CO6A3_CHICK
ID CO6A3_CHICK Reviewed; 3137 AA.
AC P15989;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Collagen alpha-3(VI) chain;
DE Flags: Precursor;
GN Name=COL6A3;
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] OF 1-853.
RC TISSUE=Aorta;
RX PubMed=1977751; DOI=10.1083/jcb.111.5.2197;
RA Doliana R., Bonaldo P., Colombatti A.;
RT "Multiple forms of chicken alpha 3(VI) collagen chain generated by
RT alternative splicing in type A repeated domains.";
RL J. Cell Biol. 111:2197-2205(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-2871.
RX PubMed=2322559; DOI=10.1021/bi00457a021;
RA Bonaldo P., Russo V., Bucciotti F., Doliana R., Colombatti A.;
RT "Structural and functional features of the alpha 3 chain indicate a
RT bridging role for chicken collagen VI in connective tissues.";
RL Biochemistry 29:1245-1254(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2871-3137.
RX PubMed=2584214; DOI=10.1016/s0021-9258(19)47052-x;
RA Bonaldo P., Colombatti A.;
RT "The carboxyl terminus of the chicken alpha 3 chain of collagen VI is a
RT unique mosaic structure with glycoprotein Ib-like, fibronectin type III,
RT and Kunitz modules.";
RL J. Biol. Chem. 264:20235-20239(1989).
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=1;
CC Comment=At least 2 isoforms are produced.;
CC Name=1;
CC IsoId=P15989-1; Sequence=Displayed;
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; M24282; AAA03201.1; -; mRNA.
DR PIR; A37797; A37797.
DR SMR; P15989; -.
DR STRING; 9031.ENSGALP00000006240; -.
DR PaxDb; P15989; -.
DR PRIDE; P15989; -.
DR VEuPathDB; HostDB:geneid_396548; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P15989; -.
DR OrthoDB; 1049829at2759; -.
DR PhylomeDB; P15989; -.
DR Proteomes; UP000000539; Unplaced.
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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00109; KU; 1.
DR CDD; cd01481; vWA_collagen_alpha3-VI-like; 6.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 11.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR041900; vWA_collagen_alpha3-VI-like.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 11.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 12.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF53300; SSF53300; 12.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50234; VWFA; 12.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..3137
FT /note="Collagen alpha-3(VI) chain"
FT /id="PRO_0000005846"
FT DOMAIN 38..212
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 241..418
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 444..623
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 644..817
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 842..1014
FT /note="VWFA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1035..1207
FT /note="VWFA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1239..1410
FT /note="VWFA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1441..1621
FT /note="VWFA 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1641..1814
FT /note="VWFA 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1840..2029
FT /note="VWFA 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2407..2587
FT /note="VWFA 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2625..2821
FT /note="VWFA 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2957..3051
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3068..3137
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 26..2042
FT /note="Nonhelical region"
FT REGION 2043..2379
FT /note="Triple-helical region"
FT REGION 2045..2372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2166..2172
FT /note="Interruption in collagenous region"
FT REGION 2254..2259
FT /note="Interruption in collagenous region"
FT REGION 2308..2309
FT /note="Interruption in collagenous region"
FT REGION 2380..3137
FT /note="Nonhelical region"
FT REGION 2887..2956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2045..2047
FT /note="Cell attachment site"
FT MOTIF 2153..2155
FT /note="Cell attachment site"
FT MOTIF 2159..2161
FT /note="Cell attachment site"
FT COMPBIAS 2113..2129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2140..2162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2297..2311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2887..2949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 3082..3083
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2084
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3072..3122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 3081..3105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 3097..3118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 3137 AA; 339599 MW; ECB428578B536357 CRC64;
MRKHRHLPLA AILGLLLSGF CSVGAQQQAA VRNVAVADII FLVDSSWSIG KEHFQLVREF
LYDVVKALDV GGNDFRFALV QFSGNPHTEF QLNTYPSNQD VLSHIANMPY MGGGSKTGKG
LEYLIENHLT KAAGSRASEG VPQVIIVLTD GQSQDDVALP SSVLKSAHVN MIAVGVQDAV
EGELKEIASR PFDTHLFNLE NFTALHGIVG DLVASVRTSM TPEQAGAKGL VKDITAQESA
DLIFLIDGSD NIGSVNFQAI RDFLVNLIES LRVGAQQIHI GVVQYSDQPR TEFALNSYST
KADVLDAVKA LSFRGGKEAN TGAALEYVVE NLFTQAGGSR IEEAVPQILV LISGGESSDD
IREGLLAVKQ ASIFSFSIGV LNADSAELQQ IATDGSFAFT ALDIRNLAAL RELLLPNIVG
VAQRLILLEA PTIVTEVIEV NKKDIVFLID GSTALGTGPF NSIRDFVAKI VQRLEVGPDL
IQVAVAQYAD TVRPEFYFNT HQNRKDVMAN VKKMKLMGGT ALNTGSALDF VRNNFFTSAA
GCRMEEGVLP MLVLITGGKS MDAVEQAAAE MKRNRIVILA VGSRNADVAE LQEIAHERDF
VFQPNDFRLQ FMQAILPEVL SPIRTLSGGM VIHETPSVQV TKRDIIFLLD GSLNVGNANF
PFVRDFVVTL VNYLDVGTDK IRVGLVQFSD TPKTEFSLYS YQTKSDIIQR LGQLRPKGGS
VLNTGSALNF VLSNHFTEAG GSRINEQVPQ VLVLVTAGRS AVPFLQVSND LARAGVLTFA
VGVRNADKAE LEQIAFNPKM VYFMDDFSDL TTLPQELKKP ITTIVSGGVE EVPLAPTESK
KDILFLIDGS ANLLGSFPAV RDFIHKVISD LNVGPDATRV AVAQFSDNIQ IEFDFAELPS
KQDMLLKVKR MRLKTGKQLN IGVALDEVMR RLFVKEAGSR IEEGIPQFLV LLAAGRSTDE
VERPSGALKE AGVVTFAIKA KNADLSELER IAYAPQFILN VESLPRISEL QANIVNLLKT
IQFQPTVVER GEKKDVVFLI DGSDGVRRGF PLLKTFVERV VESLDIGRDK VRVAIVQYSN
AIQPEFLLDA YEDKADLVSA IQALTIMGGS PLNTGAALDY LIKNVFTVSS GSRIAEGVPQ
FLILLTADRS QDDVRRPSVV LKTSGTVPFG IGIGNADLTE LQTISFLPDF AISVPDFSQL
DSVQQAVSNR VIRLTKKEIE SLAPDLVFTS PSPVGVKRDV VFLVDGSRYA AQEFYLIRDL
IERIVNNLDV GFDTTRISVV QFSEHPHVEF LLNAHSTKDE VQGAVRRLRP RGGQQVNVGE
ALEFVAKTIF TRPSGSRIEE GVPQFLVILS SRKSDDDLEF PSVQVKQVGV APMVIAKNMD
PEEMVQISLS PDYVFQVSSF QELPSLEQKL LAPIETLTAD QIRQLLGDVT TIPDVSGEEK
DVVFLIDSSD SVRSDGLAHI RDFISRIVQQ LDVGPNKVRI GVVQFSNNVF PEFYLRTHKS
KNAVLQAIRR LRLRGGYPVN AGKALDYVVK NYFIKSAGSR IEDGVPQHLV VILGDQSQDD
VNRPANVISS TSIQPLGVGA RNVDRNQLQV ITNDPGRVLV VQDFTGLPTL ERKVQNILEE
LTVPTTEGPV YPGPEGKKQA DIVFLLDGSI NLGRDNFQEV LQFVYSIVDA IYEDGDSIQV
GLAQYNSDVT DEFFLKDYSS KPEILDAINK VIYKGGRVAN TGAAIKHLQA KHFVKEAGSR
IDQRVPQIAF IITGGKSSDD GQGASMEVAQ KGVKVFAVGV RNIDLEEVSK LASESATSFR
VSTAQELSEL NEQVLVTLAA AMKEKLCPGT TDVTRDCDLD VILGFDVSDV GAGQNIFNSQ
RGLESRVEAV LNRITQMQKI SCTGSRAPSV RVAIMAQSRG GPVEGLDFSE YQPELFERFQ
GMRTRGPYFL TAETLKSYQN KFRSAPSGST KVVIHFTDGT DDYLDQMKTA SADLRRQGVH
ALLFVGLDRV KNFEEVMQLE FGRGFTYNRP LRVNLLDLDF ELAEQLDNIA ERTCCGVPCK
CSGQRGDRGL PGPIGPKGAT GEIGYGGYPG DEGGPGERGP PGVNGTQGFQ GCPGHRGTKG
SRGFPGEKGE LGEMGLDGID GEEGDKGLPG FSGEKGFSGR RGSKGAKGER GERGDRGLRG
DPGESGADNT QRGTRGQKGE IGQMGEPGPA GQRGQDGGVG RKGMAGRRGP IGVKGTKGAL
GQPGPAGEQG MRGPQGPPGQ IGTPGIRGEQ GIPGPRAGGG QPGAPGERGR IGPLGRKGEP
GNPGPRGPNG QQGPRGEMGD DGRDGIGGPG PKGRKGERGF VGYPGPKGGP GDRGGAGGPG
PKGNRGRRGN AGNPGTPGQK GEIGYPGPSG LKGDKGPSIS QCALVQNIKD KCPCCYGPKE
CPVFPTELAF AIDTSSGVGR DVFNRMKQTV LRVVSNLTIA ESNCPRGARV ALVTYNNEVT
TEIRFADARK KSSLLQQIQN FQATLTTKPR SLETAMSFVA RNTFKRARSG FLMRKVAVFF
SNGETRASPQ LNDAVLKLYD AGVTPVFLTS RQDAVLERAL EINNTAVGHA IVLPTSGSQL
NDTIRRLLTC HVCLDVCEPD PICGYGSQRP VFRDRRAAPT DVDTDIAFIM DSSASTTPLQ
FNEMKKYISH LVSNMEISSE PKISQHHARV AVLQQAPYDH ETNSSFPPVK TEFSLTDYGS
KEKIINYLHN QMTQLYGTMA MGSAVEHTVA HVFESAPNPR DLKVIVLMIT GKMEKQELEY
LREAVIDAKC KGYLFVILGI GKNVDVKNIY SLASEPNDVF FKLVSKPGEL HEEPLLRFGR
LLPSFIRSDF AFYLSPEIRK QCKWLQADQT PKSPGHTGQK AVYIAPNGTV TQTISTTTTL
STTFKPAAST SAHAKTTTAS TTAQTRATER PTESTTVQVN ATVQSQGSTA ANTKATSRTT
TSTTAAAASG RRRQGAKMND IQITDVTENS ARLRWASPEP HNAYVFDLAI TLAHDHSLVL
KQNVTGTERV IGGLRSGQKY LVFITGYLKS QPKVTYTGTF STKTPAQPKV ALANMMLNAE
PLEGPENVMD ICLLQKEEGT CRDFVLKWHY DLKTKSCARF WYGGCGGNEN RFNTQKECEK
ACSPGNISPG VVTTIGT
