COCA1_HUMAN
ID COCA1_HUMAN Reviewed; 3063 AA.
AC Q99715; O43853; Q15955; Q5VYK1; Q5VYK2; Q71UR3; Q99716;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Collagen alpha-1(XII) chain;
DE Flags: Precursor;
GN Name=COL12A1; Synonyms=COL12A1L;
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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
RP 1280-1295; 1782-1801 AND 2906-2916, AND VARIANT SER-3058.
RX PubMed=9143499; DOI=10.1006/geno.1997.4638;
RA Gerecke D.R., Olson P.F., Koch M., Knoll J.H.M., Taylor R., Hudson D.L.,
RA Champliaud M.-F., Olsen B.R., Burgeson R.E.;
RT "Complete primary structure of two splice variants of collagen XII, and
RT assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX) collagen
RT (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-
RT q13.";
RL Genomics 41:236-242(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=9826181; DOI=10.1046/j.1432-1327.1998.2570362.x;
RA Chiquet M., Mumenthaler U., Wittwer M., Jin W., Koch M.;
RT "The chick and human collagen alpha1(XII) gene promoter -- activity of
RT highly conserved regions around the first exon and in the first intron.";
RL Eur. J. Biochem. 257:362-371(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 299-816 (ISOFORMS 1/4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cornea;
RX PubMed=9344363;
RA Wessel H., Anderson S., Fite D., Halvas E., Hempel J., SundarRaj N.;
RT "Type XII collagen contributes to diversities in human corneal and limbal
RT extracellular matrices.";
RL Invest. Ophthalmol. Vis. Sci. 38:2408-2422(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2567-2755 (ISOFORM 4).
RX PubMed=1427837; DOI=10.1016/s0888-7543(05)80210-1;
RA Oh S.P., Taylor R.W., Gerecke D.R., Rochelle J.M., Seldin M.F., Olsen B.R.;
RT "The mouse alpha 1(XII) and human alpha 1(XII)-like collagen genes are
RT localized on mouse chromosome 9 and human chromosome 6.";
RL Genomics 14:225-231(1992).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2528 AND ASN-2679.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INVOLVEMENT IN UCMD2, INVOLVEMENT IN BTHLM2, AND VARIANT BTHLM2 THR-2334.
RX PubMed=24334604; DOI=10.1093/hmg/ddt627;
RA Zou Y., Zwolanek D., Izu Y., Gandhy S., Schreiber G., Brockmann K.,
RA Devoto M., Tian Z., Hu Y., Veit G., Meier M., Stetefeld J., Hicks D.,
RA Straub V., Voermans N.C., Birk D.E., Barton E.R., Koch M., Boennemann C.G.;
RT "Recessive and dominant mutations in COL12A1 cause a novel EDS/myopathy
RT overlap syndrome in humans and mice.";
RL Hum. Mol. Genet. 23:2339-2352(2014).
RN [9]
RP INVOLVEMENT IN BTHLM2, VARIANTS BTHLM2 CYS-1965 AND ASP-2786, AND VARIANTS
RP THR-1738 AND SER-3058.
RX PubMed=24334769; DOI=10.1093/hmg/ddt637;
RA Hicks D., Farsani G.T., Laval S., Collins J., Sarkozy A., Martoni E.,
RA Shah A., Zou Y., Koch M., Boennemann C.G., Roberts M., Lochmueller H.,
RA Bushby K., Straub V.;
RT "Mutations in the collagen XII gene define a new form of extracellular
RT matrix-related myopathy.";
RL Hum. Mol. Genet. 23:2353-2363(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Type XII collagen interacts with type I collagen-containing
CC fibrils, the COL1 domain could be associated with the surface of the
CC fibrils, and the COL2 and NC3 domains may be localized in the
CC perifibrillar matrix. {ECO:0000250}.
CC -!- SUBUNIT: Trimer of identical chains each containing 190 kDa of non-
CC triple-helical sequences.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=The final tissue form of collagen XII may contain homotrimers
CC of either isoform 1 or isoform 2 or any combination of isoform 1 and
CC isoform 2.;
CC Name=1; Synonyms=Long;
CC IsoId=Q99715-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q99715-2; Sequence=VSP_001149;
CC Name=4;
CC IsoId=Q99715-4; Sequence=VSP_024942;
CC -!- TISSUE SPECIFICITY: Found in collagen I-containing tissues: both
CC isoform 1 and isoform 2 appear in amnion, chorion, skeletal muscle,
CC small intestine, and in cell culture of dermal fibroblasts,
CC keratinocytes and endothelial cells. Only isoform 2 is found in lung,
CC placenta, kidney and a squamous cell carcinoma cell line. Isoform 1 is
CC also present in the corneal epithelial Bowman's membrane (BM) and the
CC interfibrillar matrix of the corneal stroma, but it is not detected in
CC the limbal BM. {ECO:0000269|PubMed:9344363}.
CC -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC end. {ECO:0000250}.
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: Isoform 1 O-glycosylation; glycosaminoglycan of chondroitin-
CC sulfate type. {ECO:0000250}.
CC -!- DISEASE: Ullrich congenital muscular dystrophy 2 (UCMD2) [MIM:616470]:
CC A form of Ullrich muscular dystrophy, a congenital myopathy
CC characterized by muscle weakness and multiple joint contractures,
CC generally noted at birth or early infancy. The clinical course is more
CC severe than in Bethlem myopathy. {ECO:0000269|PubMed:24334604}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Bethlem myopathy 2 (BTHLM2) [MIM:616471]: A form of Bethlem
CC myopathy, a benign proximal myopathy characterized by early childhood
CC onset and joint contractures most frequently affecting the elbows and
CC ankles. BTHLM2 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:24334604, ECO:0000269|PubMed:24334769}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; U73778; AAC51244.1; -; mRNA.
DR EMBL; U73779; AAD40483.1; -; mRNA.
DR EMBL; AL080250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF061871; AAC83578.1; -; Genomic_DNA.
DR EMBL; U68139; AAC01506.1; -; mRNA.
DR EMBL; AH004088; AAB23937.2; -; Genomic_DNA.
DR CCDS; CCDS43481.1; -. [Q99715-2]
DR CCDS; CCDS43482.1; -. [Q99715-1]
DR PIR; A44479; A44479.
DR RefSeq; NP_004361.3; NM_004370.5. [Q99715-1]
DR RefSeq; NP_542376.2; NM_080645.2. [Q99715-2]
DR SMR; Q99715; -.
DR BioGRID; 107700; 67.
DR ComplexPortal; CPX-1753; Collagen type XII trimer.
DR IntAct; Q99715; 9.
DR STRING; 9606.ENSP00000325146; -.
DR GlyConnect; 1131; 70 N-Linked glycans (4 sites).
DR GlyGen; Q99715; 14 sites, 82 N-linked glycans (4 sites), 9 O-linked glycans (6 sites).
DR iPTMnet; Q99715; -.
DR PhosphoSitePlus; Q99715; -.
DR BioMuta; COL12A1; -.
DR DMDM; 146345397; -.
DR EPD; Q99715; -.
DR jPOST; Q99715; -.
DR MassIVE; Q99715; -.
DR MaxQB; Q99715; -.
DR PaxDb; Q99715; -.
DR PeptideAtlas; Q99715; -.
DR PRIDE; Q99715; -.
DR ProteomicsDB; 78429; -. [Q99715-1]
DR ProteomicsDB; 78430; -. [Q99715-2]
DR ProteomicsDB; 78431; -. [Q99715-4]
DR Antibodypedia; 2124; 101 antibodies from 20 providers.
DR DNASU; 1303; -.
DR Ensembl; ENST00000322507.13; ENSP00000325146.8; ENSG00000111799.22. [Q99715-1]
DR Ensembl; ENST00000345356.10; ENSP00000305147.9; ENSG00000111799.22. [Q99715-2]
DR Ensembl; ENST00000416123.6; ENSP00000412864.2; ENSG00000111799.22. [Q99715-4]
DR GeneID; 1303; -.
DR KEGG; hsa:1303; -.
DR MANE-Select; ENST00000322507.13; ENSP00000325146.8; NM_004370.6; NP_004361.3.
DR UCSC; uc063ppm.1; human. [Q99715-1]
DR CTD; 1303; -.
DR DisGeNET; 1303; -.
DR GeneCards; COL12A1; -.
DR HGNC; HGNC:2188; COL12A1.
DR HPA; ENSG00000111799; Tissue enhanced (endometrium).
DR MalaCards; COL12A1; -.
DR MIM; 120320; gene.
DR MIM; 616470; phenotype.
DR MIM; 616471; phenotype.
DR neXtProt; NX_Q99715; -.
DR OpenTargets; ENSG00000111799; -.
DR Orphanet; 610; Bethlem myopathy.
DR Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
DR Orphanet; 536516; Myopathic Ehlers-Danlos syndrome.
DR PharmGKB; PA26704; -.
DR VEuPathDB; HostDB:ENSG00000111799; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000154923; -.
DR HOGENOM; CLU_000467_0_0_1; -.
DR InParanoid; Q99715; -.
DR OMA; KAEIQKC; -.
DR OrthoDB; 67372at2759; -.
DR PhylomeDB; Q99715; -.
DR TreeFam; TF329914; -.
DR PathwayCommons; Q99715; -.
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; Q99715; -.
DR SIGNOR; Q99715; -.
DR BioGRID-ORCS; 1303; 5 hits in 1068 CRISPR screens.
DR ChiTaRS; COL12A1; human.
DR GeneWiki; Collagen,_type_XII,_alpha_1; -.
DR GenomeRNAi; 1303; -.
DR Pharos; Q99715; Tbio.
DR PRO; PR:Q99715; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99715; protein.
DR Bgee; ENSG00000111799; Expressed in tibia and 170 other tissues.
DR ExpressionAtlas; Q99715; baseline and differential.
DR Genevisible; Q99715; HS.
DR GO; GO:0005595; C:collagen type XII trimer; TAS:ProtInc.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
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; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; NAS:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR CDD; cd00063; FN3; 18.
DR Gene3D; 2.60.40.10; -; 18.
DR Gene3D; 3.40.50.410; -; 4.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00041; fn3; 18.
DR Pfam; PF00092; VWA; 4.
DR SMART; SM00060; FN3; 18.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 4.
DR SUPFAM; SSF49265; SSF49265; 11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 4.
DR PROSITE; PS50853; FN3; 18.
DR PROSITE; PS50234; VWFA; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Collagen;
KW Congenital muscular dystrophy; Direct protein sequencing; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..3063
FT /note="Collagen alpha-1(XII) chain"
FT /id="PRO_0000005783"
FT DOMAIN 27..117
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 140..316
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 336..426
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 440..616
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 634..722
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 725..816
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 817..905
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 907..998
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 999..1087
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1089..1179
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1199..1371
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1387..1476
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1477..1567
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1568..1658
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1659..1754
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1755..1849
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1850..1935
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1936..2026
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2027..2117
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2118..2206
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2207..2294
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2323..2496
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2520..2712
FT /note="Laminin G-like"
FT DOMAIN 2747..2798
FT /note="Collagen-like 1"
FT DOMAIN 2802..2852
FT /note="Collagen-like 2"
FT DOMAIN 2853..2898
FT /note="Collagen-like 3"
FT DOMAIN 2941..2990
FT /note="Collagen-like 4"
FT REGION 799..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2283..2312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2451..2746
FT /note="Nonhelical region (NC3)"
FT REGION 2743..2896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2747..2898
FT /note="Triple-helical region (COL2) with 1 imperfection"
FT REGION 2899..2941
FT /note="Nonhelical region (NC2)"
FT REGION 2932..3063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2942..3044
FT /note="Triple-helical region (COL1) with 2 imperfections"
FT REGION 3045..3063
FT /note="Nonhelical region (NC1)"
FT MOTIF 862..864
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2779..2781
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2895..2897
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1078..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2297..2312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2778..2797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2824..2838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2940..2954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3018..3036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3048..3063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2944
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2947
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2950
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2959
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2965
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2968
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2971
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2983
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3000
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3003
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3014
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3023
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3026
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3029
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 25..1188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9143499"
FT /id="VSP_001149"
FT VAR_SEQ 2651..2726
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_024942"
FT VARIANT 461
FT /note="A -> P (in dbSNP:rs34730529)"
FT /id="VAR_048768"
FT VARIANT 1738
FT /note="I -> T (in dbSNP:rs240736)"
FT /evidence="ECO:0000269|PubMed:24334769"
FT /id="VAR_048769"
FT VARIANT 1965
FT /note="R -> C (in BTHLM2; unknown pathological
FT significance; dbSNP:rs200487396)"
FT /evidence="ECO:0000269|PubMed:24334769"
FT /id="VAR_074546"
FT VARIANT 2021
FT /note="R -> Q (in dbSNP:rs34438461)"
FT /id="VAR_061111"
FT VARIANT 2160
FT /note="E -> V (in dbSNP:rs35523808)"
FT /id="VAR_048770"
FT VARIANT 2334
FT /note="I -> T (in BTHLM2; dbSNP:rs796052093)"
FT /evidence="ECO:0000269|PubMed:24334604"
FT /id="VAR_074547"
FT VARIANT 2596
FT /note="I -> V (in dbSNP:rs35710072)"
FT /id="VAR_048771"
FT VARIANT 2786
FT /note="G -> D (in BTHLM2; dbSNP:rs796052094)"
FT /evidence="ECO:0000269|PubMed:24334769"
FT /id="VAR_074548"
FT VARIANT 3048
FT /note="Q -> H (in dbSNP:rs57396313)"
FT /id="VAR_061112"
FT VARIANT 3058
FT /note="G -> S (in dbSNP:rs970547)"
FT /evidence="ECO:0000269|PubMed:24334769,
FT ECO:0000269|PubMed:9143499"
FT /id="VAR_074549"
FT CONFLICT 47
FT /note="K -> E (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 441..442
FT /note="IV -> M (in Ref. 4; AAC01506)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="R -> D (in Ref. 4; AAC01506)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="S -> N (in Ref. 4; AAC01506)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="W -> S (in Ref. 4; AAC01506)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="R -> K (in Ref. 4; AAC01506)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="Y -> C (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="V -> G (in Ref. 4; AAC01506)"
FT /evidence="ECO:0000305"
FT CONFLICT 1355
FT /note="A -> D (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1690
FT /note="A -> G (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1729
FT /note="P -> A (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1949..1951
FT /note="SLD -> RLG (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2614
FT /note="P -> S (in Ref. 5; AAB23937)"
FT /evidence="ECO:0000305"
FT CONFLICT 2647..2648
FT /note="SF -> RK (in Ref. 5; AAB23937)"
FT /evidence="ECO:0000305"
FT CONFLICT 2848
FT /note="G -> S (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2858
FT /note="P -> R (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
FT CONFLICT 3035
FT /note="R -> Q (in Ref. 1; AAC51244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3063 AA; 333147 MW; EA38CAFECE8393D2 CRC64;
MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD PIVGYRITVD
PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV EESVPVIGQL TIQTGSSTKP
VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIAALVSAF DIGEEKTRVG
VVQYSSDTRT EFNLNQYYQR DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG
FPKVAIIITD GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV KLNWNPSPSP
VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY QISVSAMKGM TSSEPISIME
KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLVKSF EISPNRVQIS
LVQYSRDPHT EFTLKKFTKV EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN
VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT NWSPAGENVF
SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN VTAEYEDGFS IPLAGEETTE
EVKGAPRNLK VTDETTDSFK ITWTQAPGRV LRYRIIYRPV AGGESREVTT PPNQRRRTLE
NLIPDTKYEV SVIPEYFSGP GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK
VKQYLVTYTP VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT
TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE KNLPEDAIHT
MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK TLKVDEETEN TMRVTWKPAP
GKVVNYRVVY RPHGRGKQMV AKVPPTVTST VLKRLQPQTT YDITVLPIYK MGEGKLRQGS
GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN
TVVLEELRAG TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI
VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK
SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA RKIGVLITDG KSQDDVEAPS
KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSRIVDD LTINLCNSVK
GPGDLEAPSN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV
LKDLKPETEY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA
TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH DLTSEPVTVR
EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY KTPEEDVKEV EVDRSETSTS
LKDLFSQTLY TVSVSAVHDE GESPPVTAQE TTRPVPAPTN LKITEVTSEG FRGTWDHGAS
DVSLYRITWA PFGSSDKMET ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS
ERTLPILTTQ APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT
IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL RVYDPSTSTL
NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL RNLQPDTSYT VTVVPVYTEG
DGGRTSDTGR TLMRGLARNV QVYNPTPNSL DVRWDPAPGP VLQYRVVYSP VDGTRPSESI
VVPGNTRMVH LERLIPDTLY SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS
LSVAWDHADG PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE
DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY KPVGSNEPME
AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG TTLYLNVTDL KTYQIGWDTF
CVKWSPHRAA TSYRLKLSPA DGTRGQEITV RGSETSHCFT GLSPDTDYGV TVFVQTPNLE
GPGVSVKEHT TVKPTEAPTE PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN
KVVKFIFNTV GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN
TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ SGFSVFVVGV
ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV CETATSSCPL IYLDGYTSPG
FKMLEAYNLT EKNFASVQGV SLESGSFPSY SAYRIQKNAF VNQPTADLHP NGLPPSYTII
LLFRLLPETP SDPFAIWQIT DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV
KTLFYGSFHK VHIVVTSKSV KIYIDCYEII EKDIKEAGNI TTDGYEILGK LLKGERKSAA
FQIQSFDIVC SPVWTSRDRC CDIPSRRDEG KCPAFPNSCT CTQDSVGPPG PPGPAGGPGA
KGPRGERGIS GAIGPPGPRG DIGPPGPQGP PGPQGPNGLS IPGEQGRQGM KGDAGEPGLP
GRTGTPGLPG PPGPMGPPGD RGFTGKDGAM GPRGPPGPPG SPGSPGVTGP SGKPGKPGDH
GRPGPSGLKG EKGDRGDIAS QNMMRAVARQ VCEQLISGQM NRFNQMLNQI PNDYQSSRNQ
PGPPGPPGPP GSAGARGEPG PGGRPGFPGT PGMQGPPGER GLPGEKGERG TGSSGPRGLP
GPPGPQGESR TGPPGSTGSR GPPGPPGRPG NSGIRGPPGP PGYCDSSQCA SIPYNGQGYP
GSG
