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Q9R1J8

- P3H1_RAT

UniProt

Q9R1J8 - P3H1_RAT

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Protein
Prolyl 3-hydroxylase 1
Gene
Lepre1, P3h1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts By similarity.

Catalytic activityi

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-3-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactori

Iron By similarity.
Ascorbate By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi579 – 5791Iron
Metal bindingi581 – 5811Iron
Metal bindingi651 – 6511Iron
Active sitei661 – 6611 By similarity

GO - Molecular functioni

  1. L-ascorbic acid binding Source: UniProtKB-KW
  2. iron ion binding Source: InterPro
  3. procollagen-proline 3-dioxygenase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl 3-hydroxylase 1 (EC:1.14.11.7)
    Alternative name(s):
    Leucine- and proline-enriched proteoglycan 1
    Short name:
    Leprecan-1
    Gene namesi
    Name:Lepre1
    Synonyms:P3h1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi628823. Lepre1.

    Subcellular locationi

    Endoplasmic reticulum. Secretedextracellular spaceextracellular matrix
    Note: Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG).1 Publication

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414 Reviewed prediction
    Add
    BLAST
    Chaini15 – 728714Prolyl 3-hydroxylase 1
    PRO_0000240354Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi308 – 3081N-linked (GlcNAc...) Reviewed prediction
    Glycosylationi450 – 4501N-linked (GlcNAc...) Reviewed prediction
    Glycosylationi459 – 4591N-linked (GlcNAc...) Reviewed prediction
    Glycosylationi532 – 5321N-linked (GlcNAc...) Reviewed prediction

    Post-translational modificationi

    O-glycosylated; chondroitin sulfate.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9R1J8.
    PRIDEiQ9R1J8.

    Expressioni

    Tissue specificityi

    Expressed in basement membranes of cardiac muscle, skeletal muscle, central nervous system, intestinal tract, trachea, ear, skin, liver and kidney. In kidney, localizes to the glomerular basement membrane, mesangial matrix and Bowman's capsule of the nephron. In the renal parenchyma, expressed in the basement membranes of tubules and blood vessels. In the ear and trachea, localizes to the perimeter of resident chondrocytes in lacunae.1 Publication

    Gene expression databases

    GenevestigatoriQ9R1J8.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9R1J8. 1 interaction.
    MINTiMINT-1775508.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R1J8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati25 – 5834TPR 1
    Add
    BLAST
    Repeati135 – 16834TPR 2
    Add
    BLAST
    Repeati197 – 23034TPR 3
    Add
    BLAST
    Repeati293 – 32634TPR 4
    Add
    BLAST
    Domaini556 – 670115Fe2OG dioxygenase
    Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili393 – 43139 Reviewed prediction
    Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi725 – 7284Prevents secretion from ER Reviewed prediction

    Sequence similaritiesi

    Belongs to the leprecan family.
    Contains 4 TPR repeats.

    Keywords - Domaini

    Coiled coil, Repeat, Signal, TPR repeat

    Phylogenomic databases

    eggNOGiNOG269251.
    HOGENOMiHOG000231087.
    HOVERGENiHBG053224.
    KOiK08134.
    PhylomeDBiQ9R1J8.

    Family and domain databases

    Gene3Di1.25.40.10. 3 hits.
    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
    [Graphical view]
    SMARTiSM00702. P4Hc. 1 hit.
    [Graphical view]
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9R1J8-1 [UniParc]FASTAAdd to Basket

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    MVAVAAAAAS RATAESEPEW NVAAPDLLYA EGTAAYARGD WPGVVLNMER    50
    ALRSRAALRA LRLRCRTRCA TELPWAPDLD LGPASSLNHD PGAAALHDLR 100
    FFGALLRRAA CLRRCLGPPS AHLLSEELDL EFNKRSPYNY LQVAYFKINK 150
    LEKAVAAAHT FFVGNPEHME MRQNLDYYQT MSGVKEEDFK DLEAKPHMHE 200
    FRLGVRLYSE EKPLEAVPHL EAALQEYFVA DEECRALCEG PYDYDGYNYL 250
    DYSADLFQAI TDHYVQVLSC KQNCVTELAS HPSREKPFED FLPSHYNYLQ 300
    FAYYNIGNYT QAIECAKTYL LFFPNDEVMS QNLAYYTAVL GEEEASSISP 350
    RENAQEYRHR SLLEKELLFF AYDIFGIPFV DPDSWTPEEV IPKRLQEKQK 400
    SERETAVRIS QEIGNLMKEI ETLVEEKTKE SLDVSRLTRE GGPLLYEGIN 450
    LTMNSKVLNG SQRVVMDGVI SDDECQELQR LTNAAATSGD GYRGQTSPHT 500
    PNEKFYGVTV LKALKLGQEG KVPLQSAHMY YNVTEKVRRV MESYFRLDTP 550
    LYFSYSHLVC RTAIEESQAE RKDSSHPVHV DNCILNAESL VCIKEPPAYT 600
    FRDYSAILYL NGDFDGGNFY FTELDAKTVT AEVQPQCGRA VGFSSGTENP 650
    HGVKAVTRGQ RCAIALWFTL DPRHSERDRV QADDLVKMLF SPEEVDLPQE 700
    QPLPDQQGSP KPGEESLSDR ESQPKDEL 728
    Length:728
    Mass (Da):82,390
    Last modified:May 1, 2000 - v1
    Checksum:i06AFE6972BF3EE1F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087433 mRNA. Translation: AAD51875.1.
    RefSeqiNP_446119.1. NM_053667.1.
    UniGeneiRn.13741.

    Genome annotation databases

    GeneIDi114200.
    KEGGirno:114200.
    UCSCiRGD:628823. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087433 mRNA. Translation: AAD51875.1 .
    RefSeqi NP_446119.1. NM_053667.1.
    UniGenei Rn.13741.

    3D structure databases

    ProteinModelPortali Q9R1J8.
    ModBasei Search...

    Protein-protein interaction databases

    IntActi Q9R1J8. 1 interaction.
    MINTi MINT-1775508.

    Proteomic databases

    PaxDbi Q9R1J8.
    PRIDEi Q9R1J8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 114200.
    KEGGi rno:114200.
    UCSCi RGD:628823. rat.

    Organism-specific databases

    CTDi 64175.
    RGDi 628823. Lepre1.

    Phylogenomic databases

    eggNOGi NOG269251.
    HOGENOMi HOG000231087.
    HOVERGENi HBG053224.
    KOi K08134.
    PhylomeDBi Q9R1J8.

    Miscellaneous databases

    NextBioi 618365.
    PROi Q9R1J8.

    Gene expression databases

    Genevestigatori Q9R1J8.

    Family and domain databases

    Gene3Di 1.25.40.10. 3 hits.
    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a novel basement membrane-associated proteoglycan, leprecan."
      Wassenhove-McCarthy D.J., McCarthy K.J.
      J. Biol. Chem. 274:25004-25017(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Fibroblast.

    Entry informationi

    Entry nameiP3H1_RAT
    AccessioniPrimary (citable) accession number: Q9R1J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: May 1, 2000
    Last modified: April 16, 2014
    This is version 88 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

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