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Q0VF58

- COJA1_MOUSE

UniProt

Q0VF58 - COJA1_MOUSE

Protein

Collagen alpha-1(XIX) chain

Gene

Col19a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle.1 PublicationCurated

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. extracellular matrix organization Source: MGI
    4. skeletal muscle tissue development Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Cell adhesion, Differentiation, Myogenesis

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199055. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XIX) chain
    Alternative name(s):
    Collagen alpha-1(Y) chain
    Gene namesi
    Name:Col19a1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1095415. Col19a1.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Mice show severe signs of malnourishment and the majority die within the first three weeks of postnatal life. Newborn homozygotes do not show gross anatomical abnormalities, except for smaller size of the internal organs. However, necroscopy of the mice that survive past the weaning stage reveals a dilated esophagus (megaesophagus) with retention of ingesta immediately above the diaphragm level. Mutant mice also exhibit an additional defect, namely impaired smooth-to-skeletal muscle cell transdifferentiation in the abdominal segment of the esophagus. Heterozygotes by comparison are morphologically normal, viable and fertile.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 11361113Collagen alpha-1(XIX) chainSequence AnalysisPRO_0000284731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.Curated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiQ0VF58.
    PRIDEiQ0VF58.

    PTM databases

    PhosphoSiteiQ0VF58.

    Expressioni

    Developmental stagei

    Expressed in the myotome of somites from E9.5. In muscular tissues, expression is transient and is confined to a few sites of the developing embryo, such as limbs, tongue, and smooth muscle layers of stomach and esophagus. Also detected in skin at E16.5 and in cerebral cortex and hippocampus of the newborn brain. In adult, expression is only observed in cerebrum, cerebellum, eyes, and testis. In CNS, expression gradually increases following birth. Also expressed in embryonic fibroblasts and to a lesser extent in adult fibroblasts.2 Publications

    Gene expression databases

    ArrayExpressiQ0VF58.
    BgeeiQ0VF58.
    CleanExiMM_COL19A1.
    GenevestigatoriQ0VF58.

    Interactioni

    Subunit structurei

    Oligomer; disulfide-linked.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ0VF58.
    SMRiQ0VF58. Positions 48-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 231185Laminin G-likeAdd
    BLAST
    Domaini292 – 34655Collagen-like 1Add
    BLAST
    Domaini347 – 38842Collagen-like 2Add
    BLAST
    Domaini389 – 43042Collagen-like 3Add
    BLAST
    Domaini519 – 57759Collagen-like 4Add
    BLAST
    Domaini578 – 61841Collagen-like 5Add
    BLAST
    Domaini620 – 67354Collagen-like 6Add
    BLAST
    Domaini722 – 77756Collagen-like 7Add
    BLAST
    Domaini778 – 81033Collagen-like 8Add
    BLAST
    Domaini833 – 89159Collagen-like 9Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni289 – 34860Triple-helical region 1 (COL1)Sequence AnalysisAdd
    BLAST
    Regioni367 – 42660Triple-helical region 2 (COL2)Sequence AnalysisAdd
    BLAST
    Regioni442 – 682241Triple-helical region 3 (COL3)Sequence AnalysisAdd
    BLAST
    Regioni694 – 812119Triple-helical region 4 (COL4)Sequence AnalysisAdd
    BLAST
    Regioni827 – 1006180Triple-helical region 5 (COL5)Sequence AnalysisAdd
    BLAST
    Regioni1048 – 110558Triple-helical region 6 (COL6)Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi946 – 9483Cell attachment siteSequence Analysis

    Domaini

    The numerous interruptions in the triple helix may make this molecule either elastic or flexible.By similarity

    Sequence similaritiesi

    Contains 9 collagen-like domains.Curated
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG275976.
    GeneTreeiENSGT00750000117628.
    HOGENOMiHOG000085653.
    HOVERGENiHBG060240.
    InParanoidiQ0VF58.
    OMAiERWFLWQ.
    OrthoDBiEOG7353W7.
    PhylomeDBiQ0VF58.
    TreeFamiTF351778.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01391. Collagen. 9 hits.
    [Graphical view]
    SMARTiSM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q0VF58-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRHTGSWKLW TWVTTFLLPA CTCLTVRDKP ETTCPTLRTE RYQDDRNKSE     50
    LSGFDLGESF ALRHAFCEGD KTCFKLGSVL LIRDTVKIFP KGLPEEYAIA 100
    VMFRVRRSTK KERWFLWKIL NQQNMAQISV VIDGTKKVVE FMFRGAEGDL 150
    LNYVFKNREL RPLFDRQWHK LGIGVQSRVL SLYMDCNLIA SRHTEEKNSV 200
    DFQGRTIIAA RASDGKPVDI ELHQLRIYCN ANFLAEESCC NLSPTKCPEQ 250
    DDFGSTTSSW GTSNTGKMSS YLPGKQELKD TCQCIPNKEE AGLPGTLRSI 300
    GHKGDKGEPG EHGLDGTPGL PGQKGEQGLE GIKGEIGEKG EPGAKGDSGL 350
    DGLNGQDGLK GDSGPQGPPG PKGDKGDMGP PGPPALTGSI GIQGPQGPPG 400
    KEGQRGRRGK TGPPGNPGPP GPPGPPGLQG LQQPFGGYFN KGTGEHGASG 450
    PKGEKGDTGL PGFPGSVGPK GHKGEPGEPL TKGEKGDRGE PGLLGPQGIK 500
    GEPGDPGPPG LLGSPGLKGQ QGPAGSMGPR GPPGDVGLPG EHGIPGKQGV 550
    KGEKGDPGGR LGPPGLPGLK GDAGPPGISL PGKPGLDGNP GSPGPRGPKG 600
    ERGLPGLHGS PGDTGPPGVG IPGRTGSQGP AGEPGIQGPR GLPGLPGTPG 650
    MPGNDGAPGK DGKPGLPGPP GDPIALPLLG DIGALLKNFC GNCQANVPGL 700
    KSIKGDDGST GEPGKYDPAA RKGDVGPRGP PGFPGREGPK GSKGERGYPG 750
    IHGEKGDEGL QGIPGLSGAP GPTGPPGLTG RTGHPGPTGA KGDKGSEGPP 800
    GKPGPPGPPG VPLNEGNGMS SLYKIQGGVN VPGYPGPPGP PGPKGDPGPV 850
    GEPGAMGLPG LEGFPGVKGD RGPAGPPGIA GISGKPGAPG PPGVPGEQGE 900
    RGPIGDTGFP GPEGPSGKPG INGKDGLPGA QGIMGKPGDR GPKGERGDQG 950
    IPGDRGPQGE RGKPGLTGMK GAIGPVGPAG SKGSTGPPGH QGPPGNPGIP 1000
    GTPADAVSFE EIKHYINQEV LRIFEERMAV FLSQLKLPAA MLSAQAHGRP 1050
    GPPGKDGLPG PPGDPGPQGY RGQKGERGEP GIGLPGSPGL PGSSAVGLPG 1100
    SPGAPGPQGP PGPSGRCNPE DCLYPAPPPH QQAGGK 1136
    Length:1,136
    Mass (Da):114,197
    Last modified:April 17, 2007 - v2
    Checksum:iC480216027D70B43
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101K → Q in BAA23578. (PubMed:9202028)Curated
    Sequence conflicti315 – 3151D → N in BAA23578. (PubMed:9202028)Curated
    Sequence conflicti315 – 3151D → N in AAI18971. (PubMed:15489334)Curated
    Sequence conflicti528 – 5281G → K in BAA23578. (PubMed:9202028)Curated
    Sequence conflicti597 – 5971G → E in BAA23578. (PubMed:9202028)Curated
    Sequence conflicti717 – 7171D → E in BAA23578. (PubMed:9202028)Curated
    Sequence conflicti717 – 7171D → E in AAI18971. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000636 mRNA. Translation: BAA23578.1.
    AC116998 Genomic DNA. No translation available.
    AC130201 Genomic DNA. No translation available.
    AC161879 Genomic DNA. No translation available.
    BC118970 mRNA. Translation: AAI18971.1.
    CCDSiCCDS14854.1.
    RefSeqiNP_031759.2. NM_007733.2.
    XP_006495708.1. XM_006495645.1.
    UniGeneiMm.329196.

    Genome annotation databases

    EnsembliENSMUST00000115244; ENSMUSP00000110899; ENSMUSG00000026141.
    GeneIDi12823.
    KEGGimmu:12823.
    UCSCiuc007amq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000636 mRNA. Translation: BAA23578.1 .
    AC116998 Genomic DNA. No translation available.
    AC130201 Genomic DNA. No translation available.
    AC161879 Genomic DNA. No translation available.
    BC118970 mRNA. Translation: AAI18971.1 .
    CCDSi CCDS14854.1.
    RefSeqi NP_031759.2. NM_007733.2.
    XP_006495708.1. XM_006495645.1.
    UniGenei Mm.329196.

    3D structure databases

    ProteinModelPortali Q0VF58.
    SMRi Q0VF58. Positions 48-242.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q0VF58.

    Proteomic databases

    PaxDbi Q0VF58.
    PRIDEi Q0VF58.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000115244 ; ENSMUSP00000110899 ; ENSMUSG00000026141 .
    GeneIDi 12823.
    KEGGi mmu:12823.
    UCSCi uc007amq.1. mouse.

    Organism-specific databases

    CTDi 1310.
    MGIi MGI:1095415. Col19a1.

    Phylogenomic databases

    eggNOGi NOG275976.
    GeneTreei ENSGT00750000117628.
    HOGENOMi HOG000085653.
    HOVERGENi HBG060240.
    InParanoidi Q0VF58.
    OMAi ERWFLWQ.
    OrthoDBi EOG7353W7.
    PhylomeDBi Q0VF58.
    TreeFami TF351778.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    NextBioi 282302.
    PROi Q0VF58.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q0VF58.
    Bgeei Q0VF58.
    CleanExi MM_COL19A1.
    Genevestigatori Q0VF58.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01391. Collagen. 9 hits.
    [Graphical view ]
    SMARTi SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Ubiquitous expression of the alpha1(XIX) collagen gene (Col19a1) during mouse embryogenesis becomes restricted to a few tissues in the adult organism."
      Sumiyoshi H., Inoguchi K., Khaleduzzaman M., Ninomiya Y., Yoshioka H.
      J. Biol. Chem. 272:17104-17111(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
      Strain: BALB/cImported.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Embryonic expression of type XIX collagen is transient and confined to muscle cells."
      Sumiyoshi H., Laub F., Yoshioka H., Ramirez F.
      Dev. Dyn. 220:155-162(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    5. "Esophageal muscle physiology and morphogenesis require assembly of a collagen XIX-rich basement membrane zone."
      Sumiyoshi H., Mor N., Lee S.Y., Doty S., Henderson S., Tanaka S., Yoshioka H., Rattan S., Ramirez F.
      J. Cell Biol. 166:591-600(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiCOJA1_MOUSE
    AccessioniPrimary (citable) accession number: Q0VF58
    Secondary accession number(s): O35053
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 71 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3