CO6A2_MOUSE
ID CO6A2_MOUSE Reviewed; 1034 AA.
AC Q02788; Q05505; Q8C972; Q8K229;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Collagen alpha-2(VI) chain;
DE Flags: Precursor;
GN Name=Col6a2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ibrahimi A., Bardon S., Dani C.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-343.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-1034.
RX PubMed=8380980; DOI=10.1042/bj2890141;
RA Ibrahimi A., Bertrand B., Bardon S., Amri E.-Z., Grimaldi P., Ailhaud G.,
RA Dani C.;
RT "Cloning of alpha 2 chain of type VI collagen and expression during mouse
RT development.";
RL Biochem. J. 289:141-147(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-605.
RC STRAIN=C57BL/6J; TISSUE=Fibroblast;
RX PubMed=1709252; DOI=10.1016/s0934-8832(11)80221-0;
RA Constantinou C.D., Jimenez S.A.;
RT "Structure of cDNAs encoding the triple-helical domain of murine alpha 2
RT (VI) collagen chain and comparison to human and chick homologues. Use of
RT polymerase chain reaction and partially degenerate oligonucleotide for
RT generation of novel cDNA clones.";
RL Matrix 11:1-9(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 664-1034.
RX PubMed=8489506; DOI=10.1042/bj2910787;
RA Zhang R.Z., Pan T.C., Timpl R., Chu M.-L.;
RT "Cloning and sequence analysis of cDNAs encoding the alpha 1, alpha 2 and
RT alpha 3 chains of mouse collagen VI.";
RL Biochem. J. 291:787-792(1993).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein.
CC -!- SUBUNIT: Trimers composed of three different chains: alpha-1(VI),
CC alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-
CC 6(VI). Interacts with CSPG4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Recruited on membranes by CSPG4.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adipose tissue, lung, adrenal
CC glands and ovary. Lower levels in testis, tongue, skin, kidney, heart,
CC intestine and spleen. No expression in skeletal muscle or liver.
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.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31374.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA46541.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA46541.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X65582; CAA46541.1; ALT_SEQ; mRNA.
DR EMBL; BC034414; AAH34414.1; -; mRNA.
DR EMBL; AK042826; BAC31374.2; ALT_INIT; mRNA.
DR EMBL; X62332; CAA44206.1; -; mRNA.
DR EMBL; L06343; AAA37441.1; -; mRNA.
DR EMBL; Z18272; CAA79153.1; -; mRNA.
DR CCDS; CCDS23951.1; -.
DR PIR; S21369; S21369.
DR PIR; S32604; S32604.
DR RefSeq; NP_001334136.1; NM_001347207.1.
DR RefSeq; NP_666119.1; NM_146007.2.
DR AlphaFoldDB; Q02788; -.
DR SMR; Q02788; -.
DR BioGRID; 198824; 7.
DR ComplexPortal; CPX-2965; Collagen type VI trimer.
DR IntAct; Q02788; 3.
DR MINT; Q02788; -.
DR STRING; 10090.ENSMUSP00000001181; -.
DR GlyConnect; 2221; 1 N-Linked glycan (1 site).
DR GlyGen; Q02788; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q02788; -.
DR PhosphoSitePlus; Q02788; -.
DR REPRODUCTION-2DPAGE; Q02788; -.
DR EPD; Q02788; -.
DR jPOST; Q02788; -.
DR MaxQB; Q02788; -.
DR PaxDb; Q02788; -.
DR PeptideAtlas; Q02788; -.
DR PRIDE; Q02788; -.
DR ProteomicsDB; 283667; -.
DR Antibodypedia; 1646; 251 antibodies from 31 providers.
DR DNASU; 12834; -.
DR Ensembl; ENSMUST00000001181; ENSMUSP00000001181; ENSMUSG00000020241.
DR GeneID; 12834; -.
DR KEGG; mmu:12834; -.
DR UCSC; uc007fuu.2; mouse.
DR CTD; 1292; -.
DR MGI; MGI:88460; Col6a2.
DR VEuPathDB; HostDB:ENSMUSG00000020241; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155682; -.
DR HOGENOM; CLU_009158_2_0_1; -.
DR InParanoid; Q02788; -.
DR OrthoDB; 140989at2759; -.
DR PhylomeDB; Q02788; -.
DR TreeFam; TF331207; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12834; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Col6a2; mouse.
DR PRO; PR:Q02788; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q02788; protein.
DR Bgee; ENSMUSG00000020241; Expressed in vault of skull and 213 other tissues.
DR ExpressionAtlas; Q02788; baseline and differential.
DR Genevisible; Q02788; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF00092; VWA; 3.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF53300; SSF53300; 3.
DR PROSITE; PS50234; VWFA; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Collagen; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1034
FT /note="Collagen alpha-2(VI) chain"
FT /id="PRO_0000005833"
FT DOMAIN 61..249
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 630..820
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 848..1029
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 26..270
FT /note="Nonhelical region"
FT REGION 271..605
FT /note="Triple-helical region"
FT REGION 272..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..1034
FT /note="Nonhelical region"
FT MOTIF 381..383
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 441..443
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 504..506
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 513..515
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 554..556
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 574..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12110"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12110"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="S -> P (in Ref. 1; CAA46541)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> L (in Ref. 1; CAA46541)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="H -> S (in Ref. 5; AAA37441)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="A -> S (in Ref. 6; CAA79153)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="L -> Q (in Ref. 1; CAA46541 and 4; CAA44206)"
FT /evidence="ECO:0000305"
FT CONFLICT 967..971
FT /note="TGNDS -> GNDSL (in Ref. 1; CAA46541 and 4;
FT CAA44206)"
FT /evidence="ECO:0000305"
FT CONFLICT 981..982
FT /note="KQ -> TR (in Ref. 1; CAA46541 and 4; CAA44206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1034 AA; 110334 MW; DC56F4CC552E9997 CRC64;
MTTIKMLQGP LSVLLIGGLL GVLHAQQQEA ISPQEQEAVS PDISTTERNN NCPEKADCPV
NVYFVLDTSE SVAMQSPTDS LLYHMQQFVP QFISQLQNEF YLDQVALSWR YGGLHFSDQV
EVFSPPGSDR ASFTKSLQGI RSFRRGTFTD CALANMTQQI RQHVGKGVVN FAVVITDGHV
TGSPCGGIKM QAERAREEGI RLFAVAPNRN LNEQGLRDIA NSPHELYRNN YATMRPDSTE
IDQDTINRII KVMKHEAYGE CYKVSCLEIP GPHGPKGYRG QKGAKGNMGE PGEPGQKGRQ
GDPGIEGPIG FPGPKGVPGF KGEKGEFGSD GRKGAPGLAG KNGTDGQKGK LGRIGPPGCK
GDPGSRGPDG YPGEAGSPGE RGDQGAKGDS GRPGRRGPPG DPGDKGSKGY QGNNGAPGSP
GVKGGKGGPG PRGPKGEPGR RGDPGTKGGP GSDGPKGEKG DPGPEGPRGL AGEVGSKGAK
GDRGLPGPRG PQGALGEPGK QGSRGDPGDA GPRGDSGQPG PKGDPGRPGF SYPGPRGTPG
EKGEPGPPGP EGGRGDFGLK GTPGRKGDKG EPADPGPPGE PGPRGPRGIP GPEGEPGPPG
DPGLTECDVM TYVRETCGCC DCEKRCGALD VVFVIDSSES IGYTNFTLEK NFVINVVNRL
GAIAKDPKSE TGTRVGVVQY SHEGTFEAIR LDDERVNSLS SFKEAVKNLE WIAGGTWTPS
ALKFAYNQLI KESRRQKTRV FAVVITDGRH DPRDDDLNLR ALCDRDVTVT AIGIGDMFHE
THESENLYSI ACDKPQQVRN MTLFSDLVAE KFIDDMEDVL CPDPQIVCPE LPCQTELYVA
QCTQRPVDIV FLLDGSERLG EQNFHKVRRF VEDVSRRLTL ARRDDDPLNA RMALLQYGSQ
NQQQVAFPLT YNVTTIHEAL ERATYLNSFS HVGTGIVHAI NNVVRGARGG ARRHAELSFV
FLTDGVTGND SLEESVHSMR KQNVVPTVVA VGGDVDMDVL TKISLGDRAA IFREKDFDSL
AQPSFFDRFI RWIC
