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Protein

Collagen alpha-2(VI) chain

Gene

Col6a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Collagen VI acts as a cell-binding protein.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.
R-MMU-186797. Signaling by PDGF.
R-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-419037. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(VI) chain
Gene namesi
Name:Col6a2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:88460. Col6a2.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: MGI
  • extracellular space Source: MGI
  • extracellular vesicle Source: MGI
  • proteinaceous extracellular matrix Source: MGI
  • protein complex Source: MGI
  • sarcolemma Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000583326 – 1034Collagen alpha-2(VI) chainAdd BLAST1009

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi645N-linked (GlcNAc...)Sequence analysis1
Modified residuei716PhosphothreonineBy similarity1
Modified residuei720PhosphoserineBy similarity1
Glycosylationi800N-linked (GlcNAc...)Sequence analysis1
Glycosylationi912N-linked (GlcNAc...)Sequence analysis1

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.

Keywords - PTMi

Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiQ02788.
PaxDbiQ02788.
PeptideAtlasiQ02788.
PRIDEiQ02788.

2D gel databases

REPRODUCTION-2DPAGEQ02788.

PTM databases

iPTMnetiQ02788.
PhosphoSitePlusiQ02788.

Expressioni

Tissue specificityi

Highly expressed in adipose tissue, lung, adrenal glands and ovary. Lower levels in testis, tongue, skin, kidney, heart, intestine and spleen. No expression in skeletal muscle or liver.

Gene expression databases

BgeeiENSMUSG00000020241.
CleanExiMM_COL6A2.
ExpressionAtlasiQ02788. baseline and differential.
GenevisibleiQ02788. MM.

Interactioni

Subunit structurei

Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). Interacts with CSPG4 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ02788. 2 interactors.
MINTiMINT-4381294.
STRINGi10090.ENSMUSP00000001181.

Structurei

3D structure databases

ProteinModelPortaliQ02788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 249VWFA 1PROSITE-ProRule annotationAdd BLAST189
Domaini630 – 820VWFA 2PROSITE-ProRule annotationAdd BLAST191
Domaini848 – 1029VWFA 3PROSITE-ProRule annotationAdd BLAST182

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 270Nonhelical regionAdd BLAST245
Regioni271 – 605Triple-helical regionAdd BLAST335
Regioni606 – 1034Nonhelical regionAdd BLAST429

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi381 – 383Cell attachment siteSequence analysis3
Motifi441 – 443Cell attachment siteSequence analysis3
Motifi504 – 506Cell attachment siteSequence analysis3
Motifi513 – 515Cell attachment siteSequence analysis3
Motifi554 – 556Cell attachment siteSequence analysis3

Sequence similaritiesi

Belongs to the type VI collagen family.Curated
Contains 3 VWFA domains.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IS7F. Eukaryota.
ENOG410XT53. LUCA.
GeneTreeiENSGT00820000126981.
HOGENOMiHOG000111863.
HOVERGENiHBG051051.
InParanoidiQ02788.
KOiK06238.
OrthoDBiEOG091G020V.
PhylomeDBiQ02788.
TreeFamiTF331207.

Family and domain databases

Gene3Di3.40.50.410. 3 hits.
InterProiIPR008160. Collagen.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 5 hits.
PF00092. VWA. 3 hits.
[Graphical view]
SMARTiSM00327. VWA. 3 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 3 hits.
PROSITEiPS50234. VWFA. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q02788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTIKMLQGP LSVLLIGGLL GVLHAQQQEA ISPQEQEAVS PDISTTERNN
60 70 80 90 100
NCPEKADCPV NVYFVLDTSE SVAMQSPTDS LLYHMQQFVP QFISQLQNEF
110 120 130 140 150
YLDQVALSWR YGGLHFSDQV EVFSPPGSDR ASFTKSLQGI RSFRRGTFTD
160 170 180 190 200
CALANMTQQI RQHVGKGVVN FAVVITDGHV TGSPCGGIKM QAERAREEGI
210 220 230 240 250
RLFAVAPNRN LNEQGLRDIA NSPHELYRNN YATMRPDSTE IDQDTINRII
260 270 280 290 300
KVMKHEAYGE CYKVSCLEIP GPHGPKGYRG QKGAKGNMGE PGEPGQKGRQ
310 320 330 340 350
GDPGIEGPIG FPGPKGVPGF KGEKGEFGSD GRKGAPGLAG KNGTDGQKGK
360 370 380 390 400
LGRIGPPGCK GDPGSRGPDG YPGEAGSPGE RGDQGAKGDS GRPGRRGPPG
410 420 430 440 450
DPGDKGSKGY QGNNGAPGSP GVKGGKGGPG PRGPKGEPGR RGDPGTKGGP
460 470 480 490 500
GSDGPKGEKG DPGPEGPRGL AGEVGSKGAK GDRGLPGPRG PQGALGEPGK
510 520 530 540 550
QGSRGDPGDA GPRGDSGQPG PKGDPGRPGF SYPGPRGTPG EKGEPGPPGP
560 570 580 590 600
EGGRGDFGLK GTPGRKGDKG EPADPGPPGE PGPRGPRGIP GPEGEPGPPG
610 620 630 640 650
DPGLTECDVM TYVRETCGCC DCEKRCGALD VVFVIDSSES IGYTNFTLEK
660 670 680 690 700
NFVINVVNRL GAIAKDPKSE TGTRVGVVQY SHEGTFEAIR LDDERVNSLS
710 720 730 740 750
SFKEAVKNLE WIAGGTWTPS ALKFAYNQLI KESRRQKTRV FAVVITDGRH
760 770 780 790 800
DPRDDDLNLR ALCDRDVTVT AIGIGDMFHE THESENLYSI ACDKPQQVRN
810 820 830 840 850
MTLFSDLVAE KFIDDMEDVL CPDPQIVCPE LPCQTELYVA QCTQRPVDIV
860 870 880 890 900
FLLDGSERLG EQNFHKVRRF VEDVSRRLTL ARRDDDPLNA RMALLQYGSQ
910 920 930 940 950
NQQQVAFPLT YNVTTIHEAL ERATYLNSFS HVGTGIVHAI NNVVRGARGG
960 970 980 990 1000
ARRHAELSFV FLTDGVTGND SLEESVHSMR KQNVVPTVVA VGGDVDMDVL
1010 1020 1030
TKISLGDRAA IFREKDFDSL AQPSFFDRFI RWIC
Length:1,034
Mass (Da):110,334
Last modified:February 6, 2007 - v3
Checksum:iDC56F4CC552E9997
GO

Sequence cautioni

The sequence BAC31374 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA46541 differs from that shown. Reason: Frameshift at position 4.Curated
The sequence CAA46541 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12S → P in CAA46541 (Ref. 1) Curated1
Sequence conflicti205V → L in CAA46541 (Ref. 1) Curated1
Sequence conflicti273H → S in AAA37441 (PubMed:1709252).Curated1
Sequence conflicti809A → S in CAA79153 (PubMed:8489506).Curated1
Sequence conflicti853L → Q in CAA46541 (Ref. 1) Curated1
Sequence conflicti853L → Q in CAA44206 (PubMed:8380980).Curated1
Sequence conflicti967 – 971TGNDS → GNDSL in CAA46541 (Ref. 1) Curated5
Sequence conflicti967 – 971TGNDS → GNDSL in CAA44206 (PubMed:8380980).Curated5
Sequence conflicti981 – 982KQ → TR in CAA46541 (Ref. 1) Curated2
Sequence conflicti981 – 982KQ → TR in CAA44206 (PubMed:8380980).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65582 mRNA. Translation: CAA46541.1. Sequence problems.
BC034414 mRNA. Translation: AAH34414.1.
AK042826 mRNA. Translation: BAC31374.2. Different initiation.
X62332 mRNA. Translation: CAA44206.1.
L06343 mRNA. Translation: AAA37441.1.
Z18272 mRNA. Translation: CAA79153.1.
CCDSiCCDS23951.1.
PIRiS21369.
S32604.
RefSeqiNP_666119.1. NM_146007.2.
UniGeneiMm.1949.

Genome annotation databases

EnsembliENSMUST00000001181; ENSMUSP00000001181; ENSMUSG00000020241.
GeneIDi12834.
KEGGimmu:12834.
UCSCiuc007fuu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65582 mRNA. Translation: CAA46541.1. Sequence problems.
BC034414 mRNA. Translation: AAH34414.1.
AK042826 mRNA. Translation: BAC31374.2. Different initiation.
X62332 mRNA. Translation: CAA44206.1.
L06343 mRNA. Translation: AAA37441.1.
Z18272 mRNA. Translation: CAA79153.1.
CCDSiCCDS23951.1.
PIRiS21369.
S32604.
RefSeqiNP_666119.1. NM_146007.2.
UniGeneiMm.1949.

3D structure databases

ProteinModelPortaliQ02788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ02788. 2 interactors.
MINTiMINT-4381294.
STRINGi10090.ENSMUSP00000001181.

PTM databases

iPTMnetiQ02788.
PhosphoSitePlusiQ02788.

2D gel databases

REPRODUCTION-2DPAGEQ02788.

Proteomic databases

MaxQBiQ02788.
PaxDbiQ02788.
PeptideAtlasiQ02788.
PRIDEiQ02788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001181; ENSMUSP00000001181; ENSMUSG00000020241.
GeneIDi12834.
KEGGimmu:12834.
UCSCiuc007fuu.2. mouse.

Organism-specific databases

CTDi1292.
MGIiMGI:88460. Col6a2.

Phylogenomic databases

eggNOGiENOG410IS7F. Eukaryota.
ENOG410XT53. LUCA.
GeneTreeiENSGT00820000126981.
HOGENOMiHOG000111863.
HOVERGENiHBG051051.
InParanoidiQ02788.
KOiK06238.
OrthoDBiEOG091G020V.
PhylomeDBiQ02788.
TreeFamiTF331207.

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.
R-MMU-186797. Signaling by PDGF.
R-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-419037. NCAM1 interactions.

Miscellaneous databases

ChiTaRSiCol6a2. mouse.
PROiQ02788.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020241.
CleanExiMM_COL6A2.
ExpressionAtlasiQ02788. baseline and differential.
GenevisibleiQ02788. MM.

Family and domain databases

Gene3Di3.40.50.410. 3 hits.
InterProiIPR008160. Collagen.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 5 hits.
PF00092. VWA. 3 hits.
[Graphical view]
SMARTiSM00327. VWA. 3 hits.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 3 hits.
PROSITEiPS50234. VWFA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO6A2_MOUSE
AccessioniPrimary (citable) accession number: Q02788
Secondary accession number(s): Q05505, Q8C972, Q8K229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 6, 2007
Last modified: November 2, 2016
This is version 149 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.