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P04258

- CO3A1_BOVIN

UniProt

P04258 - CO3A1_BOVIN

Protein

Collagen alpha-1(III) chain

Gene

COL3A1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      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

    GO - Biological processi

    1. cerebral cortex development Source: UniProtKB
    2. negative regulation of neuron migration Source: UniProtKB
    3. positive regulation of Rho protein signal transduction Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_209041. Scavenging by Class A Receptors.
    REACT_222217. ECM proteoglycans.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(III) chain
    Gene namesi
    Name:COL3A1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    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
    Chaini1 – 10491049Collagen alpha-1(III) chainPRO_0000059398Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei95 – 9515-hydroxylysine2 Publications
    Modified residuei107 – 10715-hydroxylysine2 Publications
    Glycosylationi107 – 1071O-linked (Gal...)1 Publication
    Modified residuei119 – 11915-hydroxylysine2 Publications
    Modified residuei938 – 93815-hydroxylysine2 Publications
    Modified residuei950 – 95015-hydroxylysine2 Publications
    Glycosylationi950 – 9501O-linked (Gal...)
    Disulfide bondi1040 – 1040Interchain
    Disulfide bondi1041 – 1041Interchain

    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.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP04258.
    PRIDEiP04258.

    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

    STRINGi9913.ENSBTAP00000028617.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1414Nonhelical region (N-terminal)Add
    BLAST
    Regioni15 – 10401026Triple-helical regionAdd
    BLAST
    Regioni1041 – 10499Nonhelical region (C-terminal)

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.Curated

    Keywords - Domaini

    Collagen, Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.

    Family and domain databases

    InterProiIPR008160. Collagen.
    [Graphical view]
    PfamiPF01391. Collagen. 7 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04258-1 [UniParc]FASTAAdd to Basket

    « Hide

    EYEAYDVKSG VAGGGIAGYP GPAGPPGPPG PPGTSGHPGA PGAPGYQGPP     50
    GEPGQAGPAG PPGPPGAIGP SGKDGESGRP GRPGPRGFPG PPGMKGPAGM 100
    PGFPGMKGHR GFDGRNGEKG EPGAPGLKGE NGVPGEDGAP GPMGPRGAPG 150
    ERGRPGLPGA AGARGNDGAR GSDGQPGPPG PPGTAGFPGS PGAKGEVGPA 200
    GSPGSSGAPG QRGEPGPQGH AGAPGPPGPP GSDGSPGGKG EMGPAGIPGA 250
    PGLIGARGPP GPPGTNGVPG QRGAAGEPGK NGAKGDPGPR GERGEAGSPG 300
    IAGPKGEDGK DGSPGEPGAN GLPGAAGERG VPGFRGPAGA NGLPGEKGPP 350
    GDRGGPGPAG PRGVAGEPGR NGLPGGPGLR GIPGSPGGPG SNGKPGPPGS 400
    QGETGRPGPP GSPGPRGQPG VMGFPGPKGN DGAPGKNGER GGPGGPGPQG 450
    PAGKNGETGP QGPPGPTGPS GDKGDTGPPG PQGLQGLPGT SGPPGENGKP 500
    GEPGPKGEAG APGIPGGKGD SGAPGERGPP GAGGPPGPRG GAGPPGPEGG 550
    KGAAGPPGPP GSAGTPGLQG MPGERGGPGG PGPKGDKGEP GSSGVDGAPG 600
    KDGPRGPTGP IGPPGPAGQP GDKGESGAPG VPGIAGPRGG PGERGEQGPP 650
    GPAGFPGAPG QNGEPGAKGE RGAPGEKGEG GPPGAAGPAG GSGPAGPPGP 700
    QGVKGERGSP GGPGAAGFPG GRGPPGPPGS NGNPGPPGSS GAPGKDGPPG 750
    PPGSNGAPGS PGISGPKGDS GPPGERGAPG PQGPPGAPGP LGIAGLTGAR 800
    GLAGPPGMPG ARGSPGPQGI KGENGKPGPS GQNGERGPPG PQGLPGLAGT 850
    AGEPGRDGNP GSDGLPGRDG APGAKGDRGE NGSPGAPGAP GHPGPPGPVG 900
    PAGKSGDRGE TGPAGPSGAP GPAGSRGPPG PQGPRGDKGE TGERGAMGIK 950
    GHRGFPGNPG APGSPGPAGH QGAVGSPGPA GPRGPVGPSG PPGKDGASGH 1000
    PGPIGPPGPR GNRGERGSEG SPGHPGQPGP PGPPGAPGPC CGAGGVAAI 1049
    Length:1,049
    Mass (Da):93,651
    Last modified:March 20, 1987 - v1
    Checksum:i8EEC33D1C66EC9A3
    GO

    Sequence databases

    PIRiA02862. CGBO7S.
    UniGeneiBt.64714.

    Cross-referencesi

    Sequence databases

    PIRi A02862. CGBO7S.
    UniGenei Bt.64714.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000028617.

    Proteomic databases

    PaxDbi P04258.
    PRIDEi P04258.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.

    Enzyme and pathway databases

    Reactomei REACT_209041. Scavenging by Class A Receptors.
    REACT_222217. ECM proteoglycans.

    Family and domain databases

    InterProi IPR008160. Collagen.
    [Graphical view ]
    Pfami PF01391. Collagen. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (positions 1-222)."
      Fietzek P.P., Allmann H., Rauterberg J., Henkel W., Wachter E., Kuhn K.
      Hoppe-Seyler's Z. Physiol. Chem. 360:809-820(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-242, HYDROXYLATION.
    2. "The covalent structure of calf skin type III collagen. II. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB1,8,10,2 (positions 223-402)."
      Dewes H., Fietzek P.P., Kuhn K.
      Hoppe-Seyler's Z. Physiol. Chem. 360:821-832(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 243-422.
    3. "The covalent structure of calf skin type III collagen. III. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB4 (positions 403-551)."
      Bentz H., Fietzek P.P., Kuhn K.
      Hoppe-Seyler's Z. Physiol. Chem. 360:833-840(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 423-571.
    4. "The covalent structure of calf skin type III collagen. IV. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB5 (positions 552-788)."
      Lang H., Glanville R.W., Fietzek P.P., Kuhn K.
      Hoppe-Seyler's Z. Physiol. Chem. 360:841-850(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 572-808.
    5. "The covalent structure of calf skin type III collagen. V. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB9A (position 789-927)."
      Dewes H., Fietzek P.P., Kuhn K.
      Hoppe-Seyler's Z. Physiol. Chem. 360:851-860(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 809-947, HYDROXYLATION.
    6. "The covalent structure of calf skin type III collagen. VI. The amino acid sequence of the carboxyterminal cyanogen bromide peptide alpha 1(III)CB9B (positions 928-1028)."
      Allmann H., Fietzek P.P., Glanville R.W., Kuhn K.
      Hoppe-Seyler's Z. Physiol. Chem. 360:861-868(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 948-1049, HYDROXYLATION.

    Entry informationi

    Entry nameiCO3A1_BOVIN
    AccessioniPrimary (citable) accession number: P04258
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3