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Q9JI03

- CO5A1_RAT

UniProt

Q9JI03 - CO5A1_RAT

Protein

Collagen alpha-1(V) chain

Gene

Col5a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin By similarity.By similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: InterPro
    2. heparin binding Source: RGD

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(V) chain
    Gene namesi
    Name:Col5a1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi70920. Col5a1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen type V trimer Source: RGD

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 18401810Collagen alpha-1(V) chainPRO_0000041762Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei234 – 2341SulfotyrosineSequence Analysis
    Modified residuei236 – 2361SulfotyrosineSequence Analysis
    Modified residuei240 – 2401SulfotyrosineSequence Analysis
    Modified residuei262 – 2621SulfotyrosineSequence Analysis
    Modified residuei263 – 2631SulfotyrosineSequence Analysis
    Modified residuei336 – 3361SulfotyrosineSequence Analysis
    Modified residuei338 – 3381SulfotyrosineSequence Analysis
    Modified residuei344 – 3441SulfotyrosineSequence Analysis
    Modified residuei572 – 57214-hydroxyprolineBy similarity
    Modified residuei578 – 57814-hydroxyprolineBy similarity
    Modified residuei623 – 62314-hydroxyprolineBy similarity
    Modified residuei629 – 62915-hydroxylysineBy similarity
    Modified residuei641 – 64114-hydroxyprolineBy similarity
    Modified residuei644 – 64415-hydroxylysineBy similarity
    Modified residuei650 – 65014-hydroxyprolineBy similarity
    Modified residuei656 – 65614-hydroxyprolineBy similarity
    Modified residuei659 – 65914-hydroxyprolineBy similarity
    Modified residuei677 – 67714-hydroxyprolineBy similarity
    Modified residuei680 – 68014-hydroxyprolineBy similarity
    Modified residuei682 – 68213-hydroxyprolineBy similarity
    Modified residuei688 – 68813-hydroxyprolineBy similarity
    Modified residuei692 – 69214-hydroxyprolineBy similarity
    Modified residuei698 – 69814-hydroxyprolineBy similarity
    Modified residuei707 – 70714-hydroxyprolineBy similarity
    Modified residuei710 – 71015-hydroxylysineBy similarity
    Modified residuei719 – 71914-hydroxyprolineBy similarity
    Modified residuei722 – 72214-hydroxyprolineBy similarity
    Modified residuei728 – 72814-hydroxyprolineBy similarity
    Modified residuei734 – 73414-hydroxyprolineBy similarity
    Modified residuei746 – 74615-hydroxylysineBy similarity
    Modified residuei752 – 75214-hydroxyprolineBy similarity
    Modified residuei758 – 75814-hydroxyprolineBy similarity
    Modified residuei764 – 76414-hydroxyprolineBy similarity
    Modified residuei767 – 76714-hydroxyprolineBy similarity
    Modified residuei773 – 77314-hydroxyprolineBy similarity
    Modified residuei776 – 77615-hydroxylysineBy similarity
    Modified residuei782 – 78214-hydroxyprolineBy similarity
    Modified residuei791 – 79114-hydroxyprolineBy similarity
    Modified residuei797 – 79715-hydroxylysineBy similarity
    Modified residuei806 – 80615-hydroxylysineBy similarity
    Modified residuei809 – 80915-hydroxylysineBy similarity
    Modified residuei812 – 81215-hydroxylysineBy similarity
    Modified residuei818 – 81814-hydroxyprolineBy similarity
    Modified residuei821 – 82115-hydroxylysineBy similarity
    Modified residuei836 – 83614-hydroxyprolineBy similarity
    Modified residuei848 – 84815-hydroxylysineBy similarity
    Modified residuei866 – 86615-hydroxylysineBy similarity
    Modified residuei872 – 87214-hydroxyprolineBy similarity
    Modified residuei875 – 87514-hydroxyprolineBy similarity
    Modified residuei878 – 87814-hydroxyprolineBy similarity
    Modified residuei884 – 88415-hydroxylysineBy similarity
    Modified residuei890 – 89014-hydroxyprolineBy similarity
    Modified residuei893 – 89314-hydroxyprolineBy similarity
    Modified residuei899 – 89915-hydroxylysineBy similarity
    Modified residuei905 – 90514-hydroxyprolineBy similarity
    Modified residuei908 – 90814-hydroxyprolineBy similarity
    Modified residuei932 – 93214-hydroxyprolineBy similarity
    Modified residuei947 – 94714-hydroxyprolineBy similarity
    Modified residuei1019 – 101914-hydroxyprolineBy similarity
    Modified residuei1022 – 102214-hydroxyprolineBy similarity
    Modified residuei1025 – 102514-hydroxyprolineBy similarity
    Modified residuei1031 – 103114-hydroxyprolineBy similarity
    Modified residuei1223 – 122314-hydroxyprolineBy similarity
    Modified residuei1226 – 122614-hydroxyprolineBy similarity
    Modified residuei1469 – 146914-hydroxyprolineBy similarity
    Modified residuei1472 – 147214-hydroxyprolineBy similarity
    Modified residuei1603 – 16031SulfotyrosineSequence Analysis
    Modified residuei1606 – 16061SulfotyrosineSequence Analysis

    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.By similarity
    Sulfated on 40% of tyrosines.By similarity
    Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

    Keywords - PTMi

    Hydroxylation, Sulfation

    Proteomic databases

    PaxDbiQ9JI03.
    PRIDEiQ9JI03.

    Expressioni

    Tissue specificityi

    A high molecular weight form was detected in Schwann cells and peripheral nerve. A lower, probably processed form, is detected in all other tissues tested (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriQ9JI03.

    Interactioni

    Subunit structurei

    Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta. Interacts with CSPG4 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9JI03. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JI03.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 244173Laminin G-likeAdd
    BLAST
    Domaini1611 – 1839229Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni231 – 445215Nonhelical regionBy similarityAdd
    BLAST
    Regioni446 – 560115Interrupted collagenous regionBy similarityAdd
    BLAST
    Regioni561 – 15721012Triple-helical regionBy similarityAdd
    BLAST
    Regioni1573 – 160735Nonhelical regionBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    InParanoidiQ9JI03.
    KOiK06236.
    PhylomeDBiQ9JI03.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000885. Fib_collagen_C.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51461. NC1_FIB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9JI03-1 [UniParc]FASTAAdd to Basket

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    MDVHTRWKAP RPGAPLLSSP LLLLLLLLWA PPPSRAAQPT DLLEMLDFHN     50
    LPSGVTKTTG FCATRRSSKE PDVAYRVSKD AQLSMPTKQL YPESDFPEDF 100
    SILTTVKAKK GSQAFLVSVY NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE 150
    EYPLFPGINL SDGKWHRIAI SVYKKNVTLI LDCKKKITKF LNRGDHPIID 200
    VNGIIMFGSR ILDDEIFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD 250
    TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP SQKPVEAARE 300
    TTEVPEEQTQ PPSEAPTVPE TSDTAGKEDN PGIGDYDYVP TDDYYTTSPY 350
    EDFGYGEGVE NPDQPTNPDS GAEIPTSTSV TSNSSNPAPS PEEGKDDLGG 400
    EFTEETIKNL DENYYDPYFD PDSDSNVSPS EIGPGMPANQ DTIYEGIGGP 450
    RGEKGQKGEP AIIEPGMLIE GPPGPEGPAG LPGPPGTTGP TGQMGDPGER 500
    GPPGRPGLPG ADGLPGPPGT MLMLPFRFGG GGDAGSKGPM VSAQESQAQA 550
    ILQQARLALR GPAGPMGLTG RPGPMGPPGS GGLKGEPGDM GPQGPRGVQG 600
    PPGPTGKPGR RGRAGSDGAR GMPGQTGPKG DRGFDGLAGL PGEKGHRGDP 650
    GPSGPPGLPG DDGERGDDGE VGPRGLPGEP GPRGLLGPKG PPGPPGPPGV 700
    TGMDGQPGPK GNVGPQGEPG PPGQQGNPGA QGLPGPQGAI GPPGEKGPLG 750
    KPGLPGMPGA DGPPGHPGKE GPPGEKGGQG PPGPQGPIGY PGPRGVKGAD 800
    GIRGLKGTKG EKGEDGFPGF KGDMGIKGDR GEIGPPGPRG EDGPEGPKGR 850
    GGPNGDPGPL GPTGEKGKLG VPGLPGYPGR QGPKGSIGFP GFPGANGEKG 900
    GRGTPGKPGP RGQRGPTGPR GERGPRGITG KPGPKGNSGG DGPAGPPGER 950
    GPNGPQGPTG FPGPKGPPGP PGKDGLPGHP GQRGETGFQG KTGPPGPPGV 1000
    VGPQGPTGET GPMGERGHPG PPGPPGEQGL PGAAGKEGTK GDPGPAGLPG 1050
    KDGPPGLRGF PGDRGLPGPV GALGLKGSEG PPGPPGPAGS PGERGPAGAA 1100
    GPIGIPGRPG PQGPPGPAGE KGVPGEEGPQ GPAGRDGLQG PVGLPGPAGP 1150
    VGPPGEDGDK GEIGEPGQKG SKGDKGEQGP PGPTGPQGPT GQPGPSGADG 1200
    EPGPRGQQGL FGQKGDEGSR GFPGPPGPVG LQGLPGPPGE KGETGDVGQM 1250
    GPPGPPGPRG PSGAPGADGP QGPPGGIGNP GAVGEKGEPG EAGEPGLPGE 1300
    GGPLGPKGER GEKGEAGPSG AAGPPGPKGP PGDDGPKGSP GPVGFPGDPG 1350
    PPGEPGPAGQ DGPPGDKGDD GEPGQTGSPG PTGEPGPSGP PGKRGPPGPA 1400
    GPEGRQGEKG AKGEAGLEGP PGKTGPIGPQ GAPGKPGPDG LRGIPGPVGE 1450
    QGLPGSPGPD GPPGPMGPPG LPGLKGDSGP KGEKGHPGLI GLIGPPGEQG 1500
    EKGDRGLPGP QGSSGPKGEQ GITGPSGPLG PPGPPGLPGP PGPKGAKGSS 1550
    GPTGPKGEAG HPGLPGPPGP PGEVIQPLPI QASRTRRNID ASQLLDDGAG 1600
    ESYVDYADGM EEIFGSLNSL KLEIEQMKRP LGTQQNPART CKDLQLCHPD 1650
    FPDGEYWVDP NQGCSRDSFK VYCNFTAGGS TCVFPDKKSE GARITSWPKE 1700
    NPGSWFSEFK RGKLLSYVDA EGNPVGVVQM TFLRLLSASA QQNITYNCYQ 1750
    SVAWQDAATG SYDKAIRFLG SNDEEMSYDN NPYIRALVDG CATKKGYQKT 1800
    VLEIDTPKVE QVPIVDIMFT DFGEASQKFG FEVGPACFLG 1840
    Length:1,840
    Mass (Da):183,987
    Last modified:October 1, 2000 - v1
    Checksum:iAD38F5FF886B923C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272662 mRNA. Translation: AAF76433.1.
    RefSeqiNP_604447.1. NM_134452.1.
    UniGeneiRn.117.

    Genome annotation databases

    GeneIDi85490.
    KEGGirno:85490.
    UCSCiRGD:70920. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272662 mRNA. Translation: AAF76433.1 .
    RefSeqi NP_604447.1. NM_134452.1.
    UniGenei Rn.117.

    3D structure databases

    ProteinModelPortali Q9JI03.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JI03. 1 interaction.

    Proteomic databases

    PaxDbi Q9JI03.
    PRIDEi Q9JI03.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 85490.
    KEGGi rno:85490.
    UCSCi RGD:70920. rat.

    Organism-specific databases

    CTDi 1289.
    RGDi 70920. Col5a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    InParanoidi Q9JI03.
    KOi K06236.
    PhylomeDBi Q9JI03.

    Miscellaneous databases

    NextBioi 617576.

    Gene expression databases

    Genevestigatori Q9JI03.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000885. Fib_collagen_C.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51461. NC1_FIB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Schwann cells synthesize type V collagen that contains a novel alpha 4 chain. Molecular cloning, biochemical characterization, and high affinity heparin binding of alpha 4(V) collagen."
      Chernousov M.A., Rothblum K., Tyler W.A., Stahl R.C., Carey D.J.
      J. Biol. Chem. 275:28208-28215(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, HEPARIN-BINDING.
      Strain: Sprague-Dawley.
      Tissue: Schwann cell.

    Entry informationi

    Entry nameiCO5A1_RAT
    AccessioniPrimary (citable) accession number: Q9JI03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: October 1, 2000
    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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3