COJA1_HUMAN
ID COJA1_HUMAN Reviewed; 1142 AA.
AC Q14993; Q00559; Q05850; Q12885; Q13676; Q14DH1; Q5JUF0; Q5T424; Q9H572;
AC Q9NPZ2; Q9NQP2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 188.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7775380; DOI=10.1093/oxfordjournals.jbchem.a124700;
RA Inoguchi K., Yoshioka H., Khaleduzzaman M., Ninomiya Y.;
RT "The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains
RT a long unusual 3' untranslated region and displays many unique splicing
RT 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 suggests it
RT 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., 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 [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 project:
RT 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 (D6S228E)
RT 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., Dion A.S.;
RT "Human cDNA clones transcribed from an unusually high-molecular-weight RNA
RT 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; DOI=10.1016/s0021-9258(17)32344-x;
RA Myers J.C., Yang H., D'Ippolito J.A., Presente A., Miller M.K., Dion A.S.;
RT "The triple-helical region of human type XIX collagen consists of multiple
RT collagenous subdomains and exhibits limited sequence homology to alpha
RT 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 by
RT 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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal 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 the
CC developing esophagus. May play a role in organization of the
CC pericellular matrix or the sphinteric smooth muscle.
CC {ECO:0000269|PubMed:12788917}.
CC -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000269|PubMed:12788917}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Localized to vascular, neuronal, mesenchymal, and
CC some epithelial basement membrane zones in umbilical cord.
CC {ECO:0000269|PubMed:12788917}.
CC -!- DOMAIN: The numerous interruptions in the triple helix may make this
CC molecule either elastic or flexible. {ECO:0000269|PubMed:12788917}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; D38163; BAA07368.1; -; mRNA.
DR EMBL; AB004629; BAA23309.1; -; Genomic_DNA.
DR EMBL; AL118519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359539; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS4970.1; -.
DR PIR; JX0369; JX0369.
DR RefSeq; NP_001849.2; NM_001858.5.
DR RefSeq; XP_011533740.1; XM_011535438.2.
DR RefSeq; XP_016865744.1; XM_017010255.1.
DR AlphaFoldDB; Q14993; -.
DR BioGRID; 107705; 1.
DR ComplexPortal; CPX-1760; Collagen type XIX trimer.
DR IntAct; Q14993; 1.
DR STRING; 9606.ENSP00000480474; -.
DR iPTMnet; Q14993; -.
DR PhosphoSitePlus; Q14993; -.
DR BioMuta; COL19A1; -.
DR DMDM; 68840003; -.
DR jPOST; Q14993; -.
DR MassIVE; Q14993; -.
DR PaxDb; Q14993; -.
DR PeptideAtlas; Q14993; -.
DR PRIDE; Q14993; -.
DR ProteomicsDB; 60277; -.
DR Antibodypedia; 31201; 201 antibodies from 26 providers.
DR DNASU; 1310; -.
DR Ensembl; ENST00000620364.5; ENSP00000480474.1; ENSG00000082293.13.
DR GeneID; 1310; -.
DR KEGG; hsa:1310; -.
DR MANE-Select; ENST00000620364.5; ENSP00000480474.1; NM_001858.6; NP_001849.2.
DR UCSC; uc032xam.2; human.
DR CTD; 1310; -.
DR DisGeNET; 1310; -.
DR GeneCards; COL19A1; -.
DR HGNC; HGNC:2196; COL19A1.
DR HPA; ENSG00000082293; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 120165; gene.
DR neXtProt; NX_Q14993; -.
DR OpenTargets; ENSG00000082293; -.
DR PharmGKB; PA26712; -.
DR VEuPathDB; HostDB:ENSG00000082293; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000158276; -.
DR HOGENOM; CLU_282267_0_0_1; -.
DR InParanoid; Q14993; -.
DR OMA; FMFQATE; -.
DR OrthoDB; 1295141at2759; -.
DR PhylomeDB; Q14993; -.
DR TreeFam; TF351778; -.
DR PathwayCommons; Q14993; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q14993; -.
DR BioGRID-ORCS; 1310; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; COL19A1; human.
DR GeneWiki; Collagen,_type_XIX,_alpha_1; -.
DR GenomeRNAi; 1310; -.
DR Pharos; Q14993; Tbio.
DR PRO; PR:Q14993; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q14993; protein.
DR Bgee; ENSG00000082293; Expressed in mucosa of stomach and 110 other tissues.
DR ExpressionAtlas; Q14993; baseline and differential.
DR Genevisible; Q14993; HS.
DR GO; GO:0005581; C:collagen trimer; TAS:ProtInc.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01391; Collagen; 10.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Collagen; Developmental protein; Differentiation;
KW Disulfide bond; Extracellular matrix; Hydroxylation; Myogenesis;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1142
FT /note="Collagen alpha-1(XIX) chain"
FT /id="PRO_0000005797"
FT DOMAIN 50..234
FT /note="Laminin G-like"
FT DOMAIN 292..349
FT /note="Collagen-like 1"
FT DOMAIN 350..391
FT /note="Collagen-like 2"
FT DOMAIN 392..433
FT /note="Collagen-like 3"
FT DOMAIN 474..516
FT /note="Collagen-like 4"
FT DOMAIN 568..624
FT /note="Collagen-like 5"
FT DOMAIN 626..678
FT /note="Collagen-like 6"
FT DOMAIN 728..778
FT /note="Collagen-like 7"
FT DOMAIN 779..814
FT /note="Collagen-like 8"
FT DOMAIN 845..903
FT /note="Collagen-like 9"
FT DOMAIN 904..947
FT /note="Collagen-like 10"
FT DOMAIN 948..1004
FT /note="Collagen-like 11"
FT REGION 288..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..351
FT /note="Triple-helical region 1 (COL1)"
FT REGION 370..429
FT /note="Triple-helical region 2 (COL2)"
FT REGION 448..688
FT /note="Triple-helical region 3 (COL3)"
FT REGION 700..818
FT /note="Triple-helical region 4 (COL4)"
FT REGION 704..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..1012
FT /note="Triple-helical region 5 (COL5)"
FT REGION 1053..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1111
FT /note="Triple-helical region 6 (COL6)"
FT MOTIF 952..954
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 352
FT /note="A -> G (in dbSNP:rs2273426)"
FT /id="VAR_024419"
FT VARIANT 361
FT /note="G -> D (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1313704586)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035746"
FT VARIANT 406
FT /note="G -> E (in dbSNP:rs13204209)"
FT /id="VAR_048782"
FT VARIANT 496
FT /note="E -> G (in dbSNP:rs13204209)"
FT /id="VAR_048783"
FT VARIANT 1019
FT /note="K -> N (in a breast cancer sample; somatic mutation;
FT dbSNP:rs771562232)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035747"
FT CONFLICT 89
FT /note="I -> MY (in Ref. 2; BAA23309)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..119
FT /note="FRVRRNAKKERWFL -> ETTVPFWRFFVLET (in Ref. 6;
FT AAA36358)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Q -> L (in Ref. 1; BAA07368)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..355
FT /note="AG -> GC (in Ref. 5; AAA58468)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> V (in Ref. 1; BAA07368 and 5; AAA58468)"
FT /evidence="ECO:0000305"
FT CONFLICT 441..442
FT /note="YY -> DD (in Ref. 1; BAA07368 and 5; AAA58468)"
FT /evidence="ECO:0000305"
FT CONFLICT 622..624
FT /note="PQG -> QRD (in Ref. 5; AAA58468)"
FT /evidence="ECO:0000305"
FT CONFLICT 816..823
FT /note="GIPFNERN -> VSCSRLKI (in Ref. 6; AAA36358)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="Q -> E (in Ref. 1; BAA07368)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="G -> C (in Ref. 2; BAA23309)"
FT /evidence="ECO:0000305"
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
