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   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.
DR   Genevisible; Q0VF58; MM.
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
//