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   27-MAR-2024, entry version 213.
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).
RN   [11]
RP   GLYCOSYLATION AT SER-329.
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).
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; 72.
DR   ComplexPortal; CPX-1753; Collagen type XII trimer.
DR   IntAct; Q99715; 10.
DR   STRING; 9606.ENSP00000325146; -.
DR   GlyConnect; 1131; 70 N-Linked glycans (4 sites).
DR   GlyCosmos; Q99715; 13 sites, 90 glycans.
DR   GlyGen; Q99715; 23 sites, 82 N-linked glycans (4 sites), 10 O-linked glycans (14 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; 9606-ENSP00000325146; -.
DR   PeptideAtlas; Q99715; -.
DR   ProteomicsDB; 78429; -. [Q99715-1]
DR   ProteomicsDB; 78430; -. [Q99715-2]
DR   ProteomicsDB; 78431; -. [Q99715-4]
DR   Pumba; Q99715; -.
DR   Antibodypedia; 2124; 113 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   AGR; HGNC:2188; -.
DR   CTD; 1303; -.
DR   DisGeNET; 1303; -.
DR   GeneCards; COL12A1; -.
DR   HGNC; HGNC:2188; COL12A1.
DR   HPA; ENSG00000111799; Low tissue specificity.
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 muscular dystrophy.
DR   Orphanet; 536516; Myopathic Ehlers-Danlos syndrome.
DR   Orphanet; 75840; Ullrich congenital muscular dystrophy.
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; WKRPPDE; -.
DR   OrthoDB; 5353225at2759; -.
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 1148 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 172 other cell types or tissues.
DR   ExpressionAtlas; Q99715; baseline and differential.
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   CDD; cd01482; vWA_collagen_alphaI-XII-like; 4.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 18.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; IPR048287; TSPN-like_N.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF70; PH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   Pfam; PF00041; fn3; 18.
DR   Pfam; PF00092; VWA; 4.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00060; FN3; 18.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00327; VWA; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 11.
DR   SUPFAM; SSF53300; vWA-like; 4.
DR   PROSITE; PS50853; FN3; 18.
DR   PROSITE; PS50234; VWFA; 4.
DR   Genevisible; Q99715; HS.
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        329
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:32337544"
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; uncertain significance;
FT                   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
//