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   27-MAR-2024, entry version 180.
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
RC   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; 7.
DR   ComplexPortal; CPX-2965; Collagen type VI trimer.
DR   IntAct; Q04857; 4.
DR   MINT; Q04857; -.
DR   STRING; 10090.ENSMUSP00000001147; -.
DR   GlyCosmos; Q04857; 5 sites, 12 glycans.
DR   GlyGen; Q04857; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q04857; -.
DR   PhosphoSitePlus; Q04857; -.
DR   SwissPalm; Q04857; -.
DR   EPD; Q04857; -.
DR   jPOST; Q04857; -.
DR   MaxQB; Q04857; -.
DR   PaxDb; 10090-ENSMUSP00000001147; -.
DR   PeptideAtlas; Q04857; -.
DR   ProteomicsDB; 283545; -.
DR   Pumba; Q04857; -.
DR   Antibodypedia; 10507; 445 antibodies from 39 providers.
DR   DNASU; 12833; -.
DR   Ensembl; ENSMUST00000001147.5; ENSMUSP00000001147.5; ENSMUSG00000001119.8.
DR   GeneID; 12833; -.
DR   KEGG; mmu:12833; -.
DR   UCSC; uc007fux.1; mouse.
DR   AGR; MGI:88459; -.
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; QEKKCPD; -.
DR   OrthoDB; 2906665at2759; -.
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 77 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 280 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
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:0097708; C:intracellular vesicle; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0030016; C:myofibril; IMP:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IMP: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:0006103; P:2-oxoglutarate metabolic process; IMP:MGI.
DR   GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR   GO; GO:0030262; P:apoptotic nuclear changes; IMP:MGI.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0006914; P:autophagy; IMP:MGI.
DR   GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR   GO; GO:0060348; P:bone development; IMP:MGI.
DR   GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0070836; P:caveola assembly; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR   GO; GO:0007623; P:circadian rhythm; IMP:MGI.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR   GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR   GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR   GO; GO:0085029; P:extracellular matrix assembly; IMP:MGI.
DR   GO; GO:0070341; P:fat cell proliferation; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0006096; P:glycolytic process; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IDA:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0036022; P:limb joint morphogenesis; IMP:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0060487; P:lung epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0051882; P:mitochondrial depolarization; IMP:MGI.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0071965; P:multicellular organismal locomotion; IMP:MGI.
DR   GO; GO:0010657; P:muscle cell apoptotic process; IMP:MGI.
DR   GO; GO:0055001; P:muscle cell development; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR   GO; GO:0061061; P:muscle structure development; IGI:MGI.
DR   GO; GO:0003012; P:muscle system process; IMP:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR   GO; GO:0050877; P:nervous system process; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR   GO; GO:0006996; P:organelle organization; IMP:MGI.
DR   GO; GO:0001503; P:ossification; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR   GO; GO:0051262; P:protein tetramerization; IDA:MGI.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
DR   GO; GO:0002023; P:reduction of food intake in response to dietary excess; IMP:MGI.
DR   GO; GO:0008361; P:regulation of cell size; IMP:MGI.
DR   GO; GO:1904026; P:regulation of collagen fibril organization; IMP:MGI.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0014823; P:response to activity; IMP:MGI.
DR   GO; GO:1904975; P:response to bleomycin; IMP:MGI.
DR   GO; GO:0036293; P:response to decreased oxygen levels; IMP:MGI.
DR   GO; GO:0033993; P:response to lipid; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
DR   GO; GO:0014850; P:response to muscle activity; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:1901652; P:response to peptide; IMP:MGI.
DR   GO; GO:1904583; P:response to polyamine macromolecule; IMP:MGI.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR   GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR   GO; GO:0009411; P:response to UV; IDA:MGI.
DR   GO; GO:0009611; P:response to wounding; IDA:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR   GO; GO:0050954; P:sensory perception of mechanical stimulus; IMP:MGI.
DR   GO; GO:0007338; P:single fertilization; IGI:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR   GO; GO:0098528; P:skeletal muscle fiber differentiation; IGI:MGI.
DR   GO; GO:0060538; P:skeletal muscle organ development; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0048630; P:skeletal muscle tissue growth; IMP:MGI.
DR   GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0048771; P:tissue remodeling; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IMP:MGI.
DR   GO; GO:0060065; P:uterus development; IGI:MGI.
DR   CDD; cd01480; vWA_collagen_alpha_1-VI-type; 3.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF84; COLLAGEN ALPHA-1(XXI) CHAIN-LIKE ISOFORM X1; 1.
DR   Pfam; PF01391; Collagen; 5.
DR   Pfam; PF00092; VWA; 3.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00327; VWA; 3.
DR   SUPFAM; SSF53300; vWA-like; 3.
DR   PROSITE; PS50234; VWFA; 3.
DR   Genevisible; Q04857; MM.
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
//