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Q02788

- CO6A2_MOUSE

UniProt

Q02788 - CO6A2_MOUSE

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Protein

Collagen alpha-2(VI) chain

Gene

Col6a2

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

Functioni

Collagen VI acts as a cell-binding protein.

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. protein heterotrimerization Source: MGI
  3. response to glucose Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(VI) chain
Gene namesi
Name:Col6a2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:88460. Col6a2.

Subcellular locationi

Secretedextracellular spaceextracellular matrix By similarity. Membrane By similarity; Peripheral membrane protein By similarity
Note: Recruited on membranes by CSPG4.By similarity

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular matrix Source: UniProtKB
  3. extracellular region Source: MGI
  4. extracellular space Source: Ensembl
  5. extracellular vesicular exosome Source: Ensembl
  6. proteinaceous extracellular matrix Source: UniProtKB-KW
  7. protein complex Source: MGI
  8. sarcolemma Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 10341009Collagen alpha-2(VI) chainPRO_0000005833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi645 – 6451N-linked (GlcNAc...)Sequence Analysis
Modified residuei716 – 7161PhosphothreonineBy similarity
Modified residuei718 – 7181PhosphothreonineBy similarity
Modified residuei720 – 7201PhosphoserineBy similarity
Glycosylationi800 – 8001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi912 – 9121N-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.

Keywords - PTMi

Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiQ02788.
PaxDbiQ02788.
PRIDEiQ02788.

2D gel databases

REPRODUCTION-2DPAGEQ02788.

PTM databases

PhosphoSiteiQ02788.

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

BgeeiQ02788.
CleanExiMM_COL6A2.
ExpressionAtlasiQ02788. baseline and differential.
GenevestigatoriQ02788.

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 interactions.
MINTiMINT-4381294.

Structurei

3D structure databases

ProteinModelPortaliQ02788.
SMRiQ02788. Positions 630-797, 841-992.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 249189VWFA 1PROSITE-ProRule annotationAdd
BLAST
Domaini630 – 820191VWFA 2PROSITE-ProRule annotationAdd
BLAST
Domaini848 – 1029182VWFA 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 270245Nonhelical regionAdd
BLAST
Regioni271 – 605335Triple-helical regionAdd
BLAST
Regioni606 – 1034429Nonhelical regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi381 – 3833Cell attachment siteSequence Analysis
Motifi441 – 4433Cell attachment siteSequence Analysis
Motifi504 – 5063Cell attachment siteSequence Analysis
Motifi513 – 5153Cell attachment siteSequence Analysis
Motifi554 – 5563Cell attachment siteSequence Analysis

Sequence similaritiesi

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG256042.
GeneTreeiENSGT00760000119051.
HOGENOMiHOG000111863.
HOVERGENiHBG051051.
InParanoidiQ02788.
KOiK06238.
OrthoDBiEOG72G16P.
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 CAA46541.1 differs from that shown. Reason: Frameshift at position 4.
The sequence BAC31374.2 differs from that shown. Reason: Erroneous initiation.
The sequence CAA46541.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121S → P in CAA46541. 1 PublicationCurated
Sequence conflicti205 – 2051V → L in CAA46541. 1 PublicationCurated
Sequence conflicti273 – 2731H → S in AAA37441. (PubMed:1709252)Curated
Sequence conflicti809 – 8091A → S in CAA79153. (PubMed:8489506)Curated
Sequence conflicti853 – 8531L → Q in CAA46541. 1 PublicationCurated
Sequence conflicti853 – 8531L → Q in CAA44206. (PubMed:8380980)Curated
Sequence conflicti967 – 9715TGNDS → GNDSL in CAA46541. 1 PublicationCurated
Sequence conflicti967 – 9715TGNDS → GNDSL in CAA44206. (PubMed:8380980)Curated
Sequence conflicti981 – 9822KQ → TR in CAA46541. 1 PublicationCurated
Sequence conflicti981 – 9822KQ → TR in CAA44206. (PubMed:8380980)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS23951.1.
PIRi S21369.
S32604.
RefSeqi NP_666119.1. NM_146007.2.
UniGenei Mm.1949.

3D structure databases

ProteinModelPortali Q02788.
SMRi Q02788. Positions 630-797, 841-992.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q02788. 2 interactions.
MINTi MINT-4381294.

PTM databases

PhosphoSitei Q02788.

2D gel databases

REPRODUCTION-2DPAGE Q02788.

Proteomic databases

MaxQBi Q02788.
PaxDbi Q02788.
PRIDEi Q02788.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001181 ; ENSMUSP00000001181 ; ENSMUSG00000020241 .
GeneIDi 12834.
KEGGi mmu:12834.
UCSCi uc007fuu.2. mouse.

Organism-specific databases

CTDi 1292.
MGIi MGI:88460. Col6a2.

Phylogenomic databases

eggNOGi NOG256042.
GeneTreei ENSGT00760000119051.
HOGENOMi HOG000111863.
HOVERGENi HBG051051.
InParanoidi Q02788.
KOi K06238.
OrthoDBi EOG72G16P.
PhylomeDBi Q02788.
TreeFami TF331207.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi COL6A2. mouse.
NextBioi 282346.
PROi Q02788.
SOURCEi Search...

Gene expression databases

Bgeei Q02788.
CleanExi MM_COL6A2.
ExpressionAtlasi Q02788. baseline and differential.
Genevestigatori Q02788.

Family and domain databases

Gene3Di 3.40.50.410. 3 hits.
InterProi IPR008160. Collagen.
IPR002035. VWF_A.
[Graphical view ]
Pfami PF01391. Collagen. 5 hits.
PF00092. VWA. 3 hits.
[Graphical view ]
SMARTi SM00327. VWA. 3 hits.
[Graphical view ]
SUPFAMi SSF53300. SSF53300. 3 hits.
PROSITEi PS50234. VWFA. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Ibrahimi A., Bardon S., Dani C.
    Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-343.
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  4. "Cloning of alpha 2 chain of type VI collagen and expression during mouse development."
    Ibrahimi A., Bertrand B., Bardon S., Amri E.-Z., Grimaldi P., Ailhaud G., Dani C.
    Biochem. J. 289:141-147(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-1034.
  5. "Structure of cDNAs encoding the triple-helical domain of murine alpha 2 (VI) collagen chain and comparison to human and chick homologues. Use of polymerase chain reaction and partially degenerate oligonucleotide for generation of novel cDNA clones."
    Constantinou C.D., Jimenez S.A.
    Matrix 11:1-9(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-605.
    Strain: C57BL/6.
    Tissue: Fibroblast.
  6. "Cloning and sequence analysis of cDNAs encoding the alpha 1, alpha 2 and alpha 3 chains of mouse collagen VI."
    Zhang R.Z., Pan T.C., Timpl R., Chu M.-L.
    Biochem. J. 291:787-792(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 664-1034.

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: October 29, 2014
This is version 131 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

External Data

Dasty 3