ID COJA1_HUMAN Reviewed; 1142 AA. AC Q14993; Q00559; Q05850; Q12885; Q13676; Q14DH1; Q5JUF0; Q5T424; AC Q9H572; Q9NPZ2; Q9NQP2; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 3. DT 16-OCT-2013, entry version 127. DE RecName: Full=Collagen alpha-1(XIX) chain; DE AltName: Full=Collagen alpha-1(Y) chain; DE Flags: Precursor; GN Name=COL19A1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7775380; RA Inoguchi K., Yoshioka H., Khaleduzzaman M., Ninomiya Y.; RT "The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, RT contains a long unusual 3' untranslated region and displays many RT unique splicing variants."; RL J. Biochem. 117:137-146(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9344653; DOI=10.1006/geno.1997.4921; RA Khaleduzzaman M., Sumiyoshi H., Ueki Y., Inoguchi K., Ninomiya Y., RA Yoshioka H.; RT "Structure of the human type XIX collagen (COL19A1) gene, which RT suggests it has arisen from an ancestor gene of the FACIT family."; RL Genomics 45:304-312(1997). RN [3] 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-624. RC TISSUE=Rhabdomyosarcoma; RX PubMed=1639419; DOI=10.1016/0888-7543(92)90176-S; RA Yoshioka H., Zhang H., Ramirez F., Mattei M.-G., Moradi-Ameli M., RA van der Rest M., Gordon M.K.; RT "Synteny between the loci for a novel FACIT-like collagen locus RT (D6S228E) and alpha 1 (IX) collagen (COL9A1) on 6q12-q14 in humans."; RL Genomics 13:884-886(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-1020. RX PubMed=7916703; DOI=10.1016/0378-1119(93)90126-N; RA Myers J.C., Sun M.J., D'Ippolito J.A., Jabs E.W., Neilson E.G., RA Dion A.S.; RT "Human cDNA clones transcribed from an unusually high-molecular-weight RT RNA encode a new collagen chain."; RL Gene 123:211-217(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 738-1142. RC TISSUE=Skin; RX PubMed=8034603; RA Myers J.C., Yang H., D'Ippolito J.A., Presente A., Miller M.K., RA Dion A.S.; RT "The triple-helical region of human type XIX collagen consists of RT multiple collagenous subdomains and exhibits limited sequence homology RT to alpha 1(XVI)."; RL J. Biol. Chem. 269:18549-18557(1994). RN [8] RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DOMAIN. RX PubMed=12788917; DOI=10.1074/jbc.M304629200; RA Myers J.C., Li D., Amenta P.S., Clark C.C., Nagaswami C., Weisel J.W.; RT "Type XIX collagen purified from human umbilical cord is characterized RT by multiple sharp kinks delineating collagenous subdomains and by RT intermolecular aggregates via globular, disulfide-linked, and heparin- RT binding amino termini."; RL J. Biol. Chem. 278:32047-32057(2003). RN [9] RP VARIANTS [LARGE SCALE ANALYSIS] ASP-361 AND ASN-1019. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: May act as a cross-bridge between fibrils and other CC extracellular matrix molecules. Involved in skeletal myogenesis in CC the developing esophagus. May play a role in organization of the CC pericellular matrix or the sphinteric smooth muscle. CC -!- SUBUNIT: Oligomer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix (By similarity). CC -!- TISSUE SPECIFICITY: Localized to vascular, neuronal, mesenchymal, CC and some epithelial basement membrane zones in umbilical cord. CC -!- DOMAIN: The numerous interruptions in the triple helix may make CC this molecule either elastic or flexible. CC -!- PTM: Prolines at the third position of the tripeptide repeating CC unit (G-X-Y) are hydroxylated in some or all of the chains. CC -!- SIMILARITY: Belongs to the fibril-associated collagens with CC interrupted helices (FACIT) family. CC -!- SIMILARITY: Contains 11 collagen-like domains. CC -!- SIMILARITY: Contains 1 laminin G-like domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAC12699.3; Type=Erroneous gene model prediction; CC Sequence=CAI42319.2; Type=Erroneous gene model prediction; CC Sequence=CAI42496.2; Type=Erroneous gene model prediction; 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; D38163; BAA07368.1; -; mRNA. DR EMBL; AB004629; BAA23309.1; -; Genomic_DNA. DR EMBL; AL118519; CAB99331.2; -; Genomic_DNA. DR EMBL; AL133388; CAI42496.2; ALT_SEQ; Genomic_DNA. DR EMBL; AL136445; CAI42496.2; JOINED; Genomic_DNA. DR EMBL; AL160262; CAI42496.2; JOINED; Genomic_DNA. DR EMBL; AL133388; CAI42497.1; -; Genomic_DNA. DR EMBL; AL118519; CAI42497.1; JOINED; Genomic_DNA. DR EMBL; AL136445; CAI42497.1; JOINED; Genomic_DNA. DR EMBL; AL359539; CAI42497.1; JOINED; Genomic_DNA. DR EMBL; AL160262; CAI42497.1; JOINED; Genomic_DNA. DR EMBL; AL136445; CAC12699.3; ALT_SEQ; Genomic_DNA. DR EMBL; AL133388; CAC12699.3; JOINED; Genomic_DNA. DR EMBL; AL160262; CAC12699.3; JOINED; Genomic_DNA. DR EMBL; AL136445; CAI42716.1; -; Genomic_DNA. DR EMBL; AL118519; CAI42716.1; JOINED; Genomic_DNA. DR EMBL; AL133388; CAI42716.1; JOINED; Genomic_DNA. DR EMBL; AL160262; CAI42716.1; JOINED; Genomic_DNA. DR EMBL; AL359539; CAI42716.1; JOINED; Genomic_DNA. DR EMBL; AL160262; CAI42319.2; ALT_SEQ; Genomic_DNA. DR EMBL; AL133388; CAI42319.2; JOINED; Genomic_DNA. DR EMBL; AL136445; CAI42319.2; JOINED; Genomic_DNA. DR EMBL; AL160262; CAI42322.1; -; Genomic_DNA. DR EMBL; AL118519; CAI42322.1; JOINED; Genomic_DNA. DR EMBL; AL133388; CAI42322.1; JOINED; Genomic_DNA. DR EMBL; AL136445; CAI42322.1; JOINED; Genomic_DNA. DR EMBL; AL359539; CAI42322.1; JOINED; Genomic_DNA. DR EMBL; AL359539; CAI16492.1; -; Genomic_DNA. DR EMBL; AL118519; CAI16492.1; JOINED; Genomic_DNA. DR EMBL; AL133388; CAI16492.1; JOINED; Genomic_DNA. DR EMBL; AL136445; CAI16492.1; JOINED; Genomic_DNA. DR EMBL; AL160262; CAI16492.1; JOINED; Genomic_DNA. DR EMBL; BC113362; AAI13363.1; -; mRNA. DR EMBL; BC113364; AAI13365.1; -; mRNA. DR EMBL; M63597; AAA58468.1; -; mRNA. DR EMBL; L12347; AAA36358.1; -; mRNA. DR EMBL; U09279; AAA21146.1; -; mRNA. DR EMBL; AH000850; AAA21147.1; -; Genomic_DNA. DR IPI; IPI00019090; -. DR PIR; JX0369; JX0369. DR RefSeq; NP_001849.2; NM_001858.4. DR UniGene; Hs.444842; -. DR ProteinModelPortal; Q14993; -. DR SMR; Q14993; 51-245. DR PhosphoSite; Q14993; -. DR DMDM; 68840003; -. DR PaxDb; Q14993; -. DR PRIDE; Q14993; -. DR Ensembl; ENST00000322773; ENSP00000316030; ENSG00000082293. DR GeneID; 1310; -. DR KEGG; hsa:1310; -. DR UCSC; uc003pfc.1; human. DR CTD; 1310; -. DR GeneCards; GC06P070633; -. DR HGNC; HGNC:2196; COL19A1. DR HPA; HPA042422; -. DR MIM; 120165; gene. DR neXtProt; NX_Q14993; -. DR PharmGKB; PA26712; -. DR eggNOG; NOG275976; -. DR HOVERGEN; HBG060240; -. DR InParanoid; Q14993; -. DR OMA; ERWFLWQ; -. DR OrthoDB; EOG41JZCF; -. DR PhylomeDB; Q14993; -. DR Reactome; REACT_118779; Extracellular matrix organization. DR ChiTaRS; COL19A1; human. DR GeneWiki; Collagen,_type_XIX,_alpha_1; -. DR GenomeRNAi; 1310; -. DR NextBio; 5357; -. DR PRO; PR:Q14993; -. DR ArrayExpress; Q14993; -. DR Bgee; Q14993; -. DR Genevestigator; Q14993; -. DR GO; GO:0005581; C:collagen; NAS:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. DR GO; GO:0030674; F:protein binding, bridging; NAS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0016337; P:cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0030574; P:collagen catabolic process; TAS:Reactome. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR008985; ConA-like_lec_gl_sf. DR InterPro; IPR013320; ConA-like_subgrp. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF01391; Collagen; 11. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; SSF49899; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; FALSE_NEG. PE 1: Evidence at protein level; KW Cell adhesion; Collagen; Complete proteome; Developmental protein; KW Differentiation; Disulfide bond; Extracellular matrix; Hydroxylation; KW Myogenesis; Polymorphism; Reference proteome; Repeat; Secreted; KW Signal. FT SIGNAL 1 23 Potential. FT CHAIN 24 1142 Collagen alpha-1(XIX) chain. FT /FTId=PRO_0000005797. FT DOMAIN 50 234 Laminin G-like. FT DOMAIN 292 349 Collagen-like 1. FT DOMAIN 350 391 Collagen-like 2. FT DOMAIN 392 433 Collagen-like 3. FT DOMAIN 474 516 Collagen-like 4. FT DOMAIN 568 624 Collagen-like 5. FT DOMAIN 626 678 Collagen-like 6. FT DOMAIN 728 778 Collagen-like 7. FT DOMAIN 779 814 Collagen-like 8. FT DOMAIN 845 903 Collagen-like 9. FT DOMAIN 904 947 Collagen-like 10. FT DOMAIN 948 1004 Collagen-like 11. FT REGION 292 351 Triple-helical region 1 (COL1). FT REGION 370 429 Triple-helical region 2 (COL2). FT REGION 448 688 Triple-helical region 3 (COL3). FT REGION 700 818 Triple-helical region 4 (COL4). FT REGION 833 1012 Triple-helical region 5 (COL5). FT REGION 1054 1111 Triple-helical region 6 (COL6). FT MOTIF 952 954 Cell attachment site (Potential). FT VARIANT 352 352 A -> G (in dbSNP:rs2273426). FT /FTId=VAR_024419. FT VARIANT 361 361 G -> D (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035746. FT VARIANT 406 406 G -> E (in dbSNP:rs13204209). FT /FTId=VAR_048782. FT VARIANT 496 496 E -> G (in dbSNP:rs13204209). FT /FTId=VAR_048783. FT VARIANT 1019 1019 K -> N (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035747. FT CONFLICT 89 89 I -> MY (in Ref. 2; BAA23309). FT CONFLICT 106 119 FRVRRNAKKERWFL -> ETTVPFWRFFVLET (in Ref. FT 6; AAA36358). FT CONFLICT 279 279 Q -> L (in Ref. 1; BAA07368). FT CONFLICT 354 355 AG -> GC (in Ref. 5; AAA58468). FT CONFLICT 365 365 D -> V (in Ref. 1; BAA07368 and 5; FT AAA58468). FT CONFLICT 441 442 YY -> DD (in Ref. 1; BAA07368 and 5; FT AAA58468). FT CONFLICT 622 624 PQG -> QRD (in Ref. 5; AAA58468). FT CONFLICT 816 823 GIPFNERN -> VSCSRLKI (in Ref. 6; FT AAA36358). FT CONFLICT 937 937 Q -> E (in Ref. 1; BAA07368). FT CONFLICT 1140 1140 G -> C (in Ref. 2; BAA23309). SQ SEQUENCE 1142 AA; 115221 MW; F1153CE751387943 CRC64; MRLTGPWKLW LWMSIFLLPA STSVTVRDKT EESCPILRIE GHQLTYDNIN KLEVSGFDLG DSFSLRRAFC ESDKTCFKLG SALLIRDTIK IFPKGLPEEY SVAAMFRVRR NAKKERWFLW QVLNQQNIPQ ISIVVDGGKK VVEFMFQATE GDVLNYIFRN RELRPLFDRQ WHKLGISIQS QVISLYMDCN LIARRQTDEK DTVDFHGRTV IATRASDGKP VDIELHQLKI YCSANLIAQE TCCEISDTKC PEQDGFGNIA SSWVTAHASK MSSYLPAKQE LKDQCQCIPN KGEAGLPGAP GSPGQKGHKG EPGENGLHGA PGFPGQKGEQ GFEGSKGETG EKGEQGEKGD PALAGLNGEN GLKGDLGPHG PPGPKGEKGD TGPPGPPALP GSLGIQGPQG PPGKEGQRGR RGKTGPPGKP GPPGPPGPPG IQGIHQTLGG YYNKDNKGND EHEAGGLKGD KGETGLPGFP GSVGPKGQKG EPGEPFTKGE KGDRGEPGVI GSQGVKGEPG DPGPPGLIGS PGLKGQQGSA GSMGPRGPPG DVGLPGEHGI PGKQGIKGEK GDPGGIIGPP GLPGPKGEAG PPGKSLPGEP GLDGNPGAPG PRGPKGERGL PGVHGSPGDI GPQGIGIPGR TGAQGPAGEP GIQGPRGLPG LPGTPGTPGN DGVPGRDGKP GLPGPPGDPI ALPLLGDIGA LLKNFCGNCQ ASVPGLKSNK GEEGGAGEPG KYDSMARKGD IGPRGPPGIP GREGPKGSKG ERGYPGIPGE KGDEGLQGIP GIPGAPGPTG PPGLMGRTGH PGPTGAKGEK GSDGPPGKPG PPGPPGIPFN ERNGMSSLYK IKGGVNVPSY PGPPGPPGPK GDPGPVGEPG AMGLPGLEGF PGVKGDRGPA GPPGIAGMSG KPGAPGPPGV PGEPGERGPV GDIGFPGPEG PSGKPGINGK DGIPGAQGIM GKPGDRGPKG ERGDQGIPGD RGSQGERGKP GLTGMKGAIG PMGPPGNKGS MGSPGHQGPP GSPGIPGIPA DAVSFEEIKK YINQEVLRIF EERMAVFLSQ LKLPAAMLAA QAYGRPGPPG KDGLPGPPGD PGPQGYRGQK GERGEPGIGL PGSPGLPGTS ALGLPGSPGA PGPQGPPGPS GRCNPEDCLY PVSHAHQRTG GN //