CO6A2_CHICK
ID CO6A2_CHICK Reviewed; 1022 AA.
AC P15988; Q6LEJ6; Q90583; Q90604;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Collagen alpha-2(VI) chain;
DE Flags: Precursor;
GN Name=COL6A2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2787244; DOI=10.1002/j.1460-2075.1989.tb03475.x;
RA Koller E., Winterhalter K.H., Trueb B.;
RT "The globular domains of type VI collagen are related to the collagen-
RT binding domains of cartilage matrix protein and von Willebrand factor.";
RL EMBO J. 8:1073-1077(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=2015818; DOI=10.1111/j.1432-1033.1991.tb15896.x;
RA Hayman A.R., Koppel J., Trueb B.;
RT "Complete structure of the chicken alpha 2(VI) collagen gene.";
RL Eur. J. Biochem. 197:177-184(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-38.
RC TISSUE=Liver;
RX PubMed=2011522; DOI=10.1093/nar/19.3.485;
RA Koller E., Hayman A.R., Trueb B.;
RT "The promoter of the chicken alpha 2(VI) collagen gene has features
RT characteristic of house-keeping genes and of proto-oncogenes.";
RL Nucleic Acids Res. 19:485-491(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 77-796.
RX PubMed=2491845; DOI=10.1016/s0021-9258(17)31234-6;
RA Trueb B., Schaeren-Wiemers N., Schreier T., Winterhalter K.H.;
RT "Molecular cloning of chicken type VI collagen: primary structure of the
RT subunit alpha-2(VI)-pepsin.";
RL J. Biol. Chem. 264:136-140(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 273-680.
RX PubMed=2351679; DOI=10.1016/s0021-9258(19)38751-4;
RA Hayman A.R., Koeppel J., Winterhalter K.H., Trueb B.;
RT "The triple-helical domain of alpha-2 (VI) collagen is encoded by 19 short
RT exons that are multiples of 9 base pairs.";
RL J. Biol. Chem. 265:9864-9868(1990).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein.
CC -!- SUBUNIT: Trimers composed of three different chains: alpha 1(VI), alpha
CC 2(VI), and alpha 3(VI).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15988-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15988-2; Sequence=VSP_001165, VSP_001166;
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; X15041; CAA33144.1; -; mRNA.
DR EMBL; X56659; CAA39982.1; -; Genomic_DNA.
DR EMBL; X56659; CAA39981.1; -; Genomic_DNA.
DR EMBL; X56595; CAA39933.1; -; Genomic_DNA.
DR EMBL; J04425; AAA48705.1; -; Genomic_RNA.
DR EMBL; J05475; AAA49132.1; -; Genomic_DNA.
DR PIR; S23377; S23377.
DR PIR; S23378; S04111.
DR RefSeq; NP_990679.1; NM_205348.3. [P15988-1]
DR RefSeq; XP_015144623.1; XM_015289137.1. [P15988-2]
DR AlphaFoldDB; P15988; -.
DR SMR; P15988; -.
DR STRING; 9031.ENSGALP00000042596; -.
DR PaxDb; P15988; -.
DR PRIDE; P15988; -.
DR Ensembl; ENSGALT00000064755; ENSGALP00000053721; ENSGALG00000039216. [P15988-2]
DR Ensembl; ENSGALT00000065376; ENSGALP00000043563; ENSGALG00000039216. [P15988-1]
DR GeneID; 396292; -.
DR KEGG; gga:396292; -.
DR CTD; 1292; -.
DR VEuPathDB; HostDB:geneid_396292; -.
DR GeneTree; ENSGT00940000155682; -.
DR InParanoid; P15988; -.
DR OMA; GNERQEW; -.
DR OrthoDB; 140989at2759; -.
DR PhylomeDB; P15988; -.
DR TreeFam; TF331207; -.
DR Reactome; R-GGA-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:P15988; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000039216; Expressed in colon and 11 other tissues.
DR ExpressionAtlas; P15988; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 4.
DR Pfam; PF00092; VWA; 3.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF53300; SSF53300; 3.
DR PROSITE; PS50234; VWFA; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Collagen; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT CHAIN 28..1022
FT /note="Collagen alpha-2(VI) chain"
FT /id="PRO_0000005834"
FT DOMAIN 44..168
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 613..738
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 833..957
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 28..255
FT /note="Nonhelical region"
FT REGION 256..590
FT /note="Triple-helical region"
FT REGION 263..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..519
FT /note="Interruption in collagenous region"
FT REGION 591..1022
FT /note="Nonhelical region"
FT MOTIF 348..350
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 366..368
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 426..428
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 444..446
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 465..467
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 489..491
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 498..500
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 344..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 821..918
FT /note="ELAVAQCTQRPVDIVFLLDGSERIGEQNFHRAHHFVEQVAQQLTLARRNDDN
FT MNARIALLQYGSEREQNVVFPLTYNLTEISNALAQIKYLDSSSNIG -> DDRNPGNVN
FT PLIFRPMEEGVNINIPSTIHSIAQFLNSTRETQDPRMYTQLVATLAFTAEKAKFATGNE
FT RQEWMDLFIDTFKMVHSEIVGDPETVLGLC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001165"
FT VAR_SEQ 919..1022
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001166"
FT CONFLICT 658..680
FT /note="ARVGVVQYSHEGTFEAIKLDDER -> LECVWGGAGGRSGDGQKKRVLDP
FT (in Ref. 5; AAA49132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1022 AA; 109177 MW; 5194CFD1475AE893 CRC64;
MSRRTAEMFQ QAFLSTLLCV ALVPLHAQFD DEPVTSCTEK TDCPISVYFV IDTSESIALQ
TVPIQSLVDQ IKQFIPRFIE KLENEVYQNQ VSITWMFGGL HYSDVVEIYS PLTRSKDTYL
TKLRAIRYLG RGTFTDCAIS NMTQQFQSQT ARDVKFAVVI TDGHVTGSPC GGMKMQAERA
RDMGIKLFAV APSEDVYEQG LREIASPPHD LYRSNYTITP KDALHIDENT IERIIKAMKH
EAYAECYKMT CLEIAGPAGP KGYRGQKGAK GNMGEPGSPG LKGRQGDPGI EGPIGYPGPK
GVPGLKGEKG EIGSDGRRGA AGLAGRNGTD GQKGKLGRIG PPGCKGDRGD KGPDGYPGDA
GDQGERGDEG MKGDPGRPGR SGPPGPPGEK GSPGIPGNPG AQGPGGTKGR KGETGPPGPK
GEPGRRGDPG TKGSKGGPGA KGERGDPGPE GPRGLPGEVG NKGARGDQGL PGPRGPTGAV
GEPGNIGSRG DPGDLGPRGD AGPPGPKGDR GRPGFSYPGP RGPQGDKGEK GQPGPKGGRG
ELGPKGTQGT KGEKGEPGDP GPRGEPGTRG PPGEAGPEGT PGPPGDPGLT DCDVMTYVRE
TCGCCDCEKR CGALDIMFVI DSSESIGYTN FTLEKNFVVN VVSRLGSIAK DPKSETGARV
GVVQYSHEGT FEAIKLDDER INSLSSFKEA VKRLEWIAGG TWTPSALQFA YNKLIKESRR
EKAQVFAVVI TDGRYDPRDD DKNLGALCGR DVLVNTIGIG DIFDQPEQSE TLVSIACNEP
QRVQKMRLFS DLVAEEFIDK MEDMLCPDPQ IVCPELPCQT ELAVAQCTQR PVDIVFLLDG
SERIGEQNFH RAHHFVEQVA QQLTLARRND DNMNARIALL QYGSEREQNV VFPLTYNLTE
ISNALAQIKY LDSSSNIGSA IIHAINNIVL SPGNGQRVAR RNAELSFVFI TDGITGSKNL
EEAINSMKKQ DVMPTVVALG SDVDMDVLLK LGLGDRAAIF REKDYESLSQ PSFFDRFIRW
IC
