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P13941

- CO3A1_RAT

UniProt

P13941 - CO3A1_RAT

Protein

Collagen alpha-1(III) chain

Gene

Col3a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of Gpr56 in the developing brain and binding to Gpr56 inhibits neuronal migration and activates the RhoA pathway by coupling Gpr56 to Gna13 and possibly Gna12 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1277 – 12771CalciumBy similarity
    Metal bindingi1279 – 12791CalciumBy similarity
    Metal bindingi1280 – 12801Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1282 – 12821Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1285 – 12851CalciumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. aging Source: RGD
    2. blood vessel development Source: Ensembl
    3. cell-matrix adhesion Source: Ensembl
    4. cellular response to amino acid stimulus Source: Ensembl
    5. cerebral cortex development Source: UniProtKB
    6. collagen biosynthetic process Source: Ensembl
    7. collagen fibril organization Source: Ensembl
    8. digestive tract development Source: Ensembl
    9. extracellular fibril organization Source: Ensembl
    10. heart development Source: Ensembl
    11. integrin-mediated signaling pathway Source: Ensembl
    12. negative regulation of immune response Source: Ensembl
    13. negative regulation of neuron migration Source: UniProtKB
    14. peptide cross-linking Source: Ensembl
    15. positive regulation of Rho protein signal transduction Source: UniProtKB
    16. response to cytokine Source: Ensembl
    17. response to mechanical stimulus Source: RGD
    18. response to radiation Source: Ensembl
    19. skeletal system development Source: RGD
    20. skin development Source: Ensembl
    21. transforming growth factor beta receptor signaling pathway Source: Ensembl
    22. wound healing Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_195275. Extracellular matrix organization.
    REACT_198300. Syndecan interactions.
    REACT_198584. Collagen biosynthesis and modifying enzymes.
    REACT_198733. Scavenging by Class A Receptors.
    REACT_198756. Non-integrin membrane-ECM interactions.
    REACT_198757. ECM proteoglycans.
    REACT_199129. Assembly of collagen fibrils and other multimeric structures.
    REACT_199177. Collagen degradation.
    REACT_212371. Signaling by PDGF.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(III) chain
    Gene namesi
    Name:Col3a1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 9

    Organism-specific databases

    RGDi71029. Col3a1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen type III trimer Source: Ensembl
    2. extracellular matrix Source: RGD
    3. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323By similarityAdd
    BLAST
    Propeptidei24 – 154131N-terminal propeptideBy similarityPRO_0000005746Add
    BLAST
    Chaini155 – 12181064Collagen alpha-1(III) chainPRO_0000005747Add
    BLAST
    Propeptidei1219 – 1463245C-terminal propeptideBy similarityPRO_0000043408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei262 – 26215-hydroxylysine; alternateBy similarity
    Glycosylationi262 – 2621O-linked (Gal...); alternateBy similarity
    Modified residuei283 – 28315-hydroxylysineBy similarity
    Modified residuei859 – 85915-hydroxylysineBy similarity
    Modified residuei976 – 97615-hydroxylysineBy similarity
    Modified residuei1093 – 109315-hydroxylysineBy similarity
    Modified residuei1105 – 110515-hydroxylysineBy similarity
    Disulfide bondi1195 – 1195InterchainPROSITE-ProRule annotation
    Disulfide bondi1196 – 1196InterchainPROSITE-ProRule annotation
    Disulfide bondi1259 ↔ 1291PROSITE-ProRule annotation
    Disulfide bondi1265 – 1265Interchain (with C-1282)PROSITE-ProRule annotation
    Disulfide bondi1282 – 1282Interchain (with C-1265)PROSITE-ProRule annotation
    Disulfide bondi1299 ↔ 1461PROSITE-ProRule annotation
    Disulfide bondi1369 ↔ 1414PROSITE-ProRule annotation

    Post-translational modificationi

    O-glycosylated.By similarity
    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

    PaxDbiP13941.
    PRIDEiP13941.

    Expressioni

    Gene expression databases

    GenevestigatoriP13941.

    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.

    Protein-protein interaction databases

    IntActiP13941. 1 interaction.
    STRINGi10116.ENSRNOP00000004956.

    Structurei

    3D structure databases

    ProteinModelPortaliP13941.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 9060VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1229 – 1463235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 16915Nonhelical region (N-terminal)Add
    BLAST
    Regioni170 – 11951026Triple-helical regionAdd
    BLAST

    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.
    GeneTreeiENSGT00740000114967.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    InParanoidiP13941.
    KOiK06236.
    OMAiKYVWFGE.
    OrthoDBiEOG7TJ3HH.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 4 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: Complete.

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

    P13941-1 [UniParc]FASTAAdd to Basket

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    MMSFVQCGTW FLLTLLHPSL ILAQQSNVDE LGCNYLGQSY ESRDVWKPEP     50
    CQICVCDSGS VLCDDIMCDD EPLDCPNPEI PFGECCAICP QPSTPAPVIP 100
    DGNRPQGPKG DPGPPGIPGR NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ 150
    NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP PGPPGSSGHP GSPGSPGYQG 200
    PPGEPGQAGP AGPPGPPGAI GPSGPAGKDG ESGRPGRPGE RGLPGPPGIK 250
    GPAGIPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP 300
    RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG 350
    EVGPAGSPGS NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA 400
    GIPGAPGLLG ARGPPGPAGA NGAPGQRGPS GEPGKNGAKG EPGARGERGE 450
    AGSPGIPGPK GEDGKDGSPG EPGANGVPGN PGERGAPGFR GPAGPNGAPG 500
    EKGPAGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS PGGPGNDGKP 550
    GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG 600
    PGLPGPAGKN GETGPQGPPG PTGAPGDKGD AGPPGPQGLQ GIPGTSGPPG 650
    ENGKPGEPGP KGEAGAPGVP GGKGDSGAPG ERGPPGTAGT PGLRGGAGPP 700
    GPEGGKGPAG PPGPPGTSGP PGLQGMPGER GGPGSPGPKG EKGEPGGAGA 750
    DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE GGAPGLPGIA GPRGGPGERG 800
    EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGA AGPPGGSGPA 850
    GPPGPQGVKG ERGSPGGPGA AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK 900
    DGPPGPAGNS GSPGNPGVAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG 950
    LTGARGLAGP PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP 1000
    GQPGTAGEPG RDGNPGSDGQ PGRDGSPGGK GDRGENGSPG APGAPGHPGP 1050
    PGPVGPSGKN GDRGETGPAG PSGAPGPAGA RGAPGPQGPR GDKGETGERG 1100
    SNGIKGHRGF PGNPGPPGSP GAAGHQGAVG SPGPAGPRGP VGPHGPPGKD 1150
    GSSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA 1200
    AIAGVGGEKS GGFSPYYGDD PMDFKINTEE IMSSLKSVNG QIESLISPDG 1250
    SRKNPARNCR DLKFCHPELK SGEYWVDPNQ GCKMDAIKVF CNMETGETCI 1300
    NASPMTVPRK HWWTDAGAEK KHVWFGESMN GGFQFSYGNP DLPEDVLDVQ 1350
    LAFLRLLSSR ASQNITYHCK NSIAYMDQAN GNVKKSLKLM GSNEGEFKAE 1400
    GNSKFTYTVL EDGCTKHTGE WSKTVFEYQT RKAMRLPIID IAPYDIGGPD 1450
    QEFGVDIGPV CFL 1463
    Length:1,463
    Mass (Da):138,936
    Last modified:December 6, 2005 - v3
    Checksum:i63C218CD2BCA47B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1167 – 11671N → D in CAA06510. 1 PublicationCurated
    Sequence conflicti1256 – 12561A → G in CAA06510. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC087039 mRNA. Translation: AAH87039.1.
    X70369 mRNA. Translation: CAA49832.1.
    AJ005395 mRNA. Translation: CAA06510.1.
    M21354 mRNA. Translation: AAA40942.1.
    PIRiS41067.
    RefSeqiNP_114474.1. NM_032085.1.
    UniGeneiRn.3247.

    Genome annotation databases

    EnsembliENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357.
    GeneIDi84032.
    KEGGirno:84032.
    UCSCiRGD:71029. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC087039 mRNA. Translation: AAH87039.1 .
    X70369 mRNA. Translation: CAA49832.1 .
    AJ005395 mRNA. Translation: CAA06510.1 .
    M21354 mRNA. Translation: AAA40942.1 .
    PIRi S41067.
    RefSeqi NP_114474.1. NM_032085.1.
    UniGenei Rn.3247.

    3D structure databases

    ProteinModelPortali P13941.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13941. 1 interaction.
    STRINGi 10116.ENSRNOP00000004956.

    Proteomic databases

    PaxDbi P13941.
    PRIDEi P13941.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000004956 ; ENSRNOP00000004956 ; ENSRNOG00000003357 .
    GeneIDi 84032.
    KEGGi rno:84032.
    UCSCi RGD:71029. rat.

    Organism-specific databases

    CTDi 1281.
    RGDi 71029. Col3a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00740000114967.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    InParanoidi P13941.
    KOi K06236.
    OMAi KYVWFGE.
    OrthoDBi EOG7TJ3HH.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_195275. Extracellular matrix organization.
    REACT_198300. Syndecan interactions.
    REACT_198584. Collagen biosynthesis and modifying enzymes.
    REACT_198733. Scavenging by Class A Receptors.
    REACT_198756. Non-integrin membrane-ECM interactions.
    REACT_198757. ECM proteoglycans.
    REACT_199129. Assembly of collagen fibrils and other multimeric structures.
    REACT_199177. Collagen degradation.
    REACT_212371. Signaling by PDGF.

    Miscellaneous databases

    NextBioi 616623.
    PROi P13941.

    Gene expression databases

    Genevestigatori P13941.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 4 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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    2. "Cloning of cDNA for rat pro alpha 1(III) collagen mRNA. Different expression patterns of type I and type III collagen and fibronectin genes in experimental granulation tissue."
      Glumoff V., Maekelae J.K., Vuorio E.
      Biochim. Biophys. Acta 1217:41-48(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 828-1463.
    3. Wurtz T., Ellerstroem C., Lundmark C., Christersson C.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 900-1463.
      Strain: Sprague-Dawley.
      Tissue: Fibroblast.
    4. "Regulation of alpha 2(I), alpha 1(III), and alpha 2(V) collagen mRNAs by estradiol in the immature rat uterus."
      Frankel F.R., Hsu C.-Y.J., Meyers J.C., Lin E., Lyttle C.R., Komm B., Mohn K.
      DNA 7:347-354(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1135-1309.

    Entry informationi

    Entry nameiCO3A1_RAT
    AccessioniPrimary (citable) accession number: P13941
    Secondary accession number(s): O70604, Q5PQT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 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