ID COFA1_HUMAN Reviewed; 1388 AA.
AC P39059; Q5T6J4; Q9UDC5; Q9Y4W4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 27-MAR-2024, entry version 198.
DE RecName: Full=Collagen alpha-1(XV) chain;
DE Contains:
DE RecName: Full=Restin;
DE AltName: Full=Endostatin-XV;
DE AltName: Full=Related to endostatin;
DE AltName: Full=Restin-I;
DE Contains:
DE RecName: Full=Restin-2;
DE AltName: Full=Restin-II;
DE Contains:
DE RecName: Full=Restin-3;
DE AltName: Full=Restin-III;
DE Contains:
DE RecName: Full=Restin-4;
DE AltName: Full=Restin-IV;
DE Flags: Precursor;
GN Name=COL15A1;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Umbilical cord;
RX PubMed=8106446; DOI=10.1016/s0021-9258(17)37611-1;
RA Kivirikko S., Heinamaki P., Rehn M.V., Honkanen N., Myers J.C.,
RA Pihlajaniemi T.;
RT "Primary structure of the alpha 1 chain of human type XV collagen and exon-
RT intron organization in the 3' region of the corresponding gene.";
RL J. Biol. Chem. 269:4773-4779(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9651385; DOI=10.1074/jbc.273.28.17824;
RA Haegg P.M., Muona A., Lietard J., Kivirikko S., Pihlajaniemi T.;
RT "Complete exon-intron organization of the human gene for the alpha1 chain
RT of type XV collagen (COL15A1) and comparison with the homologous COL18A1
RT gene.";
RL J. Biol. Chem. 273:17824-17831(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-569, AND VARIANT VAL-204.
RC TISSUE=Placenta;
RX PubMed=8307960; DOI=10.1016/s0021-9258(17)41739-x;
RA Muragaki Y., Abe N., Ninomiya Y., Olsen B.R., Ooshima A.;
RT "The human alpha 1(XV) collagen chain contains a large amino-terminal non-
RT triple helical domain with a tandem repeat structure and homology to alpha
RT 1(XVIII) collagen.";
RL J. Biol. Chem. 269:4042-4046(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 544-1252.
RX PubMed=1279671; DOI=10.1073/pnas.89.21.10144;
RA Myers J.C., Kivirikko S., Gordon M.K., Dion A.S., Pihlajaniemi T.;
RT "Identification of a previously unknown human collagen chain, alpha 1(XV),
RT characterized by extensive interruptions in the triple-helical region.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10144-10148(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1145, AND CHROMOSOMAL LOCATION.
RC TISSUE=Placenta;
RX PubMed=1427836; DOI=10.1016/s0888-7543(05)80209-5;
RA Huebner K., Cannizzaro L.A., Jabs E.W., Kivirikko S., Manzone H.,
RA Pihlajaniemi T., Myers J.C.;
RT "Chromosomal assignment of a gene encoding a new collagen type (COL15A1) to
RT 9q21 --> q22.";
RL Genomics 14:220-224(1992).
RN [7]
RP PROTEIN SEQUENCE OF 1198-1210; 1207-1219; 1213-1225 AND 1221-1233,
RP IDENTIFICATION OF RESTIN-RELATED PEPTIDES, AND DISULFIDE BOND.
RX PubMed=15698950; DOI=10.1016/j.bbapap.2004.10.013;
RA John H., Radtke K., Staendker L., Forssmann W.G.;
RT "Identification and characterization of novel endogenous proteolytic forms
RT of the human angiogenesis inhibitors restin and endostatin.";
RL Biochim. Biophys. Acta 1747:161-170(2005).
RN [8]
RP FUNCTION.
RX PubMed=10049780; DOI=10.1006/bbrc.1999.0248;
RA Ramchandran R., Dhanabal M., Volk R., Waterman M.J.F., Segal M., Lu H.,
RA Knebelmann B., Sukhatme V.P.;
RT "Antiangiogenic activity of restin, NC10 domain of human collagen XV:
RT comparison to endostatin.";
RL Biochem. Biophys. Res. Commun. 255:735-739(1999).
RN [9]
RP GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND INTERCHAIN DISULFIDE BONDS.
RX PubMed=10791950; DOI=10.1074/jbc.m000519200;
RA Li D., Clark C.C., Myers J.C.;
RT "Basement membrane zone type XV collagen is a disulfide-bonded chondroitin
RT sulfate proteoglycan in human tissues and cultured cells.";
RL J. Biol. Chem. 275:22339-22347(2000).
RN [10]
RP GLYCOSYLATION AT THR-265, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA Nilsson J., Larson G.;
RT "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT prohormones as a novel class of proteoglycans.";
RL Mol. Cell. Proteomics 14:41-49(2015).
RN [12]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-745.
RX PubMed=32337544; DOI=10.1093/glycob/cwaa039;
RA Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A.,
RA Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D.,
RA Larson G., Salanti A., Clausen T.M.;
RT "An affinity chromatography and glycoproteomics workflow to profile the
RT chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in
RT the placenta and in cancer.";
RL Glycobiology 30:989-1002(2020).
RN [13]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA Pandey A.;
RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL J. Proteins Proteom. 13:187-203(2022).
RN [14]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-343.
RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL Mol. Cell. Proteomics 22:100617-100617(2023).
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000269|PubMed:10049780}.
CC -!- FUNCTION: Restin potently inhibits angiogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000269|PubMed:15698950}.
CC -!- SUBUNIT: [Restin]: Interacts moderately with EFEMP2.
CC {ECO:0000250|UniProtKB:O35206}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Secreted {ECO:0000269|PubMed:25326458,
CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
CC -!- TISSUE SPECIFICITY: Detected in fibroblasts and urine (at protein
CC level) (PubMed:25326458, PubMed:36213313, PubMed:37453717). Detected in
CC placenta (at protein level) (PubMed:32337544). Expressed predominantly
CC in internal organs such as adrenal gland, pancreas and kidney.
CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:32337544,
CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: O-glycosylated; with core 1 or possibly core 8 glycans. Contains
CC chondroitin sulfate. {ECO:0000269|PubMed:10791950,
CC ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:25326458,
CC ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family. {ECO:0000305}.
CC -!- CAUTION: The name restin has also been used for CAP-Gly domain-
CC containing linker protein 1 the product of the CLIP1 gene.
CC {ECO:0000305}.
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DR EMBL; L25286; AAA58429.1; -; mRNA.
DR EMBL; L25280; AAC78500.1; -; Genomic_DNA.
DR EMBL; L25281; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; L25282; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; L25283; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; L25284; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; L25285; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052956; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052957; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052958; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052959; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052960; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052961; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052962; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052963; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052964; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052965; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052966; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052967; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052968; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052969; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052970; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052971; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052972; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052973; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052974; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AF052975; AAC78500.1; JOINED; Genomic_DNA.
DR EMBL; AL136084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D21230; BAA04762.1; -; mRNA.
DR EMBL; L01697; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS35081.1; -.
DR PIR; A53317; A53317.
DR RefSeq; NP_001846.3; NM_001855.4.
DR RefSeq; XP_011516516.1; XM_011518214.2.
DR PDB; 3N3F; X-ray; 2.00 A; A/B=1133-1186.
DR PDBsum; 3N3F; -.
DR AlphaFoldDB; P39059; -.
DR SMR; P39059; -.
DR BioGRID; 107702; 6.
DR ComplexPortal; CPX-1756; Collagen type XV trimer.
DR IntAct; P39059; 5.
DR STRING; 9606.ENSP00000364140; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 727; 1 O-Linked glycan (1 site).
DR GlyCosmos; P39059; 22 sites, 8 glycans.
DR GlyGen; P39059; 27 sites, 8 O-linked glycans (16 sites).
DR iPTMnet; P39059; -.
DR PhosphoSitePlus; P39059; -.
DR BioMuta; COL15A1; -.
DR DMDM; 68839886; -.
DR jPOST; P39059; -.
DR MassIVE; P39059; -.
DR MaxQB; P39059; -.
DR PaxDb; 9606-ENSP00000364140; -.
DR PeptideAtlas; P39059; -.
DR ProteomicsDB; 55310; -.
DR Pumba; P39059; -.
DR Antibodypedia; 14522; 147 antibodies from 20 providers.
DR DNASU; 1306; -.
DR Ensembl; ENST00000375001.8; ENSP00000364140.3; ENSG00000204291.11.
DR GeneID; 1306; -.
DR KEGG; hsa:1306; -.
DR MANE-Select; ENST00000375001.8; ENSP00000364140.3; NM_001855.5; NP_001846.3.
DR UCSC; uc004azb.3; human.
DR AGR; HGNC:2192; -.
DR CTD; 1306; -.
DR DisGeNET; 1306; -.
DR GeneCards; COL15A1; -.
DR HGNC; HGNC:2192; COL15A1.
DR HPA; ENSG00000204291; Tissue enhanced (placenta).
DR MIM; 120325; gene.
DR neXtProt; NX_P39059; -.
DR OpenTargets; ENSG00000204291; -.
DR PharmGKB; PA26708; -.
DR VEuPathDB; HostDB:ENSG00000204291; -.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158302; -.
DR HOGENOM; CLU_004003_0_0_1; -.
DR InParanoid; P39059; -.
DR OMA; FFMSGPP; -.
DR OrthoDB; 5363002at2759; -.
DR PhylomeDB; P39059; -.
DR TreeFam; TF315821; -.
DR PathwayCommons; P39059; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P39059; -.
DR SIGNOR; P39059; -.
DR BioGRID-ORCS; 1306; 11 hits in 1160 CRISPR screens.
DR ChiTaRS; COL15A1; human.
DR GeneWiki; Collagen,_type_XV,_alpha_1; -.
DR GenomeRNAi; 1306; -.
DR Pharos; P39059; Tbio.
DR PRO; PR:P39059; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P39059; Protein.
DR Bgee; ENSG00000204291; Expressed in skin of hip and 184 other cell types or tissues.
DR ExpressionAtlas; P39059; baseline and differential.
DR Genevisible; P39059; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005582; C:collagen type XV trimer; TAS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; ISS:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF912; COLLAGEN ALPHA-1(XV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Cell adhesion; Collagen; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1388
FT /note="Collagen alpha-1(XV) chain"
FT /id="PRO_0000005788"
FT CHAIN 1198..1386
FT /note="Restin"
FT /id="PRO_0000005789"
FT CHAIN 1207..1386
FT /note="Restin-2"
FT /id="PRO_0000423014"
FT CHAIN 1213..1386
FT /note="Restin-3"
FT /id="PRO_0000423015"
FT CHAIN 1221..1386
FT /note="Restin-4"
FT /id="PRO_0000423016"
FT DOMAIN 66..249
FT /note="Laminin G-like"
FT REPEAT 358..408
FT /note="1"
FT REPEAT 409..459
FT /note="2"
FT REPEAT 460..509
FT /note="3"
FT REPEAT 510..555
FT /note="4"
FT DOMAIN 619..680
FT /note="Collagen-like 1"
FT DOMAIN 681..731
FT /note="Collagen-like 2"
FT DOMAIN 823..865
FT /note="Collagen-like 3"
FT DOMAIN 879..927
FT /note="Collagen-like 4"
FT REGION 223..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..555
FT /note="Nonhelical region 1 (NC1)"
FT REGION 266..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..555
FT /note="4 X tandem repeats"
FT REGION 371..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..573
FT /note="Triple-helical region 1 (COL1)"
FT REGION 574..618
FT /note="Nonhelical region 2 (NC2)"
FT REGION 619..732
FT /note="Triple-helical region 2 (COL2)"
FT REGION 733..763
FT /note="Nonhelical region 3 (NC3)"
FT REGION 764..798
FT /note="Triple-helical region 3 (COL3)"
FT REGION 799..822
FT /note="Nonhelical region 4 (NC4)"
FT REGION 823..867
FT /note="Triple-helical region 4 (COL4)"
FT REGION 827..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..878
FT /note="Nonhelical region 5 (NC5)"
FT REGION 879..949
FT /note="Triple-helical region 5 (COL5)"
FT REGION 950..983
FT /note="Nonhelical region 6 (NC6)"
FT REGION 984..1013
FT /note="Triple-helical region 6 (COL6)"
FT REGION 988..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1027
FT /note="Nonhelical region 7 (NC7)"
FT REGION 1028..1045
FT /note="Triple-helical region 7 (COL7)"
FT REGION 1029..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1052
FT /note="Nonhelical region 8 (NC8)"
FT REGION 1053..1107
FT /note="Triple-helical region 8 (COL8)"
FT REGION 1108..1117
FT /note="Nonhelical region 9 (NC9)"
FT REGION 1118..1132
FT /note="Triple-helical region 9 (COL9)"
FT REGION 1133..1388
FT /note="Nonhelical region 10 (NC10)"
FT COMPBIAS 375..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..664
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 243
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:37453717"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:32337544"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1237..1377
FT /evidence="ECO:0000269|PubMed:15698950"
FT DISULFID 1339..1369
FT /evidence="ECO:0000269|PubMed:15698950"
FT VARIANT 163
FT /note="R -> H (in dbSNP:rs2075662)"
FT /id="VAR_033787"
FT VARIANT 204
FT /note="M -> V (in dbSNP:rs2075663)"
FT /evidence="ECO:0000269|PubMed:8307960"
FT /id="VAR_033788"
FT VARIANT 391
FT /note="T -> M (in dbSNP:rs10988532)"
FT /id="VAR_033789"
FT VARIANT 442
FT /note="A -> T (in dbSNP:rs16918128)"
FT /id="VAR_033790"
FT VARIANT 446
FT /note="G -> R (in dbSNP:rs35934703)"
FT /id="VAR_033791"
FT VARIANT 504
FT /note="G -> V (in dbSNP:rs2297603)"
FT /id="VAR_048776"
FT VARIANT 506
FT /note="E -> D (in dbSNP:rs35250850)"
FT /id="VAR_033792"
FT VARIANT 531
FT /note="P -> R (in dbSNP:rs35529307)"
FT /id="VAR_033793"
FT VARIANT 705
FT /note="P -> L (in dbSNP:rs41308900)"
FT /id="VAR_061114"
FT VARIANT 989
FT /note="K -> R (in dbSNP:rs35642150)"
FT /id="VAR_033794"
FT VARIANT 1001
FT /note="K -> R (in dbSNP:rs35544077)"
FT /id="VAR_033795"
FT VARIANT 1332
FT /note="V -> I (in dbSNP:rs10519)"
FT /id="VAR_033796"
FT CONFLICT 10
FT /note="C -> S (in Ref. 4; BAA04762)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> D (in Ref. 1; AAA58429)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="SV -> RA (in Ref. 1; AAA58429 and 4; BAA04762)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="A -> P (in Ref. 1; AAA58429)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="A -> R (in Ref. 1; AAA58429 and 2; AAC78500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="L -> LLGELIPIPADSPPPPALSSN (in Ref. 2; AAC78500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178..1197
FT /note="Missing (in Ref. 2; AAC78500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1227
FT /note="F -> V (in Ref. 2; AAC78500)"
FT /evidence="ECO:0000305"
FT STRAND 1135..1140
FT /evidence="ECO:0007829|PDB:3N3F"
FT HELIX 1141..1145
FT /evidence="ECO:0007829|PDB:3N3F"
FT HELIX 1146..1150
FT /evidence="ECO:0007829|PDB:3N3F"
FT STRAND 1155..1159
FT /evidence="ECO:0007829|PDB:3N3F"
FT TURN 1160..1163
FT /evidence="ECO:0007829|PDB:3N3F"
FT STRAND 1164..1169
FT /evidence="ECO:0007829|PDB:3N3F"
FT STRAND 1172..1175
FT /evidence="ECO:0007829|PDB:3N3F"
SQ SEQUENCE 1388 AA; 141720 MW; AF54DDCC136C3745 CRC64;
MAPRRNNGQC WCLLMLLSVS TPLPAVTQTR GATETASQGH LDLTQLIGVP LPSSVSFVTG
YGGFPAYSFG PGANVGRPAR TLIPSTFFRD FAISVVVKPS STRGGVLFAI TDAFQKVIYL
GLRLSGVEDG HQRIILYYTE PGSHVSQEAA AFSVPVMTHR WNRFAMIVQG EEVTLLVNCE
EHSRIPFQRS SQALAFESSA GIFMGNAGAT GLERFTGSLQ QLTVHPDPRT PEELCDPEES
SASGETSGLQ EADGVAEILE AVTYTQASPK EAKVEPINTP PTPSSPFEDM ELSGEPVPEG
TLETTNMSII QHSSPKQGSG EILNDTLEGV HSVDGDPITD SGSGAGAFLD IAEEKNLAAT
AAGLAEVPIS TAGEAEASSV PTGGPTLSMS TENPEEGVTP GPDNEERLAA TAAGEAEALA
SMPGEVEASG VAPGELDLSM SAQSLGEEAT VGPSSEDSLT TAAAATEVSL STFEDEEASG
VPTDGLAPLT ATMAPERAVT SGPGDEEDLA AATTEEPLIT AGGEESGSPP PDGPPLPLPT
VAPERWITPA QREHVGMKGQ AGPKGEKGDA GEELPGPPEP SGPVGPTAGA EAEGSGLGWG
SDVGSGSGDL VGSEQLLRGP PGPPGPPGLP GIPGKPGTDV FMGPPGSPGE DGPAGEPGPP
GPEGQPGVDG ATGLPGMKGE KGARGPNGSV GEKGDPGNRG LPGPPGKKGQ AGPPGVMGPP
GPPGPPGPPG PGCTMGLGFE DTEGSGSTQL LNEPKLSRPT AAIGLKGEKG DRGPKGERGM
DGASIVGPPG PRGPPGHIKV LSNSLINITH GFMNFSDIPE LVGPPGPDGL PGLPGFPGPR
GPKGDTGLPG FPGLKGEQGE KGEPGAILTE DIPLERLMGK KGEPGMHGAP GPMGPKGPPG
HKGEFGLPGR PGRPGLNGLK GTKGDPGVIM QGPPGLPGPP GPPGPPGAVI NIKGAIFPIP
VRPHCKMPVD TAHPGSPELI TFHGVKGEKG SWGLPGSKGE KGDQGAQGPP GPPLDLAYLR
HFLNNLKGEN GDKGFKGEKG EKGDINGSFL MSGPPGLPGN PGPAGQKGET VVGPQGPPGA
PGLPGPPGFG RPGDPGPPGP PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSN
MDDMLQKAHL VIEGTFIYLR DSTEFFIRVR DGWKKLQLGE LIPIPADSPP PPALSSNPHQ
LLPPPNPISS ANYEKPALHL AALNMPFSGD IRADFQCFKQ ARAAGLLSTY RAFLSSHLQD
LSTIVRKAER YSLPIVNLKG QVLFNNWDSI FSGHGGQFNM HIPIYSFDGR DIMTDPSWPQ
KVIWHGSSPH GVRLVDNYCE AWRTADTAVT GLASPLSTGK ILDQKAYSCA NRLIVLCIEN
SFMTDARK
//
