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Q0VF58

- COJA1_MOUSE

UniProt

Q0VF58 - COJA1_MOUSE

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ0VF58.
CleanExiMM_COL19A1.
ExpressionAtlasiQ0VF58. baseline and differential.
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.
GeneTreeiENSGT00770000120455.
HOGENOMiHOG000085653.
HOVERGENiHBG060240.
InParanoidiQ0VF58.
OMAiERWFLWQ.
OrthoDBiEOG7353W7.
PhylomeDBiQ0VF58.
TreeFamiTF351778.

Family and domain databases

InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
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

        10         20         30         40         50
MRHTGSWKLW TWVTTFLLPA CTCLTVRDKP ETTCPTLRTE RYQDDRNKSE
60 70 80 90 100
LSGFDLGESF ALRHAFCEGD KTCFKLGSVL LIRDTVKIFP KGLPEEYAIA
110 120 130 140 150
VMFRVRRSTK KERWFLWKIL NQQNMAQISV VIDGTKKVVE FMFRGAEGDL
160 170 180 190 200
LNYVFKNREL RPLFDRQWHK LGIGVQSRVL SLYMDCNLIA SRHTEEKNSV
210 220 230 240 250
DFQGRTIIAA RASDGKPVDI ELHQLRIYCN ANFLAEESCC NLSPTKCPEQ
260 270 280 290 300
DDFGSTTSSW GTSNTGKMSS YLPGKQELKD TCQCIPNKEE AGLPGTLRSI
310 320 330 340 350
GHKGDKGEPG EHGLDGTPGL PGQKGEQGLE GIKGEIGEKG EPGAKGDSGL
360 370 380 390 400
DGLNGQDGLK GDSGPQGPPG PKGDKGDMGP PGPPALTGSI GIQGPQGPPG
410 420 430 440 450
KEGQRGRRGK TGPPGNPGPP GPPGPPGLQG LQQPFGGYFN KGTGEHGASG
460 470 480 490 500
PKGEKGDTGL PGFPGSVGPK GHKGEPGEPL TKGEKGDRGE PGLLGPQGIK
510 520 530 540 550
GEPGDPGPPG LLGSPGLKGQ QGPAGSMGPR GPPGDVGLPG EHGIPGKQGV
560 570 580 590 600
KGEKGDPGGR LGPPGLPGLK GDAGPPGISL PGKPGLDGNP GSPGPRGPKG
610 620 630 640 650
ERGLPGLHGS PGDTGPPGVG IPGRTGSQGP AGEPGIQGPR GLPGLPGTPG
660 670 680 690 700
MPGNDGAPGK DGKPGLPGPP GDPIALPLLG DIGALLKNFC GNCQANVPGL
710 720 730 740 750
KSIKGDDGST GEPGKYDPAA RKGDVGPRGP PGFPGREGPK GSKGERGYPG
760 770 780 790 800
IHGEKGDEGL QGIPGLSGAP GPTGPPGLTG RTGHPGPTGA KGDKGSEGPP
810 820 830 840 850
GKPGPPGPPG VPLNEGNGMS SLYKIQGGVN VPGYPGPPGP PGPKGDPGPV
860 870 880 890 900
GEPGAMGLPG LEGFPGVKGD RGPAGPPGIA GISGKPGAPG PPGVPGEQGE
910 920 930 940 950
RGPIGDTGFP GPEGPSGKPG INGKDGLPGA QGIMGKPGDR GPKGERGDQG
960 970 980 990 1000
IPGDRGPQGE RGKPGLTGMK GAIGPVGPAG SKGSTGPPGH QGPPGNPGIP
1010 1020 1030 1040 1050
GTPADAVSFE EIKHYINQEV LRIFEERMAV FLSQLKLPAA MLSAQAHGRP
1060 1070 1080 1090 1100
GPPGKDGLPG PPGDPGPQGY RGQKGERGEP GIGLPGSPGL PGSSAVGLPG
1110 1120 1130
SPGAPGPQGP PGPSGRCNPE DCLYPAPPPH QQAGGK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00770000120455.
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

Bgeei Q0VF58.
CleanExi MM_COL19A1.
ExpressionAtlasi Q0VF58. baseline and differential.
Genevestigatori Q0VF58.

Family and domain databases

InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 73 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