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-NOV-2024, entry version 217. 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 congenital muscular dystrophy, a disease CC characterized by generalized muscle weakness and striking hypermobility CC of distal joints in conjunction with variable contractures of more CC proximal joints and normal intelligence. Additional findings may CC include kyphoscoliosis, protruded calcanei, and follicular CC hyperkeratosis (rough skin). More severely affected patients manifest CC at birth and never achieve independent ambulation, while patients with CC milder phenotypes might maintain ambulation into adulthood. UCMD2 is a CC severe, autosomal recessive form with onset at birth. CC {ECO:0000269|PubMed:24334604}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Bethlem myopathy 2 (BTHLM2) [MIM:616471]: A form of Bethlem CC myopathy, a slowly progressive muscular dystrophy characterized by CC joint contractures, most frequently affecting the elbows and ankles, CC and muscle weakness and wasting involving the proximal and extensor CC muscles more than the distal and flexor ones. The clinical onset more CC often occurs in childhood or adulthood, but it can be prenatal with CC decreased fetal movements or neonatal with hypotonia. The hallmark of CC Bethlem myopathy is long finger flexion contractures. BTHLM2 CC inheritance is autosomal dominant. {ECO:0000269|PubMed:24334604, CC ECO:0000269|PubMed:24334769}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted CC helices (FACIT) family. {ECO:0000305}. 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; 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; 74. DR ComplexPortal; CPX-1753; Collagen type XII trimer. DR IntAct; Q99715; 38. DR STRING; 9606.ENSP00000325146; -. DR GlyConnect; 1131; 70 N-Linked glycans (4 sites). DR GlyCosmos; Q99715; 13 sites, 90 glycans. DR GlyGen; Q99715; 25 sites, 120 N-linked glycans (4 sites), 10 O-linked glycans (16 sites). DR iPTMnet; Q99715; -. DR PhosphoSitePlus; Q99715; -. DR BioMuta; COL12A1; -. DR DMDM; 146345397; -. DR jPOST; Q99715; -. DR MassIVE; 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; 93 antibodies from 19 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 FunFam; 2.60.40.10:FF:000018; collagen alpha-1(XII) chain isoform X1; 8. DR FunFam; 2.60.40.10:FF:000489; collagen alpha-1(XII) chain isoform X1; 1. DR FunFam; 2.60.40.10:FF:000554; collagen alpha-1(XII) chain isoform X1; 1. DR FunFam; 2.60.40.10:FF:000639; collagen alpha-1(XII) chain isoform X1; 1. DR FunFam; 2.60.40.10:FF:000704; collagen alpha-1(XII) chain isoform X1; 1. DR FunFam; 2.60.40.10:FF:000816; collagen alpha-1(XII) chain isoform X2; 1. DR FunFam; 2.60.120.200:FF:000008; Collagen type XII alpha 1 chain; 1. DR FunFam; 2.60.40.10:FF:000121; Collagen type XII alpha 1 chain; 4. DR FunFam; 2.60.40.10:FF:000480; Collagen, type XII, alpha 1; 1. DR FunFam; 3.40.50.410:FF:000001; Collagen, type XII, alpha 1; 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; IPR050525; ECM_Assembly_Org. 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. 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; Proteomics identification; Reference proteome; Repeat; KW 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 //