAYCFKPKQ NISEATTIEM
NILAETSSPS LSKEPHMVPD RATPVIPLAT ELPIFTTHFP PAGNIVNSEQ KSVVYSQAIT
GRLATESPTT TRNTINSWDL NDSLASGSGP LGMPDISEIK EEELRSTTVI SQHATGSQAV
ITEDTQTHES VSQIEQIEVG PLVTSMEITN HISLKELPEK NKTPYESTEV TLEHTTEMPT
VSASPELATT SHYGFTLRED DREDRTLTVR SDQSTRVFSQ IPEVITVSKT SEDTTYSQLG
DLESISTSTI TMLGTDRSLI DKEKEPKTNG KVTEDEFGQS QPTTTFPSQH LTEVELLPYS
GDTTSVEGIS TVIYPSLQTD VTQGRERTET PRPELKKDPY TVDEIPEKVT KDPFIGKTEE
VFSGMPLSTS SSESSVERTE SVSPALTIEK LTGKPTEARD VEEMTTLTRL ETDVTKSDKD
VTRVHLTHST LNVEVVTVSK WPGDEDNSTS KPLPSTEHAG FTKLPPVPLS TIGINGKDKE
IPSFTDGGGE YTLFPDGTPK PLEKVSEEDL ASGELTVTFH TSTSIGSAEK SASGEPTTGD
RFLPTTSTED QVINATAEGS ALGEDTEASK PLFTGPPFVH TSDVEELAFV NYSSTQEPTT
YVDISHTSPL SIIPKTEWSV LETSVPLEDE ILGKSDQDIL EQTHLEATMS PGALRTTGVS
QGETQEEPQT PGSPFPTFSS TAVMAKETTA FEEGEGSTYT PSEGRLMTGS ERVPGLETTP
VGTSYPPGAI TDQEVEMDTM VTLMSTIRPT VVSSTESEVI YEAEGSSPTE FASTLRPFQT
HVTQLMEETT EEGKKASLDY TDLGSGLFEP RATELPKFPS TPSDISVFTA IDSLHRTPPL
SPSSSFTEEQ RVFEEESSEK TTGDILPGES VTQHPVTTLI DIVAMKTESD IDHMTSKPPV
TQPTRPSVVE RKTTSKTQEL STSTPAAGTK FHPDINVYII EVRENKTGRL SDMIVSGHPI
DSESKEEEPC SEETDPLHDL FAEILPELPD SFEIDIYHSE EDEDGEEDCV NATDVTTTPS
VQYINGKQLV TTVPKDPEAA EARRGQYESV APSQNFPDSS ATDTHQFILA ETESSTTMQF
KKSKEGTELL EITWKPETYP ETPDHVSSGE PDVFPTLSSH DGKTTRWSES ITESSPNLEN
PVHKQPKPVP LFPEESSGEG AIEQASQETI LSRATEVALG KETDQSPTLS TSSILSSSVS
VNVLEEEPLT LTGISQTDES MSTIESWVEI TPSQTVKFSE SSSAPIIEGS GEVEENKNKI
FNMVTDLPQR DPTDTLSPLD MSKIMITNHH IYIPATIAPL DSKLPSPDAR PTTVWNSNST
SEWVSDKSFE GRKKKENEDE EGAVNAAHQG EVRAATERSD HLLLTPELES SNVDASSDLA
TWEGFILETT PTESEKEMAN STPVFRETIG VANVEAQPFE HSSSSHPRVQ EELTTLSGNP
PSLFTDLGSG DASTGMELIT ASLFTLDLES ETKVKKELPS TPSPSVEISS SFEPTGLTPS
TVLDIEIAGV MSQTSQKTLI SEISGKPTSQ SGVRDLYTGF PMGEDFSGDF SEYPTVSYPT
MKEETVGMGG SDDERVRDTQ TSSSIPTTSD NIYPVPDSKG PDSTVASTTA FPWEEVMSSA
EGSGEQLASV RSSVGPVLPL AVDIFSGTES PYFDEEFEEV AAVTEANERP TVLPTAASGN
TVDLTENGYI EVNSTMSLDF PQTMEPSKLW SKPEVNLDKQ EIGRETVTKE KAQGQKTFES
LHSSFAPEQT ILETQSLIET EFQTSDYSML TTLKTYITNK EVEEEGMSIA HMSTPGPGIK
DLESYTTHPE APGKSHSFSA TALVTESGAA RSVLMDSSTQ EEESIKLFQK GVKLTNKESN
ADLSFSGLGS GGALPPLPTT SVNLTDMKQI ISTLYAETSH MESLGTSILG DKMEDHERME
DVSSNEVRML ISKIGSISQD STEALDTTLS HTGTEEPTTS TLPFVKLMDL ERSPKQDPSG
GKRKPKTHRP QTMSGLISNE NSSASEAEEG ATSPTAFLPQ TYSVEMTKHF APSESQPSDL
FNVNSGEGSG EVDTLDLVYT SGTTQASSQG DSMLASHGFL EKHPEVSKTE AGATDVSPTA
SAMFLHHSEY KSSLYPTSTL PSTEPYKSPS EGIEDGLQDN IQFEGSTLKP SRRKTTESII
IDLDKEDSKD LGLTITESAI VKSLPELTSD KNIIIDIDHT KPVYEYIPGI QTDLDPEIKL
ESHGSSEESL QVQEKYEGAV TLSPTEESFE GSGDALLAGY TQAIYNESVT PNDGKQAEDI
SFSFATGIPV SSTETELHTF FPTASTLHIP SKLTTASPEI DKPNIEAISL DDIFESSTLS
DGQAIADQSE VISTLGHLEK TQEEYEEKKY GGPSFQPEFF SGVGEVLTDP PAYVSIGSTY
LIAQTLTELP NVVRPSDSTH YTEATPEVSS LAELSPQIPS SPFPVYVDNG VSKFPEVPHT
SAQPVSTVTS SQKSIESPFK EVHANIEETI KPLGGNVHRT EPPSMSRDPA LDVSEDESKH
KLLEELETSP TKPETSQDFP NKAKDHIPGE TVGMLAGIRT TESEPVITAD DMELGGATQQ
PHSASAAFRV ETGMVPQPIQ QEPERPTFPS LEINHETHTS LFGESILATS EKQVSQKILD
NSNQATVSST LDLHTAHALS PFSILDNSNE TAFLIGISEE SVEGTAVYLP GPDLCKTNPC
LNGGTCYPTE TSYVCTCAPG YSGDQCELDF DECHSNPCRN GATCVDGFNT FRCLCLPSYV
GALCEQDTET CDYGWHKFQG QCYKYFAHRR TWDAAERECR LQGAHLTSIL SHEEQMFVNR
VGHDYQWIGL NDKMFEHDFR WTDGSALQYE NWRPNQPDSF FSAGEDCVVI IWHENGQWND
VPCNYHLTYT CKKGTVACGQ PPVVENAKTF GKMKPRYEIN SLIRYHCKDG FIQRHLPTIR
CLGNGRWAMP KITCMNPSAY QRTYSKKYLK NSSSAKDNSI NTSKHEHRWS RRQETRR
