CO6A1_MOUSE
ID CO6A1_MOUSE Reviewed; 1025 AA.
AC Q04857;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Collagen alpha-1(VI) chain;
DE Flags: Precursor;
GN Name=Col6a1;
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 [GENOMIC DNA / MRNA].
RX PubMed=8326912; DOI=10.1016/s0934-8832(11)80006-5;
RA Bonaldo P., Piccolo S., Marvulli D., Volpin D., Bressan G.M.;
RT "Murine alpha 1(VI) collagen chain. Complete amino acid sequence and
RT identification of the gene promoter region.";
RL Matrix 13:223-233(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 442-1025.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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}.
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DR EMBL; X66405; CAA47032.1; -; mRNA.
DR EMBL; X66406; CAA47033.1; -; Genomic_DNA.
DR EMBL; Z18271; CAA79152.1; -; mRNA.
DR CCDS; CCDS23952.1; -.
DR PIR; S34839; S34839.
DR RefSeq; NP_034063.1; NM_009933.4.
DR AlphaFoldDB; Q04857; -.
DR SMR; Q04857; -.
DR BioGRID; 198823; 6.
DR ComplexPortal; CPX-2965; Collagen type VI trimer.
DR IntAct; Q04857; 4.
DR MINT; Q04857; -.
DR STRING; 10090.ENSMUSP00000001147; -.
DR GlyGen; Q04857; 5 sites.
DR iPTMnet; Q04857; -.
DR PhosphoSitePlus; Q04857; -.
DR EPD; Q04857; -.
DR jPOST; Q04857; -.
DR MaxQB; Q04857; -.
DR PaxDb; Q04857; -.
DR PeptideAtlas; Q04857; -.
DR PRIDE; Q04857; -.
DR ProteomicsDB; 283545; -.
DR Antibodypedia; 10507; 391 antibodies from 39 providers.
DR DNASU; 12833; -.
DR Ensembl; ENSMUST00000001147; ENSMUSP00000001147; ENSMUSG00000001119.
DR GeneID; 12833; -.
DR KEGG; mmu:12833; -.
DR UCSC; uc007fux.1; mouse.
DR CTD; 1291; -.
DR MGI; MGI:88459; Col6a1.
DR VEuPathDB; HostDB:ENSMUSG00000001119; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000162889; -.
DR HOGENOM; CLU_009158_1_0_1; -.
DR InParanoid; Q04857; -.
DR OMA; TTQICID; -.
DR OrthoDB; 140989at2759; -.
DR PhylomeDB; Q04857; -.
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; 12833; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Col6a1; mouse.
DR PRO; PR:Q04857; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q04857; protein.
DR Bgee; ENSMUSG00000001119; Expressed in efferent duct and 279 other tissues.
DR Genevisible; Q04857; 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:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; 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 Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..1025
FT /note="Collagen alpha-1(VI) chain"
FT /id="PRO_0000005759"
FT DOMAIN 36..234
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 614..802
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 826..1018
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 20..255
FT /note="N-terminal globular domain"
FT REGION 252..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..591
FT /note="Triple-helical region"
FT REGION 592..1025
FT /note="C-terminal globular domain"
FT MOTIF 261..263
FT /note="Cell attachment site"
FT MOTIF 441..443
FT /note="Cell attachment site"
FT MOTIF 477..479
FT /note="Cell attachment site"
FT COMPBIAS 302..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 674..675
FT /note="DM -> TL (in Ref. 2; CAA79152)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="T -> A (in Ref. 2; CAA79152)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="Missing (in Ref. 2; CAA79152)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="Q -> R (in Ref. 2; CAA79152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1025 AA; 108489 MW; 2A05DFED8771BBF7 CRC64;
MRLAHALLPL LLQACWVATQ DIQGSKAIAF QDCPVDLFFV LDTSESVALR LKPYGALVDK
VKSFTKRFID NLRDRYYRCD RNLVWNAGAL HYSDEVEIIR GLTRMPSGRD ELKASVDAVK
YFGKGTYTDC AIKKGLEELL IGGSHLKENK YLIVVTDGHP LEGYKEPCGG LEDAVNEAKH
LGIKVFSVAI TPDHLEPRLS IIATDHTYRR NFTAADWGHS RDAEEVISQT IDTIVDMIKN
NVEQVCCSFE CQAARGPPGP RGDPGYEGER GKPGLPGEKG EAGDPGRPGD LGPVGYQGMK
GEKGSRGEKG SRGPKGYKGE KGKRGIDGVD GMKGETGYPG LPGCKGSPGF DGIQGPPGPK
GDAGAFGMKG EKGEAGADGE AGRPGNSGSP GDEGDPGEPG PPGEKGEAGD EGNAGPDGAP
GERGGPGERG PRGTPGVRGP RGDPGEAGPQ GDQGREGPVG IPGDSGEAGP IGPKGYRGDE
GPPGPEGLRG APGPVGPPGD PGLMGERGED GPPGNGTEGF PGFPGYPGNR GPPGLNGTKG
YPGLKGDEGE VGDPGEDNND ISPRGVKGAK GYRGPEGPQG PPGHVGPPGP DECEILDIIM
KMCSCCECTC GPIDILFVLD SSESIGLQNF EIAKDFIIKV IDRLSKDELV KFEPGQSHAG
VVQYSHNQMQ EHVDMRSPNV RNAQDFKEAV KKLQWMAGGT FTGEALQYTR DRLLPPTQNN
RIALVITDGR SDTQRDTTPL SVLCGADIQV VSVGIKDVFG FVAGSDQLNV ISCQGLSQGR
PGISLVKENY AELLDDGFLK NITAQICIDK KCPDYTCPIT FSSPADITIL LDSSASVGSH
NFETTKVFAK RLAERFLSAG RADPSQDVRV AVVQYSGQGQ QQPGRAALQF LQNYTVLASS
VDSMDFINDA TDVNDALSYV TRFYREASSG ATKKRVLLFS DGNSQGATAE AIEKAVQEAQ
RAGIEIFVVV VGPQVNEPHI RVLVTGKTAE YDVAFGERHL FRVPNYQALL RGVLYQTVSR
KVALG
