ID   CO6A1_XENLA             Reviewed;        1045 AA.
AC   Q801S8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Collagen alpha-1(VI) chain;
DE   Flags: Precursor;
GN   Name=col6a1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20029839; DOI=10.1002/pmic.200900281;
RA   Devreese B., Sergeant K., Van Bakel N.H., Debyser G., Van Beeumen J.,
RA   Martens G.J., Van Herp F.;
RT   "A proteome map of the pituitary melanotrope cell activated by black-
RT   background adaptation of Xenopus laevis.";
RL   Proteomics 10:574-580(2010).
CC   -!- FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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DR   EMBL; BC047255; AAH47255.1; -; mRNA.
DR   RefSeq; NP_001080437.1; NM_001086968.1.
DR   AlphaFoldDB; Q801S8; -.
DR   SMR; Q801S8; -.
DR   DNASU; 380129; -.
DR   GeneID; 380129; -.
DR   CTD; 380129; -.
DR   Xenbase; XB-GENE-998859; col6a1.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 380129; Expressed in lung and 17 other tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 2.
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; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1045
FT                   /note="Collagen alpha-1(VI) chain"
FT                   /id="PRO_0000379424"
FT   DOMAIN          65..255
FT                   /note="VWFA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          638..825
FT                   /note="VWFA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          849..1035
FT                   /note="VWFA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          277..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..540
FT                   /note="Triple-helical region"
FT   MOTIF           501..503
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000250"
FT   MOTIF           554..556
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        329..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..613
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1045 AA;  109993 MW;  58C3E9C7DC4BAFB9 CRC64;
     MKMLQGRLPL TVLHLFLLLG GGMTQQRPQG PIKDINGLPA QGPTVSVRPG PDPSDKVTFQ
     DCPVDIFFVL DTSESVALRV KPFKTLVTQV KEFTKKFIDK LTSRYYRCDR NLVWNAGALH
     YSDEVILINS LTRDMKTLRD NVETVEYIGK GTHTDCAIKR GIEEVLIGGS HQKENKYLIV
     VTDGHPLEGY KEPCGGLEDA ANEAKHLGIK VFSVAISPNH LEPRLSVIAS DASHRRNFTA
     TSAVGLTDDE IDNTIDTIID MIKENAEQGC CTYECKPSRG LSGPSGPPGY EGEIGKPGLP
     GDRGLPGDPG RQGDIGPVGY QGMKGDQGIR GEKGGRGAKG SKGDKGKRGI DGVDGQKGED
     GYNGLPGCKG SPGFDGAPGS SGPKGDPGPY GTKGEKGVPG TPGTGGRPGN TGNTGDKGDP
     GSNGLAGEKG ESGDEGDAGA DGSPGKRGEA GELGPPGVSG GRGARGEKGE PGPPGDQGRD
     GPAGPFGDPG EAGPQGPKGY RGDEGPRGPE GPKGPRGAKG LPGEQGIAGE RGDDGRPGNG
     TDGFPGFQGY PGSRGDPGSN GTKGYPGPKG DEGEQGEPGD DNVSPGPPGP KGAKGYRGPE
     GPPGPPGPGG PPGPDECEIL DIIKRMCSCC ECTCGPLDLL FVLDSSESIG LSNFQISKDF
     ILKVIDRLSR DEHVKFDADN SHVGVVQYSH GQTQEVVAMG DSSIQSIGQL KEAVKNLKWI
     AGGTWTGEAL AFTKDNLLKR FTLEKKIALV LTDGHSDILR DKTPLNTLCE VTPVVSVGVG
     DIFQNAPNSD QLVQISCGGK PYSKGLSLQR TSFAELLDDG FLHNVTSHMC SDRKCPDYTC
     PITYEGPADI TMLVDSSTRV GNQHFQTSKS FVKLLAERFL KAKPPPSGSA RVSVVQYSGQ
     NQQIVEAQFL TNYTVLEVPV DNMQFINGAT NVVSALRAVT ELYREDSLAG VNKKLLVFSD
     GNTQEEKGLL KVVQDAQSAG IEIYVLAVGS RLNYPNLQVM LTGSAADIAG PFPEERLFRV
     PDYTSLLQGV RYQSISRRIA LKSSQ