CO6A4_MOUSE
ID CO6A4_MOUSE Reviewed; 2309 AA.
AC A2AX52; A2AX53; A2AX54; A9CR35;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Collagen alpha-4(VI) chain;
DE Flags: Precursor;
GN Name=Col6a4; Synonyms=Dvwa;
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 Nakajima M., Miyamoto Y., Ikegawa S.;
RT "Cloning and characterization of osteoarthritis-associated gene DVWA.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Uterus;
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 [3]
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:0000269|PubMed:18276594}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In newborn, it is expressed in lung, kidney, brain,
CC intestine, skin, sternum and, at weak level, calvaria. In adult, it is
CC almost absent with some weak expression in ovary and very weak
CC expression in spleen, lung, uterus and brain.
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; AB370265; BAF95091.1; -; mRNA.
DR EMBL; AM231151; CAJ77150.1; -; mRNA.
DR EMBL; AM231152; CAJ77151.1; -; mRNA.
DR EMBL; AM231153; CAJ77152.1; -; mRNA.
DR EMBL; AC120386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52907.1; -.
DR RefSeq; NP_081039.2; NM_026763.2.
DR AlphaFoldDB; A2AX52; -.
DR SMR; A2AX52; -.
DR BioGRID; 212923; 2.
DR STRING; 10090.ENSMUSP00000112472; -.
DR GlyGen; A2AX52; 3 sites.
DR iPTMnet; A2AX52; -.
DR PhosphoSitePlus; A2AX52; -.
DR MaxQB; A2AX52; -.
DR PaxDb; A2AX52; -.
DR PRIDE; A2AX52; -.
DR ProteomicsDB; 283668; -.
DR DNASU; 68553; -.
DR Ensembl; ENSMUST00000121963; ENSMUSP00000112472; ENSMUSG00000032572.
DR GeneID; 68553; -.
DR KEGG; mmu:68553; -.
DR UCSC; uc012gzq.1; mouse.
DR CTD; 68553; -.
DR MGI; MGI:1915803; Col6a4.
DR VEuPathDB; HostDB:ENSMUSG00000032572; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000163168; -.
DR HOGENOM; CLU_000182_1_0_1; -.
DR InParanoid; A2AX52; -.
DR OMA; FMERMVN; -.
DR OrthoDB; 1049829at2759; -.
DR PhylomeDB; A2AX52; -.
DR TreeFam; TF337483; -.
DR BioGRID-ORCS; 68553; 2 hits in 70 CRISPR screens.
DR PRO; PR:A2AX52; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; A2AX52; protein.
DR Bgee; ENSMUSG00000032572; Expressed in uterine cervix and 74 other tissues.
DR ExpressionAtlas; A2AX52; baseline and differential.
DR Genevisible; A2AX52; MM.
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; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005518; F:collagen binding; IPI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR Gene3D; 3.40.50.410; -; 8.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00092; VWA; 8.
DR SMART; SM00327; VWA; 9.
DR SUPFAM; SSF53300; SSF53300; 9.
DR PROSITE; PS50234; VWFA; 8.
PE 1: Evidence at protein level;
KW Cell adhesion; Collagen; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..2309
FT /note="Collagen alpha-4(VI) chain"
FT /id="PRO_5000214197"
FT DOMAIN 34..206
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 235..413
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 430..653
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 634..811
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 849..1018
FT /note="VWFA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1030..1199
FT /note="VWFA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1776..1957
FT /note="VWFA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1982..2187
FT /note="VWFA 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 21..1410
FT /note="Nonhelical region"
FT REGION 1411..1744
FT /note="Triple-helical region"
FT REGION 1414..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..2309
FT /note="Nonhelical region"
FT REGION 2262..2300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1527..1529
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2208..2210
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 2265..2284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 77
FT /note="S -> G (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="T -> A (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="G -> A (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> Q (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> L (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="N -> S (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="T -> N (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Q -> P (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="Q -> R (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="R -> G (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="R -> S (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="R -> Q (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="A -> T (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="I -> M (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="T -> I (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="G -> R (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="V -> E (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="I -> V (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="Q -> R (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1281..1283
FT /note="DET -> NEI (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1353..1354
FT /note="IG -> VS (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1434
FT /note="P -> L (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1629
FT /note="L -> P (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1703
FT /note="R -> H (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1775
FT /note="T -> M (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1780
FT /note="T -> A (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1788
FT /note="A -> S (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1809
FT /note="C -> S (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1978
FT /note="K -> D (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
FT CONFLICT 2222
FT /note="F -> L (in Ref. 1; BAF95091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2309 AA; 250798 MW; 31F0282FC77B0DE8 CRC64;
MGTWKTFWLI ISLAAGLGFV KSQRIVCREA SVGDIVFLVH NSINPQHAHS VRNFLYILAN
SLQVGRDNIR VGLAQYSDTP TSEFLLSVYH RKGDVLKHIR GLQFKPGGNR MGQALQFILE
HHFREGAGSR ASQGVPQVAV VVSSGLTEDH IREPAEALRR AGILVYAIGV KDASQAELRE
ISSSPKDNFT FFVPNFPGLP GLAQKLRPEL CSTLGKAAQY TERESPACSE ASPADIVFLV
DSSTSIGLQN FQKVKHFLHS VVSGLDVRSD QVQVGLVQYS DNIYPAFPLK QSSLKSAVLD
RIRNLPYSMG GTSTGSALEF IRANSLTEMS GSRAKDGVPQ IVVLVTDGES SDEVQDVADQ
LKRDGVFVFV VGINIQDVQE LQKIANEPFE EFLFTTENFS ILQALSGTLL QALCSTVERQ
MKKSTKTYAD VVFLIDTSQG TSQASFQWMQ NFISRIIGIL EVGQDKYQIG LAQYSDQGHT
EFLFNTHKTR NEMVAHIHEL LVFQGGSRKT GQGLRFLHRT FFQEAAGSRL LQGVPQYVVV
ITSGKSEDEV GEVAQILRKR GVDIVSVGLQ DFDRAELEGI GPVVLVSDLQ GEDRIRQLML
DVNMFIQGSP KPPRVMTDVA KDAVEECLVP VPADLVFLVE DFSSARQPNF QRVVHFLTTT
VHSLNIHPDT TRVSLVFYSE KPRLEFSLDM YQSAAQVLRH LDRLTFRARR GRAKAGAALD
FLRKEVFLPE KGSRPHRGVQ QIAVVIIESP SLDNVSTPAS YLRRAGVTIY AAGTQPASES
KDLEKIVTYP PWKHAIRLES FLQLSVVGNK LKKKLCPEML SGMPPLMSFI PESTRQSTQE
GCESVEKADI YFLIDGSGSI KPNDFIEMKD FMKEVIKMFH IGPDRVRFGV VQYSDKIISQ
FFLTQYASMA GLSAAIDNIQ QVGGGTTTGK ALSKMVPVFQ NTARIDVARY LIVITDGQST
DPVAEAAQGL RDIGVNIYAI GVRDANTTEL EEIASKKMFF IYEFDSLKSI HQEVIRDICS
SENCKSQKAD IIFLIDGSES IAPKDFEKMK DFMERMVNQS NIGADEIQIG LLQFSSNPQE
EFRLNRYSSK VDMCRAILSV QQMSDGTHTG KALNFTLPFF DSSRGGRPRV HQYLIVITDG
VSQDNVAPPA KALRDRNIII FAIGVGNVQR AQLLEITNDQ DKVFQEENFE SLQSLEKEIL
SEVCSSQGCN IDLSVGVDTS TSSERAQQEL RRLLPELMQQ LAFLSNISCE APGQMEPRFR
YVVPGSSDQP VFDSGFEKYS DETIQKFLVH QGSVNNRMDV DFLQSLGETA IHLSLAKVKV
LLVFTDGLDE DLERLRRTSE FLRSRGLSGL LLIGLGGAHK LEELQELEFG RGFAYRQPLS
SSLPSLPSVL LKQLDTIVER TCCNMYAKCY GDDGIRGEPG SRGEQGERGL DGLPGHPGEE
GDHGQRGPRG LPGLRGEEGC PGVRGPKGAR GFSGEKGNPG EEGVGGLDGE QGDRGAAGPS
GEKGSSGSRG LTGLPGPAGP RGEPGLRGDP GDPGIDNLIQ GPKGEKGRRG HQGSPGFHGP
LGEAGSVGPR GSLGRHGLPG LKGVLGETGE LGSRGEPGHP GPQGPRGRQG PPGFFGQKGD
PGTQGNPGLP GPSGSKGPDG PRGLKGEVGP AGERGPRGQQ GPRGQPGLFG PDGHGYPGRK
GRKGEPGFPG YPGVQGEDGN PGRGGEKGAK GIRGKRGNSG FPGLAGTPGD QGPPGKMGTK
GSKGLADRTP CEIVDFVRGN CPCSTGISRC PAFPTEVVFT LDMSNDVAPS DFERMRNILL
SLLMKLEMCE SNCPTGARVA IVSYNTRTDY LVRLSDHRGK AALLQAVRKI PLERSSGSRN
LGATMRFVAR HVFKRVRSGL LVRKVAVFFQ AGRNYDTASV STATLELHAA DIATAVVTFT
EEHNLPEAGL VDGPNEFHLF TWETEGQQDV ERLASCTLCY DKCRPALGCQ LRAPGPQKLD
MDLVFLVDSS QGVSRDIYLG ALRLVDSVLK DLEVAAQPGT SWHGARAALL THTTPGFWPG
VDQAPVLEYF HLTSHGHRTE MQRQIREAAS GLLQGGPALG HALEWTLENV LLTAVLPRRS
RVLYAIVASE TSIWDREKLR TLSQEAKCKG IALFVLAVGP GVGAQELAEL AKVASAPWEQ
HLLRLEGVSE AEVAYASRFT EAFLNLLNSG INQYPPPELV KECGGPNRGD TLLHFFTSAK
RFSRSQSGTS AAFANDSEAL KSQGIFLGER KSRVASVALQ EALGSHGKDR ADTEDIDQET
PAKGRHLGPT HGPCPMGPEE GECLNYVLK
