CO5A1_MOUSE
ID CO5A1_MOUSE Reviewed; 1838 AA.
AC O88207; A3KGE3; Q3UG94; Q6F6B0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Collagen alpha-1(V) chain;
DE Flags: Precursor;
GN Name=Col5a1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9582436; DOI=10.1016/s0167-4781(98)00016-5;
RA Wu Y.L., Sumiyoshi H., Khaleduzzaman M., Ninomiya Y., Yoshioka H.;
RT "cDNA sequence and expression of the mouse alpha1(V) collagen gene.";
RL Biochim. Biophys. Acta 1397:275-284(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30, AND FUNCTION.
RX PubMed=15246108; DOI=10.1016/j.matbio.2004.03.003;
RA Sakata-Takatani K., Matsuo N., Sumiyoshi H., Tsuda T., Yoshioka H.;
RT "Identification of a functional CBF-binding CCAAT-like motif in the core
RT promoter of the mouse pro-alpha1(V) collagen gene (Col5a1).";
RL Matrix Biol. 23:87-99(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1156-1838 (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [6]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE (ISOFORM 2).
RX PubMed=22149965; DOI=10.3109/03008207.2011.636160;
RA Mitchell A.L., Judis L.M., Schwarze U., Vaynshtok P.M., Drumm M.L.,
RA Byers P.H.;
RT "Characterization of tissue-specific and developmentally regulated
RT alternative splicing of exon 64 in the COL5A1 gene.";
RL Connect. Tissue Res. 53:267-276(2012).
CC -!- FUNCTION: Type V collagen is a member of group I collagen (fibrillar
CC forming collagen). It is a minor connective tissue component of nearly
CC ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate,
CC thrombospondin, heparin, and insulin (By similarity). Transcriptionally
CC activated by CEBPZ, which recognizes a CCAAT-like motif, CAAAT in the
CC COL5A1 promoter. {ECO:0000250, ECO:0000269|PubMed:15246108}.
CC -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in most
CC tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha
CC 3(V) chains in placenta. Interacts with CSPG4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A {ECO:0000303|PubMed:22149965};
CC IsoId=O88207-1; Sequence=Displayed;
CC Name=2; Synonyms=B {ECO:0000303|PubMed:22149965};
CC IsoId=O88207-2; Sequence=VSP_059656;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:22149965). Isoform 2 is
CC more highly expressed in liver, kidney and lung (PubMed:22149965).
CC {ECO:0000269|PubMed:22149965}.
CC -!- DEVELOPMENTAL STAGE: Detected at 11 dpc, 12 dpc, 14 dpc, 16 dpc and 18
CC dpc. Expressed in limbs, vertebrae, heart, brain, liver, intestine,
CC tongue, tail, skin, calvaria, lung and kidney of 18 dpc embryos
CC (PubMed:9582436). Isoform 2 is detected at 13.5 dpc and its expression
CC increases from 13.5 dpc to 5 weeks after birth more specially in liver,
CC lung, ileum and heart. The expression slightly decreases after 15 weeks
CC (PubMed:22149965). {ECO:0000269|PubMed:22149965,
CC ECO:0000269|PubMed:9582436}.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- PTM: Sulfated on 40% of tyrosines. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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; AB009993; BAA28786.1; -; mRNA.
DR EMBL; AL731778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB098608; BAD26732.1; -; Genomic_DNA.
DR EMBL; AK148055; BAE28315.1; -; mRNA.
DR CCDS; CCDS15831.1; -. [O88207-1]
DR RefSeq; NP_056549.2; NM_015734.2. [O88207-1]
DR RefSeq; XP_006497707.1; XM_006497644.3. [O88207-2]
DR AlphaFoldDB; O88207; -.
DR SMR; O88207; -.
DR BioGRID; 198821; 16.
DR ComplexPortal; CPX-2962; Collagen type V trimer variant 1.
DR ComplexPortal; CPX-2963; Collagen type V trimer variant 2.
DR ComplexPortal; CPX-2964; Collagen type V trimer variant 3.
DR ComplexPortal; CPX-2977; Collagen type XI trimer variant 3.
DR IntAct; O88207; 1.
DR STRING; 10090.ENSMUSP00000028280; -.
DR iPTMnet; O88207; -.
DR PhosphoSitePlus; O88207; -.
DR MaxQB; O88207; -.
DR PaxDb; O88207; -.
DR PeptideAtlas; O88207; -.
DR PRIDE; O88207; -.
DR ProteomicsDB; 283543; -. [O88207-1]
DR Antibodypedia; 3446; 455 antibodies from 37 providers.
DR DNASU; 12831; -.
DR Ensembl; ENSMUST00000028280; ENSMUSP00000028280; ENSMUSG00000026837. [O88207-1]
DR GeneID; 12831; -.
DR KEGG; mmu:12831; -.
DR UCSC; uc008ixt.2; mouse. [O88207-1]
DR CTD; 1289; -.
DR MGI; MGI:88457; Col5a1.
DR VEuPathDB; HostDB:ENSMUSG00000026837; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159211; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; O88207; -.
DR OMA; VAGMDGQ; -.
DR OrthoDB; 199083at2759; -.
DR PhylomeDB; O88207; -.
DR TreeFam; TF323987; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474244; Extracellular matrix organization.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12831; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Col5a1; mouse.
DR PRO; PR:O88207; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88207; protein.
DR Bgee; ENSMUSG00000026837; Expressed in umbilical cord and 260 other tissues.
DR ExpressionAtlas; O88207; baseline and differential.
DR Genevisible; O88207; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005588; C:collagen type V trimer; ISO:MGI.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0032964; P:collagen biosynthetic process; ISO:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048592; P:eye morphogenesis; ISO:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0045112; P:integrin biosynthetic process; ISO:MGI.
DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; ISO:MGI.
DR GO; GO:0051128; P:regulation of cellular component organization; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR GO; GO:0035989; P:tendon development; IMP:MGI.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:MGI.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Collagen; Extracellular matrix; Heparin-binding;
KW Hydroxylation; Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..1838
FT /note="Collagen alpha-1(V) chain"
FT /id="PRO_0000041761"
FT DOMAIN 72..244
FT /note="Laminin G-like"
FT DOMAIN 1609..1837
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 231..443
FT /note="Nonhelical region"
FT /evidence="ECO:0000250"
FT REGION 242..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..558
FT /note="Interrupted collagenous region"
FT /evidence="ECO:0000250"
FT REGION 559..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..1570
FT /note="Triple-helical region"
FT /evidence="ECO:0000250"
FT REGION 1571..1605
FT /note="Nonhelical region"
FT /evidence="ECO:0000250"
FT COMPBIAS 363..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..973
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 236
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 240
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 262
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 263
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 570
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 576
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 621
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 627
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 639
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 642
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 648
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 654
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 657
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 675
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 678
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 680
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 686
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 690
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 696
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 705
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 708
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 717
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 720
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 726
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 732
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 744
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 750
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 756
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 762
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 765
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 771
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 774
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 780
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 789
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 795
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 804
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 807
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 810
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 816
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 819
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 834
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 846
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 864
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 870
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 873
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 876
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 882
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 888
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 891
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 897
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 903
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 906
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 930
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 945
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1017
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1020
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1023
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1029
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1221
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1224
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1467
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1470
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1601
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1604
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1690..1712
FT /note="ARITSWPKENPGSWFSEFKRGKL -> SKMARWPKEQPSTWYSQYKRGSL
FT (in isoform 2)"
FT /id="VSP_059656"
FT CONFLICT 1097
FT /note="A -> S (in Ref. 1; BAA28786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1838 AA; 183677 MW; D20F4E5198A09ECF CRC64;
MDVHTRWKAA RPGALLLSSP LLLFLLLLWA PPSSRAAQPA DLLEMLDFHN LPSGVTKTTG
FCATRRSSSE PDVAYRVSKD AQLSMPTKQL YPESGFPEDF SILTTVKAKK GSQAFLVSIY
NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE EYPLFPGINL SDGKWHRIAL SVYKKNVTLI
LDCKKKITKF LSRSDHPIID TNGIVMFGSR ILDDEIFEGD IQQLLFVSDN RAAYDYCEHY
SPDCDTAVPD TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP TQKPVEAARE
TTEVPEEQTQ PLPEAPTVPE TSDTADKEDS LGIGDYDYVP PDDYYTPPPY EDFGYGEGVE
NPDQPTNPDS GAEVPTSTTV TSNTSNPAPG EGKDDLGGEF TEETIKNLEE NYYDPYFDPD
SDSSVSPSEI GPGMPANQDT IFEGIGGPRG EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP
GPPGTTGPTG QMGDPGERGP PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS
AQESQAQAIL QQARLALRGP AGPMGLTGRP GPMGPPGSGG LKGEPGDMGP QGPRGVQGPP
GPTGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP SGPPGIPGDD
GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG MDGQPGPKGN VGPQGEPGPP
GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP GLPGMPGADG PPGHPGKEGP PGEKGGQGPP
GPQGPIGYPG PRGVKGADGI RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED
GPEGPKGRGG PNGDPGPLGP TGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP NGPQGPTGFP
GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG PQGPTGETGP MGERGHPGPP
GPPGEQGLPG AAGKEGTKGD PGPAGLPGKD GPPGLRGFPG DRGLPGPVGA LGLKGSEGPP
GPPGPAGSPG ERGPAGAAGP IGIPGRPGPQ GPPGPAGEKG LPGEKGPQGP AGRDGLQGPV
GLPGPAGPVG PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP
GPRGQQGLFG QKGDEGSRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP PGPPGPRGPS
GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GDPGLPGEGG PLGPKGERGE KGEAGPSGAA
GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT
GEPGPSGPPG KRGPPGPAGP EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR
GIPGPVGEQG LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK
GDRGLPGPQG SSGPKGDQGI TGPSGPLGPP GPPGLPGPPG PKGAKGSSGP TGPKGEAGHP
GLPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGAGES YVDYADGMEE IFGSLNSLKL
EIEQMKRPLG TQQNPARTCK DLQLCHPDFP DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC
VFPDKKSEGA RITSWPKENP GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ
NVTYNCYQSV AWQDAATGSY DKAIRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFLG
