CO6A5_MOUSE
ID CO6A5_MOUSE Reviewed; 2640 AA.
AC A6H584; A6H585; A6H586; E9Q1B5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 4.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Collagen alpha-5(VI) chain;
DE AltName: Full=Collagen alpha-1(XXIX) chain;
DE Flags: Precursor;
GN Name=Col6a5; Synonyms=Col29a1, Gm7455;
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], SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=18276594; DOI=10.1074/jbc.m709540200;
RA Gara S.K., Grumati P., Urciuolo A., Bonaldo P., Kobbe B., Koch M.,
RA Paulsson M., Wagener R.;
RT "Three novel collagen VI chains with high homology to the alpha 3 chain.";
RL J. Biol. Chem. 283:10658-10670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}.
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). {ECO:0000305|PubMed:18276594}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18276594}. Note=Deposed in the extracellular
CC matrix of skeletal muscle.
CC -!- TISSUE SPECIFICITY: In newborn, it is expressed in lung, heart, kidney,
CC muscle, brain, intestine, skin, femur, sternum and calvaria. In adult,
CC it is widely expressed and is detected in lung, heart, kidney, spleen,
CC muscle, ovary, uterus, brain, skin, liver and sternum.
CC {ECO:0000269|PubMed:18276594}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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DR EMBL; AM748256; CAO01891.1; -; mRNA.
DR EMBL; AM748257; CAO01892.1; -; mRNA.
DR EMBL; AM748258; CAO01893.1; -; mRNA.
DR EMBL; AC119951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS85720.1; -.
DR RefSeq; NP_001161395.1; NM_001167923.1.
DR AlphaFoldDB; A6H584; -.
DR SMR; A6H584; -.
DR STRING; 10090.ENSMUSP00000139398; -.
DR GlyGen; A6H584; 4 sites.
DR iPTMnet; A6H584; -.
DR PhosphoSitePlus; A6H584; -.
DR PaxDb; A6H584; -.
DR PeptideAtlas; A6H584; -.
DR PRIDE; A6H584; -.
DR ProteomicsDB; 283546; -.
DR DNASU; 665033; -.
DR GeneID; 665033; -.
DR KEGG; mmu:665033; -.
DR CTD; 256076; -.
DR MGI; MGI:3648134; Col6a5.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; A6H584; -.
DR OrthoDB; 1049829at2759; -.
DR PhylomeDB; A6H584; -.
DR TreeFam; TF318242; -.
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; 665033; 1 hit in 33 CRISPR screens.
DR PRO; PR:A6H584; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A6H584; protein.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR Gene3D; 3.40.50.410; -; 9.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00092; VWA; 9.
DR SMART; SM00327; VWA; 9.
DR SUPFAM; SSF53300; SSF53300; 10.
DR PROSITE; PS50234; VWFA; 9.
PE 1: Evidence at protein level;
KW Cell adhesion; Collagen; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2640
FT /note="Collagen alpha-5(VI) chain"
FT /id="PRO_5000253010"
FT DOMAIN 30..209
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 268..445
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 474..644
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 660..829
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 846..1023
FT /note="VWFA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1037..1214
FT /note="VWFA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1226..1413
FT /note="VWFA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1426..1478
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1474..1524
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1557..1614
FT /note="Collagen-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 1632..1689
FT /note="Collagen-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 1706..1762
FT /note="Collagen-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 1790..1970
FT /note="VWFA 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1996..2186
FT /note="VWFA 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2321..2516
FT /note="VWFA 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 19..1426
FT /note="Nonhelical region"
FT REGION 1427..1760
FT /note="Triple-helical region"
FT REGION 1435..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..2640
FT /note="Nonhelical region"
FT REGION 2617..2640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1649..1651
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2216..2218
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2259..2261
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1448..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1483
FT /note="K -> E (in Ref. 1; CAO01892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1778..1781
FT /note="LIFT -> PCWK (in Ref. 1; CAO01892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2640 AA; 289575 MW; 710C3761FF672ACA CRC64;
MKLRLIAFVL ILWTETLADQ SPGPGPEYAD VVFLVDSSNY LGIKSFPFVR TFLNRMISSL
PIEANKYRVA LAQYSDALHN EFQLGTFKNR NPMLNHLKKN FGFIGGSLKI GNALQEAHRT
YFSAPTNGRD KKQFPPILVV LASAESEDDV EEAAKALRED GVKIISVGVQ KASEENLKAM
ATSQFHFNLR TARDLGMFAP NMTRIIKDVT QYREGTTVDL ITAVAPTTPA APATPAAPTI
PAALTTAANH VDKTVPFPTS CQKDSLADLI FLVDESVGTT QNLRDLQNFL ENVTSSVDVK
DNCMRLGLMS FSDRAQTISS LRSSANQSEF QQQIQKLSLQ TGASNVGAAI EQMRKEGFSE
SSGSRKAQGV PQIAVLVTHR ASDDMVREAA LDLRLEGVTM FAMGIEGANN TQLEDIVSYP
SRQSISTHSS YSHLESYSGN FLKKIRNEIW TQVSTRAEQM ELDKTGCVDT KEADIYFLID
GSSSIRKKEF EQIQIFMSSV IDMFPIGPNK VRVGVVQYSH KNEVEFPVSR YTDGIDLKKA
VFNIKQLKGL TFTGKALDFI LPLIKKGKTE RTDRAPCYLI VLTDGKSNDS VLEPANRLRA
EQITIHAIGI GEANKTQLRQ IAGKDERVNF GQNFDSLKSI KNEIVHRICS EKGCEDMKAD
IMFLVDSSGS IGPTNFETMK TFMKNLVGKI QIGADRSQVG VVQFSDYNRE EFQLNKYSTH
EEIYAAIDRM SPINRNTLTG GALTFVNEYF DLSKGGRPQV RKFLILLTDG KAQDEVGGPA
TALRSKSVTI FSVGVYGANR AQLEEISGDG SLVFHVENFD HLKAIESKLI FRVCALHDCK
RIELLDIVFV LDHSGSIGPR EQESMMNLTI HLVKKADVGR DRVQIGALTY SNHPEILFYL
NTYSSGSAIA EHLRRPRDTG GETYTAKALQ HSNVLFTEEH GSRLTQNVRQ LMIVITDGVS
HDRDKLDEAA RELRDKGITI FAVGVGNANQ DELETMAGKK ENTVHVDNFD KLRDIYLPLQ
ETLCNNSQET CNLPEADVIF LCDGSDMVSD SEFVTMTTFL SDLIDNFDIE SQRMKIGMAQ
YGSRYQEIIE LESSLNKTQW KSQVHSVAQS KGLPRLDFAL KHVSDMFDPS VGGRRNAGVP
QTLVVITSSS PRYDVTDAVK VLKDLGICVL ALGIGDVYKE QLLPITGNSE KIITFRDFNK
LKNVDVKKRM VREICQSCGK ANCFVDVVVG FDISTHRQGQ PLFQGHPRLE SYLPGILEDI
TSIRGVSCGA GAEAQVSLAF KVNSDQEFPA KFQIYQKAAF DSLLHVTVRG PTHLDAPFLQ
SLWDMFEERS ASRGQVLLIF SDGLQGESIT LLERQSDRLR EAGLDALLVV SLNTFGHDEF
SSFEFGKGFD YRTQLTIGML DLGKTLSQYL GNIAERACCC TFCKCPGIPG PHGTRGLQAS
KGSSGPKGSR GHRGEDGDPG RRGEIGLQGD RGVVGCPGTR GQKGVKGFSG AQGEHGEDGL
DGLDGEEGFY GFRGGKGQKG DPGNQGYPGI RGAAGEDGEK GFPGDPGDPG KDSNIKGQKG
EKGERGRQGI TGQKGTHGRP SSKGSRGMEG QRGPQGPSGQ AGNPGPQGTQ GPEGLQGSQG
SSGNRGGKGD KGSQGYQGPQ GSPGPAGPRG DIGRPGFGGR KGEPGVPGGP GPVGPPGQRG
KQGDYGIPGY GQTGRKGVKG PTGFPGDPGQ KGDAGNPGIP GGPGPKGFKG LTLSQGLKGR
SGLQGSQGPP GRRGPKGTAG QPIYSPCELI QFLRDHSLIF TDKCPVYPTE LVFALDQSSG
ITERRFNETR DTITSIVSDL NIRENNCPVG ARVAVVSYDS DTSYLIRGSD YHNKKHLLQL
LSQIKYQVPR KARDIGNAMR FVARNVFKRM SAGTNTRRVA VFFSNGQAAS RASILTATME
LSALDISLAV FAYNERVFLD EAFGFDDTGT FQVIPVPPVG DYEPLEKLRR CTLCYDKCFP
NTCAEEPFFP ENSYMDVAFL LDNSKNIASD DFQAVKALVS SVIDSFHITS NPSASESGDR
VALLSYSPSE SSRRKGRVKT EFAFTTYDNQ SIMKNYIYTS LQQLNGDATI GLALQWAMEG
LFLGTPNPRK HKVIIVISAG ENHEEKEFVK TVALRAKCQG YVVFVISLGS TQRDEMEELA
SYPLDHHLIQ LGRMYKPDLN YIVKFLKPFI YSVRRGFNQY PPPTLKDDCR LVELERGDTL
PHGLRLTAKL REVPESTISL ADQELNAGKD SSFVLEDHRG DHLVYVPSQM LEPHKLVSHY
GNDRESVAMA SLTSEHESHG REELGLAHEP GDASLQEYYM DVAFLIDASQ RVGGRNEFKE
VRTLITSVLD YFHIAPAPLT SVLGDRVAVL TYSPPGYLPN TEECPVYLEF DLVTYNTVHQ
MKHHLQESLQ QLNGDVFIGH ALQWTVDNVF VGTPNLRKNK VIFIVTAGET NPLDKEVLRN
ASLRAKCQGY SIFVFSFGPI HNDMELEELA SHPLDHHLVR LGRVHRPDLD YVIKFIKPFV
HSIRRAINKY PGRDLQAKCD NLTFPGPENA GTEDSALLIP EVYRIEAGEN ELSGDSGSQE
QHFFLLGNSH GNHSESTADL MRQLYLLLSS GELMVNDKEE PCSAETPAPV NSKQDGEDAR
