ID COJA1_MOUSE Reviewed; 1136 AA.
AC Q0VF58; O35053;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Collagen alpha-1(XIX) chain;
DE AltName: Full=Collagen alpha-1(Y) chain;
DE Flags: Precursor;
GN Name=Col19a1 {ECO:0000312|MGI:MGI:1095415};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA23578.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAA23578.1};
RX PubMed=9202028; DOI=10.1074/jbc.272.27.17104;
RA Sumiyoshi H., Inoguchi K., Khaleduzzaman M., Ninomiya Y., Yoshioka H.;
RT "Ubiquitous expression of the alpha1(XIX) collagen gene (Col19a1) during
RT mouse embryogenesis becomes restricted to a few tissues in the adult
RT organism.";
RL J. Biol. Chem. 272:17104-17111(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAI18971.1}
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 [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=11169848;
RX DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1099>3.0.co;2-w;
RA Sumiyoshi H., Laub F., Yoshioka H., Ramirez F.;
RT "Embryonic expression of type XIX collagen is transient and confined to
RT muscle cells.";
RL Dev. Dyn. 220:155-162(2001).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15302855; DOI=10.1083/jcb.200402054;
RA Sumiyoshi H., Mor N., Lee S.Y., Doty S., Henderson S., Tanaka S.,
RA Yoshioka H., Rattan S., Ramirez F.;
RT "Esophageal muscle physiology and morphogenesis require assembly of a
RT collagen XIX-rich basement membrane zone.";
RL J. Cell Biol. 166:591-600(2004).
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:15302855, ECO:0000305}.
CC -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000250|UniProtKB:Q14993}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the myotome of somites from 9.5 dpc.
CC In muscular tissues, expression is transient and is confined to a few
CC sites of the developing embryo, such as limbs, tongue, and smooth
CC muscle layers of stomach and esophagus. Also detected in skin at 16.5
CC dpc and in cerebral cortex and hippocampus of the newborn brain. In
CC adult, expression is only observed in cerebrum, cerebellum, eyes, and
CC testis. In CNS, expression gradually increases following birth. Also
CC expressed in embryonic fibroblasts and to a lesser extent in adult
CC fibroblasts. {ECO:0000269|PubMed:11169848, ECO:0000269|PubMed:9202028}.
CC -!- DOMAIN: The numerous interruptions in the triple helix may make this
CC molecule either elastic or flexible. {ECO:0000250|UniProtKB:Q14993}.
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. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mice show severe signs of malnourishment and the
CC majority die within the first three weeks of postnatal life. Newborn
CC homozygotes do not show gross anatomical abnormalities, except for
CC smaller size of the internal organs. However, necroscopy of the mice
CC that survive past the weaning stage reveals a dilated esophagus
CC (megaesophagus) with retention of ingesta immediately above the
CC diaphragm level. Mutant mice also exhibit an additional defect, namely
CC impaired smooth-to-skeletal muscle cell transdifferentiation in the
CC abdominal segment of the esophagus. Heterozygotes by comparison are
CC morphologically normal, viable and fertile.
CC {ECO:0000269|PubMed:15302855}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000255}.
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DR EMBL; AB000636; BAA23578.1; -; mRNA.
DR EMBL; AC116998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118970; AAI18971.1; -; mRNA.
DR CCDS; CCDS14854.1; -.
DR RefSeq; NP_031759.2; NM_007733.2.
DR RefSeq; XP_006495708.1; XM_006495645.3.
DR AlphaFoldDB; Q0VF58; -.
DR ComplexPortal; CPX-3002; Collagen type XIX trimer.
DR STRING; 10090.ENSMUSP00000110899; -.
DR GlyCosmos; Q0VF58; 1 site, No reported glycans.
DR GlyGen; Q0VF58; 1 site.
DR iPTMnet; Q0VF58; -.
DR PhosphoSitePlus; Q0VF58; -.
DR PaxDb; 10090-ENSMUSP00000110899; -.
DR ProteomicsDB; 283490; -.
DR Antibodypedia; 31201; 222 antibodies from 27 providers.
DR DNASU; 12823; -.
DR Ensembl; ENSMUST00000115244.9; ENSMUSP00000110899.3; ENSMUSG00000026141.14.
DR GeneID; 12823; -.
DR KEGG; mmu:12823; -.
DR UCSC; uc007amq.1; mouse.
DR AGR; MGI:1095415; -.
DR CTD; 1310; -.
DR MGI; MGI:1095415; Col19a1.
DR VEuPathDB; HostDB:ENSMUSG00000026141; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000158276; -.
DR HOGENOM; CLU_282267_0_0_1; -.
DR InParanoid; Q0VF58; -.
DR OMA; FMFQATE; -.
DR OrthoDB; 3809795at2759; -.
DR PhylomeDB; Q0VF58; -.
DR TreeFam; TF351778; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12823; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Col19a1; mouse.
DR PRO; PR:Q0VF58; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q0VF58; Protein.
DR Bgee; ENSMUSG00000026141; Expressed in head bone and 131 other cell types or tissues.
DR ExpressionAtlas; Q0VF58; baseline and differential.
DR Genevisible; Q0VF58; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF938; COLLAGEN ALPHA-1(XIX) CHAIN; 1.
DR Pfam; PF01391; Collagen; 11.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Collagen; Developmental protein; Differentiation;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Myogenesis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1136
FT /note="Collagen alpha-1(XIX) chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000284731"
FT DOMAIN 47..231
FT /note="Laminin G-like"
FT DOMAIN 292..346
FT /note="Collagen-like 1"
FT DOMAIN 347..388
FT /note="Collagen-like 2"
FT DOMAIN 389..430
FT /note="Collagen-like 3"
FT DOMAIN 519..577
FT /note="Collagen-like 4"
FT DOMAIN 578..618
FT /note="Collagen-like 5"
FT DOMAIN 620..673
FT /note="Collagen-like 6"
FT DOMAIN 722..777
FT /note="Collagen-like 7"
FT DOMAIN 778..810
FT /note="Collagen-like 8"
FT DOMAIN 833..891
FT /note="Collagen-like 9"
FT REGION 252..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..348
FT /note="Triple-helical region 1 (COL1)"
FT /evidence="ECO:0000255"
FT REGION 367..426
FT /note="Triple-helical region 2 (COL2)"
FT /evidence="ECO:0000255"
FT REGION 442..682
FT /note="Triple-helical region 3 (COL3)"
FT /evidence="ECO:0000255"
FT REGION 694..812
FT /note="Triple-helical region 4 (COL4)"
FT /evidence="ECO:0000255"
FT REGION 699..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..1006
FT /note="Triple-helical region 5 (COL5)"
FT /evidence="ECO:0000255"
FT REGION 1043..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1105
FT /note="Triple-helical region 6 (COL6)"
FT /evidence="ECO:0000255"
FT MOTIF 946..948
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 252..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 110
FT /note="K -> Q (in Ref. 1; BAA23578)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="D -> N (in Ref. 1; BAA23578 and 3; AAI18971)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="G -> K (in Ref. 1; BAA23578)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="G -> E (in Ref. 1; BAA23578)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="D -> E (in Ref. 1; BAA23578 and 3; AAI18971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1136 AA; 114197 MW; C480216027D70B43 CRC64;
MRHTGSWKLW TWVTTFLLPA CTCLTVRDKP ETTCPTLRTE RYQDDRNKSE LSGFDLGESF
ALRHAFCEGD KTCFKLGSVL LIRDTVKIFP KGLPEEYAIA VMFRVRRSTK KERWFLWKIL
NQQNMAQISV VIDGTKKVVE FMFRGAEGDL LNYVFKNREL RPLFDRQWHK LGIGVQSRVL
SLYMDCNLIA SRHTEEKNSV DFQGRTIIAA RASDGKPVDI ELHQLRIYCN ANFLAEESCC
NLSPTKCPEQ DDFGSTTSSW GTSNTGKMSS YLPGKQELKD TCQCIPNKEE AGLPGTLRSI
GHKGDKGEPG EHGLDGTPGL PGQKGEQGLE GIKGEIGEKG EPGAKGDSGL DGLNGQDGLK
GDSGPQGPPG PKGDKGDMGP PGPPALTGSI GIQGPQGPPG KEGQRGRRGK TGPPGNPGPP
GPPGPPGLQG LQQPFGGYFN KGTGEHGASG PKGEKGDTGL PGFPGSVGPK GHKGEPGEPL
TKGEKGDRGE PGLLGPQGIK GEPGDPGPPG LLGSPGLKGQ QGPAGSMGPR GPPGDVGLPG
EHGIPGKQGV KGEKGDPGGR LGPPGLPGLK GDAGPPGISL PGKPGLDGNP GSPGPRGPKG
ERGLPGLHGS PGDTGPPGVG IPGRTGSQGP AGEPGIQGPR GLPGLPGTPG MPGNDGAPGK
DGKPGLPGPP GDPIALPLLG DIGALLKNFC GNCQANVPGL KSIKGDDGST GEPGKYDPAA
RKGDVGPRGP PGFPGREGPK GSKGERGYPG IHGEKGDEGL QGIPGLSGAP GPTGPPGLTG
RTGHPGPTGA KGDKGSEGPP GKPGPPGPPG VPLNEGNGMS SLYKIQGGVN VPGYPGPPGP
PGPKGDPGPV GEPGAMGLPG LEGFPGVKGD RGPAGPPGIA GISGKPGAPG PPGVPGEQGE
RGPIGDTGFP GPEGPSGKPG INGKDGLPGA QGIMGKPGDR GPKGERGDQG IPGDRGPQGE
RGKPGLTGMK GAIGPVGPAG SKGSTGPPGH QGPPGNPGIP GTPADAVSFE EIKHYINQEV
LRIFEERMAV FLSQLKLPAA MLSAQAHGRP GPPGKDGLPG PPGDPGPQGY RGQKGERGEP
GIGLPGSPGL PGSSAVGLPG SPGAPGPQGP PGPSGRCNPE DCLYPAPPPH QQAGGK
//
