CO3A1_CHICK
ID CO3A1_CHICK Reviewed; 1262 AA.
AC P12105; P79758; P79759; Q90790; Q90791; Q90794; Q92029;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Collagen alpha-1(III) chain;
DE Flags: Precursor; Fragments;
GN Name=COL3A1;
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 1-886.
RC TISSUE=Kidney;
RX PubMed=8206952; DOI=10.1016/s0021-9258(17)34026-7;
RA Nah H.-D., Niu Z., Adams S.L.;
RT "An alternative transcript of the chick type III collagen gene that does
RT not encode type III collagen.";
RL J. Biol. Chem. 269:16443-16448(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-96; 332-397; 431-484; 503-535 AND
RP 869-976.
RX PubMed=6547770; DOI=10.1038/310333a0;
RA Yamada Y., Liau G., Mudryj M., Obici S., de Crombrugghe B.;
RT "Conservation of the sizes for one but not another class of exons in two
RT chick collagen genes.";
RL Nature 310:333-337(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 869-886 AND 977-994.
RX PubMed=6298201; DOI=10.1016/s0021-9258(18)32779-0;
RA Yamada Y., Mudryj M., Sullivan M., de Crombrugghe B.;
RT "Isolation and characterization of a genomic clone encoding chick alpha-1
RT type III collagen.";
RL J. Biol. Chem. 258:2758-2761(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 977-1262.
RX PubMed=6856474; DOI=10.1093/nar/11.9.2733;
RA Yamada Y., Kuhn K., de Crombrugghe B.;
RT "A conserved nucleotide sequence, coding for a segment of the C-propeptide,
RT is found at the same location in different collagen genes.";
RL Nucleic Acids Res. 11:2733-2744(1983).
CC -!- FUNCTION: Collagen type III occurs in most soft connective tissues
CC along with type I collagen.
CC -!- SUBUNIT: Trimers of identical alpha 1(III) chains. The chains are
CC linked to each other by interchain disulfide bonds. Trimers are also
CC cross-linked via hydroxylysines.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
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 fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; U07973; AAA83407.1; -; mRNA.
DR EMBL; X00822; CAB52686.1; -; Genomic_DNA.
DR EMBL; X00823; CAB52686.1; JOINED; Genomic_DNA.
DR EMBL; X00826; CAA25397.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X00825; CAA25397.1; JOINED; Genomic_DNA.
DR EMBL; X00827; CAA25398.1; -; Genomic_DNA.
DR EMBL; X00828; CAA25399.1; -; Genomic_DNA.
DR EMBL; X00830; CAA25401.1; -; Genomic_DNA.
DR EMBL; X00831; CAA25402.1; -; Genomic_DNA.
DR EMBL; K02302; AAD15299.1; -; Genomic_DNA.
DR EMBL; K02301; AAD15298.1; -; Genomic_DNA.
DR EMBL; V00391; CAA23689.1; -; Genomic_DNA.
DR EMBL; V00392; CAA23690.1; -; Genomic_DNA.
DR EMBL; M36662; AAA18519.1; ALT_SEQ; Unassigned_DNA.
DR PIR; A05269; A05269.
DR PIR; I50694; I50694.
DR AlphaFoldDB; P12105; -.
DR SMR; P12105; -.
DR PRIDE; P12105; -.
DR VEuPathDB; HostDB:geneid_396243; -.
DR VEuPathDB; HostDB:geneid_396340; -.
DR VEuPathDB; HostDB:geneid_424526; -.
DR InParanoid; P12105; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..150
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005737"
FT CHAIN 151..1017
FT /note="Collagen alpha-1(III) chain"
FT /id="PRO_0000005738"
FT PROPEP 1018..1262
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005739"
FT DOMAIN 29..88
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1028..1262
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 95..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..164
FT /note="Nonhelical region (N-terminal)"
FT REGION 160..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..994
FT /note="Triple-helical region"
FT REGION 995..1003
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 114..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1076
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1078
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1079
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1081
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1084
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 283
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 859
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 994
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 995
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1058..1090
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1064
FT /note="Interchain (with C-1285)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1081
FT /note="Interchain (with C-1268)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1098..1260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1168..1213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 96
FT /note="E -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="G -> R (in Ref. 3; CAA23689)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="G -> V (in Ref. 3; CAA23689)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="L -> V (in Ref. 3; CAA23690)"
FT /evidence="ECO:0000305"
FT CONFLICT 1132
FT /note="F -> S (in Ref. 4; AAA18519)"
FT /evidence="ECO:0000305"
FT NON_CONS 886..887
FT /evidence="ECO:0000305"
FT NON_CONS 922..923
FT /evidence="ECO:0000305"
SQ SEQUENCE 1262 AA; 121249 MW; 96ABE7B2E9DEB43D CRC64;
MMSFVQKVSL FILAVFQPSV ILAQQDALGG CTHLGQEYAD RDVWKPEPCQ ICVCDSGSVL
CDDIICDDQE LDCPNPEIPL GECCPVCPQT TPQPTELPYT QGPKGDPGSP GSPGRTGAPG
PPGQPGSPGA PGPPGICQSC PSISGGSFSP QYDSYDVKAG SVGMGYPPQP ISGFPGPPGP
SGPPGPPGHA GPPGSNGYQG PPGEPGQPGP SGPPGPAGMI GPAGPPGKDG EPGRPGRNGD
RGIPGLPGHK GHPGMPGMPG MKGARGFDGK DGAKGDSGAP GPKGEAGQPG ANGSPGQPGP
GGPTGERGRP GNPGGPGAHG KDGAPGTAGP LGPPGPPGTA GFPGSPGFKG EAGPPGPAGA
SGNPGERGEP GPQGQAGPPG PQGPPGRAGS PGGKGEMGPS GIPGGPGPPG GRGLPGPPGT
SGNPGAKGTP GEPGKNGAKG DPGPKGERGE NGTPGARGPP GEEGKRGANG EPGQNGVPGT
PGERGSPGFR GLPGSNGLPG EKGPAGERGS PGPPGPSGPA GDRGQDGGPG LPGMRGLPGI
PGSPGSDGKP GPPGNQGEPG RSGPPGPAGP RGQPGVMGFP GPKGNEGAPG KNGERGPGGP
PGTPGPAGKN GDVGLPGPPG PAGPAGDRGE PGPSGSPGLQ GLPGGPGPAG ENGKPGEPGP
KGDIGGPGFP GPKGENGIPG ERGPQGPPGP TGARGGPGPA GSEGAKGPPG PPGAPGGTGL
PGLQGMPGER GASGSPGPKG DKGEPGGKGA DGLPGARGER GNVGPIGPPG PAGPPGDKGE
TGPAGAPGPA GSRGGPGERG EQGLPGPAGF PGAPGQNGEP GGKGERGPPG LRGEAGPPGA
AGPQGGPGAP GPPGPQGVKG ERGSPGGPGA AGFPGARGPP GPPGNNGDRG ESGPPGVPGP
PGHPGPAGNN GAPGKAGERG FQGPLGPQGA IGSPGASGAR GPPGPAGPPG KDGRGGYPGP
IGPPGPRGNR GESGPAGPPG QPGLPGPSGP PGPCCGGGVA SLGAGEKGPV GYGYEYRDEP
KENEINLGEI MSSMKSINNQ IENILSPDGS RKNPARNCRD LKFCHPELKS GEYWIDPNQG
CKMDAIKVYC NMETGETCLS ANPATVPRKN WWTTESSGKK HVWFGESMKG GFQFSYGDPD
LPEDVSEVQL AFLRILSSRA SQNITYHCKN SIAYMNQASG NVKKALKLMS SVETDIKAEG
NSKYMYAVLE DGCTKHTGEW GKTVFEYRTR KTMRLPVVDI APIDIGGPDQ EFGVDVGPVC
FL
