CO6A6_MOUSE
ID CO6A6_MOUSE Reviewed; 2265 AA.
AC Q8C6K9; A6H587; A6H588; A6H589; A6H590;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Collagen alpha-6(VI) chain;
DE Flags: Precursor;
GN Name=Col6a6;
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] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE 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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C6K9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C6K9-2; Sequence=VSP_033916, VSP_033917;
CC -!- TISSUE SPECIFICITY: In newborn, it is expressed in lung, heart, kidney,
CC muscle, brain, intestine, skin, femur and sternum. In adult, it is
CC expressed in lung, heart, muscle, ovary, brain, 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; AM748259; CAO01894.1; -; mRNA.
DR EMBL; AM748260; CAO01895.1; -; mRNA.
DR EMBL; AM748261; CAO01896.1; -; mRNA.
DR EMBL; AM748262; CAO01897.1; -; mRNA.
DR EMBL; AK054356; BAC35749.1; -; mRNA.
DR CCDS; CCDS23468.1; -. [Q8C6K9-2]
DR CCDS; CCDS52906.1; -. [Q8C6K9-1]
DR RefSeq; NP_001096077.1; NM_001102607.1. [Q8C6K9-1]
DR RefSeq; NP_766515.2; NM_172927.3. [Q8C6K9-2]
DR AlphaFoldDB; Q8C6K9; -.
DR SMR; Q8C6K9; -.
DR STRING; 10090.ENSMUSP00000096040; -.
DR GlyGen; Q8C6K9; 4 sites.
DR iPTMnet; Q8C6K9; -.
DR PhosphoSitePlus; Q8C6K9; -.
DR MaxQB; Q8C6K9; -.
DR PaxDb; Q8C6K9; -.
DR PRIDE; Q8C6K9; -.
DR ProteomicsDB; 283669; -. [Q8C6K9-1]
DR ProteomicsDB; 283670; -. [Q8C6K9-2]
DR Antibodypedia; 56016; 62 antibodies from 11 providers.
DR DNASU; 245026; -.
DR Ensembl; ENSMUST00000060896; ENSMUSP00000060840; ENSMUSG00000043719. [Q8C6K9-2]
DR Ensembl; ENSMUST00000098441; ENSMUSP00000096040; ENSMUSG00000043719. [Q8C6K9-1]
DR GeneID; 245026; -.
DR KEGG; mmu:245026; -.
DR UCSC; uc009ris.1; mouse. [Q8C6K9-1]
DR UCSC; uc009rit.1; mouse. [Q8C6K9-2]
DR CTD; 131873; -.
DR MGI; MGI:2444259; Col6a6.
DR VEuPathDB; HostDB:ENSMUSG00000043719; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155619; -.
DR HOGENOM; CLU_000182_0_0_1; -.
DR InParanoid; Q8C6K9; -.
DR OMA; NFIRNTS; -.
DR OrthoDB; 1049829at2759; -.
DR PhylomeDB; Q8C6K9; -.
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; 245026; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q8C6K9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C6K9; protein.
DR Bgee; ENSMUSG00000043719; Expressed in primary oocyte and 30 other tissues.
DR ExpressionAtlas; Q8C6K9; baseline and differential.
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; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA: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; -; 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 Alternative splicing; Cell adhesion; Collagen; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2265
FT /note="Collagen alpha-6(VI) chain"
FT /id="PRO_5000253013"
FT DOMAIN 26..205
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 228..406
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 435..605
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 621..790
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 808..981
FT /note="VWFA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 999..1170
FT /note="VWFA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1186..1378
FT /note="VWFA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1756..1936
FT /note="VWFA 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1964..2165
FT /note="VWFA 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 19..1390
FT /note="Nonhelical region"
FT REGION 1391..1724
FT /note="Triple-helical region"
FT REGION 1398..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..2265
FT /note="Nonhelical region"
FT REGION 2186..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1507..1509
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1467..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1182
FT /note="N -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033916"
FT VAR_SEQ 1183..2265
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033917"
FT CONFLICT 923
FT /note="H -> N (in Ref. 2; BAC35749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2265 AA; 246323 MW; 30F442032002386A CRC64;
MLLVLCLTMI CFHVCVNQDS GPEYADVVFL VDSSDHLGLK SFPLVKTFIH KMISSLPIEA
NKYRVALAQY SDALHNEFQL GTFKNRNPML NHLKKNFGFI GGSLKIGNAL QEAHRTYFSA
PTNGRDKKQF PPILVVLASA ESEDDVEEAA KALREDGVKI ISVGVQKASE ENLKAMATSQ
FHFNLRTARD LSVFAPNMTE IIKDVTQYRE GMADDIIVEA CQGPSVADVV FLLDMAINGS
QEDLDHLKAF LGESISALDI KENCMRVGLV TYSNETRVIS SLSTGNNKTE VLQRIQDLSP
QVGQAYTGAA LRKTRKEIFS AQRGSRKNQG VPQIAVLVTH RASEDNVTKA AVNLRREGVT
IFTMGIEGAN PDELEKIASH PAEQFTSKLG NFSELATHNQ TFLKKLRNQI THTVSVFSER
TETLKSACVD TEEADIYLLI DGSGSTQPTD FHEMKTFLSE VVGMFNIAPH KVRVGAVQYA
DTWDLEFEIS KYSNKPDLGK AIENIRQMGG NTNTGAALNF TLKLLQRAKK ERGSKVPCHL
VVLTNGMSRD SVLGPAHKLR EENIRVHAIG VKEANQTQLR EIAGEEKRVY YVHEFDALRN
IRNQVVQEIC AEEACRDMKA DIMFLVDSSG SIGPENFSKM KMFMKNLVSK SQIGADRVQI
GVVQFSHENK EEFQLNTFMS QSDIANAIDR MTHIGETTLT GSALTFVSQY FSPDKGARPN
VRKFLILITD GEAQDIVRDP AIALRKEGVI IYSVGVFGSN VTQLEEISGK PEMVFYVENF
DILQHIEDDL VLGICSPREE CKRIEVLDVV FVIDSSGSID YQEYNIMKDF MIGLVKKADV
GKNQVRFGAL KYADDPEVLF YLDELGTKLE VVSVLQNDHP MGGNTYTAEA LAFSDHMFTE
ARGSRLHKGV PQVLIVITDG ESHDAEKLNT TAKALRDKGI LVLAVGIAGA NSWELLAMAG
SSDKYYFVET FGGLKGIFSD VSASVCNSSK VDCEIEKVDL VFLMDGSNSI HPDDFQKMKG
FLVSVVQDFD VSLNRVRIGV AQFSDSYRSE FLLGTFTGER EISTQIEGIQ QIFGYTHIGD
ALRKVKYYFQ PDMGSRINAG TPQVLLVLTD GRSQDEVAQA AEELRHKGVD IYSVGIGDVD
DQELVQITGT AEKKLTVHNF DELKKVKKRI VRNICTSGGE SNCFVDVVVG FDISSLQRGQ
TLLEGQPWMG SYLQDLLRAI SSLNGVSCEV GTETQVSIAF QVTNAMERYP SKFEIYSENI
LSSLQGVTVN GPSRLNANLL SSLWDTFQNK SAARGKVVLL FSDGLDDGIE KLEQKSDELR
KEGLNALITI AVDGAADSSD LADLLYIEFG KGFEYRTQFT IGMRNLGSQL SRQLINVAER
TCCCLLCKCT GGDGAMGDPG SAGKKGPPGF KGSDGYLGEE GIAGERGASG PMGEQGTKGC
FGAKGPKGTR GLSGEEGEVG EDGLDGLDGE QGDHGIPGRR GEKGDEGSQG NPGRRGAAGD
RGAKGLRGDP GTPGRDSSIQ GPKGLKGDLG RQGRRGWPGS PGTPGSRRKM VVHGRRGHIG
PQGNPGTPGP DGLAGSPGLR GPQGPRGEVG EKGEKGSLGM KGPQGPPGPG GQAGSQGHLG
SQGNKGEPGD LGEKGAAGFP GPRGLQGDDG SPGYGSIGRK GTKGQEGFPG ESGLKGDIGD
PGDPGEAGPK GARGKTVSAG IPGEPGSPGE PGPPGRKGVK GARGLASFST CDLIQYVRDH
SPGRHGKPEC PVHPTELVFV LDQSRDVTEQ DFERMKGMMV SLVRDVKVRE ANCPVGARVA
ILAYNSHTRH LIRFSDAYRK DQLLTAIKAL PYERSSDSRE IGKAMRFISR NVFKRTLPGA
HVRRIATFFS SGPSADAQTI TTAAMEFSAL DIVPVVIAFS NVPSVKRAFS IDDTGTFQVI
VVPSGSDEGP ALERLQRCTF CYDLCKPDAS CDQAKPPPIQ SYLDTAFLLD GSRHVGSAEF
EDMRDFLEAL LDHFEITSEP ETSVTGDRVA LLSHAPLDFL PNTQRSPVRT EFNLTSYSSK
RLMKRHVDQA VQQLHGDAFL GHALGWALDN VFLNTPNLRR NKVIFVISAG ETSHLDAETL
KKESLRAKCH GYALFVFSLG PDWDDKELED LASHPVDQHL IQLGRIHKPD HGYSVKFVKS
FINSIRHGIN KYPPVNLKAK CNRLGSRDLK PPPRQFRSFV PGPQKANLKD HTAEAAKLFQ
DKKRLSSMLK GGRATISSLS RSTRYAFKQG KEAIKATSKL GKRSA
