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P12105

- CO3A1_CHICK

UniProt

P12105 - CO3A1_CHICK

Protein

Collagen alpha-1(III) chain

Gene

COL3A1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (29 Aug 2001)
      Previous versions | rss
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    Functioni

    Collagen type III occurs in most soft connective tissues along with type I collagen.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1076 – 10761CalciumBy similarity
    Metal bindingi1078 – 10781CalciumBy similarity
    Metal bindingi1079 – 10791Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1081 – 10811Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1084 – 10841CalciumBy similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: InterPro
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_197897. Syndecan interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(III) chain
    Gene namesi
    Name:COL3A1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. extracellular region Source: Reactome
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 150127N-terminal propeptideBy similarityPRO_0000005737Add
    BLAST
    Chaini151 – 1017867Collagen alpha-1(III) chainPRO_0000005738Add
    BLAST
    Propeptidei1018 – 1262245C-terminal propeptideBy similarityPRO_0000005739Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei262 – 26215-hydroxylysineBy similarity
    Modified residuei283 – 28315-hydroxylysineBy similarity
    Modified residuei859 – 85915-hydroxylysineBy similarity
    Disulfide bondi994 – 994InterchainPROSITE-ProRule annotation
    Disulfide bondi995 – 995InterchainPROSITE-ProRule annotation
    Disulfide bondi1058 ↔ 1090PROSITE-ProRule annotation
    Disulfide bondi1064 – 1064Interchain (with C-1285)PROSITE-ProRule annotation
    Disulfide bondi1081 – 1081Interchain (with C-1268)PROSITE-ProRule annotation
    Disulfide bondi1098 ↔ 1260PROSITE-ProRule annotation
    Glycosylationi1163 – 11631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1168 ↔ 1213PROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP12105.

    Interactioni

    Subunit structurei

    Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.

    Structurei

    3D structure databases

    ProteinModelPortaliP12105.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 8860VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1028 – 1262235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni145 – 16420Nonhelical region (N-terminal)Add
    BLAST
    Regioni165 – 994830Triple-helical regionAdd
    BLAST
    Regioni995 – 10039Nonhelical region (C-terminal)

    Domaini

    The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.By similarity

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG004933.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 7 hits.
    PF00093. VWC. 1 hit.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    PROSITEiPS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragments.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMSFVQKVSL FILAVFQPSV ILAQQDALGG CTHLGQEYAD RDVWKPEPCQ     50
    ICVCDSGSVL CDDIICDDQE LDCPNPEIPL GECCPVCPQT TPQPTELPYT 100
    QGPKGDPGSP GSPGRTGAPG PPGQPGSPGA PGPPGICQSC PSISGGSFSP 150
    QYDSYDVKAG SVGMGYPPQP ISGFPGPPGP SGPPGPPGHA GPPGSNGYQG 200
    PPGEPGQPGP SGPPGPAGMI GPAGPPGKDG EPGRPGRNGD RGIPGLPGHK 250
    GHPGMPGMPG MKGARGFDGK DGAKGDSGAP GPKGEAGQPG ANGSPGQPGP 300
    GGPTGERGRP GNPGGPGAHG KDGAPGTAGP LGPPGPPGTA GFPGSPGFKG 350
    EAGPPGPAGA SGNPGERGEP GPQGQAGPPG PQGPPGRAGS PGGKGEMGPS 400
    GIPGGPGPPG GRGLPGPPGT SGNPGAKGTP GEPGKNGAKG DPGPKGERGE 450
    NGTPGARGPP GEEGKRGANG EPGQNGVPGT PGERGSPGFR GLPGSNGLPG 500
    EKGPAGERGS PGPPGPSGPA GDRGQDGGPG LPGMRGLPGI PGSPGSDGKP 550
    GPPGNQGEPG RSGPPGPAGP RGQPGVMGFP GPKGNEGAPG KNGERGPGGP 600
    PGTPGPAGKN GDVGLPGPPG PAGPAGDRGE PGPSGSPGLQ GLPGGPGPAG 650
    ENGKPGEPGP KGDIGGPGFP GPKGENGIPG ERGPQGPPGP TGARGGPGPA 700
    GSEGAKGPPG PPGAPGGTGL PGLQGMPGER GASGSPGPKG DKGEPGGKGA 750
    DGLPGARGER GNVGPIGPPG PAGPPGDKGE TGPAGAPGPA GSRGGPGERG 800
    EQGLPGPAGF PGAPGQNGEP GGKGERGPPG LRGEAGPPGA AGPQGGPGAP 850
    GPPGPQGVKG ERGSPGGPGA AGFPGARGPP GPPGNNGDRG ESGPPGVPGP 900
    PGHPGPAGNN GAPGKAGERG FQGPLGPQGA IGSPGASGAR GPPGPAGPPG 950
    KDGRGGYPGP IGPPGPRGNR GESGPAGPPG QPGLPGPSGP PGPCCGGGVA 1000
    SLGAGEKGPV GYGYEYRDEP KENEINLGEI MSSMKSINNQ IENILSPDGS 1050
    RKNPARNCRD LKFCHPELKS GEYWIDPNQG CKMDAIKVYC NMETGETCLS 1100
    ANPATVPRKN WWTTESSGKK HVWFGESMKG GFQFSYGDPD LPEDVSEVQL 1150
    AFLRILSSRA SQNITYHCKN SIAYMNQASG NVKKALKLMS SVETDIKAEG 1200
    NSKYMYAVLE DGCTKHTGEW GKTVFEYRTR KTMRLPVVDI APIDIGGPDQ 1250
    EFGVDVGPVC FL 1262
    Length:1,262
    Mass (Da):121,249
    Last modified:August 29, 2001 - v2
    Checksum:i96ABE7B2E9DEB43D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961E → K(PubMed:6547770)Curated
    Sequence conflicti881 – 8811G → R in CAA23689. (PubMed:6298201)Curated
    Sequence conflicti884 – 8841G → V in CAA23689. (PubMed:6298201)Curated
    Non-adjacent residuesi886 – 8872Curated
    Non-adjacent residuesi922 – 9232Curated
    Sequence conflicti984 – 9841L → V in CAA23690. (PubMed:6298201)Curated
    Sequence conflicti1132 – 11321F → S in AAA18519. (PubMed:6856474)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07973 mRNA. Translation: AAA83407.1.
    X00822, X00823 Genomic DNA. Translation: CAB52686.1.
    X00826, X00825 Genomic DNA. Translation: CAA25397.1. Sequence problems.
    X00827 Genomic DNA. Translation: CAA25398.1.
    X00828 Genomic DNA. Translation: CAA25399.1.
    X00830 Genomic DNA. Translation: CAA25401.1.
    X00831 Genomic DNA. Translation: CAA25402.1.
    K02302 Genomic DNA. Translation: AAD15299.1.
    K02301 Genomic DNA. Translation: AAD15298.1.
    V00391 Genomic DNA. Translation: CAA23689.1.
    V00392 Genomic DNA. Translation: CAA23690.1.
    M36662 Unassigned DNA. Translation: AAA18519.1. Sequence problems.
    PIRiA05269.
    I50694.
    UniGeneiGga.42140.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07973 mRNA. Translation: AAA83407.1 .
    X00822 , X00823 Genomic DNA. Translation: CAB52686.1 .
    X00826 , X00825 Genomic DNA. Translation: CAA25397.1 . Sequence problems.
    X00827 Genomic DNA. Translation: CAA25398.1 .
    X00828 Genomic DNA. Translation: CAA25399.1 .
    X00830 Genomic DNA. Translation: CAA25401.1 .
    X00831 Genomic DNA. Translation: CAA25402.1 .
    K02302 Genomic DNA. Translation: AAD15299.1 .
    K02301 Genomic DNA. Translation: AAD15298.1 .
    V00391 Genomic DNA. Translation: CAA23689.1 .
    V00392 Genomic DNA. Translation: CAA23690.1 .
    M36662 Unassigned DNA. Translation: AAA18519.1 . Sequence problems.
    PIRi A05269.
    I50694.
    UniGenei Gga.42140.

    3D structure databases

    ProteinModelPortali P12105.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P12105.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.

    Enzyme and pathway databases

    Reactomei REACT_197897. Syndecan interactions.

    Miscellaneous databases

    PROi P12105.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 7 hits.
    PF00093. VWC. 1 hit.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    PROSITEi PS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An alternative transcript of the chick type III collagen gene that does not encode type III collagen."
      Nah H.-D., Niu Z., Adams S.L.
      J. Biol. Chem. 269:16443-16448(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-886.
      Tissue: Kidney.
    2. "Conservation of the sizes for one but not another class of exons in two chick collagen genes."
      Yamada Y., Liau G., Mudryj M., Obici S., de Crombrugghe B.
      Nature 310:333-337(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-96; 332-397; 431-484; 503-535 AND 869-976.
    3. "Isolation and characterization of a genomic clone encoding chick alpha-1 type III collagen."
      Yamada Y., Mudryj M., Sullivan M., de Crombrugghe B.
      J. Biol. Chem. 258:2758-2761(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 869-886 AND 977-994.
    4. "A conserved nucleotide sequence, coding for a segment of the C-propeptide, is found at the same location in different collagen genes."
      Yamada Y., Kuhn K., de Crombrugghe B.
      Nucleic Acids Res. 11:2733-2744(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 977-1262.

    Entry informationi

    Entry nameiCO3A1_CHICK
    AccessioniPrimary (citable) accession number: P12105
    Secondary accession number(s): P79758
    , P79759, Q90790, Q90791, Q90794, Q92029
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3