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Q4KLM6

- P3H2_RAT

UniProt

Q4KLM6 - P3H2_RAT

Protein

Prolyl 3-hydroxylase 2

Gene

Leprel1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (02 Aug 2005)
      Previous versions | rss
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    Functioni

    Shows prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V By similarity. Catalyzes the 3-hydroxyproline modification in -Xaa-Pro-Gly-sequences in collagens, especially alpha-1 type II and alpha-2 type V.By similarity1 Publication

    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 bindingi575 – 5751Iron
    Metal bindingi577 – 5771Iron
    Metal bindingi647 – 6471Iron
    Active sitei657 – 6571By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. collagen metabolic process Source: UniProtKB
    2. negative regulation of cell proliferation Source: UniProtKB
    3. peptidyl-proline hydroxylation Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    ReactomeiREACT_198584. Collagen biosynthesis and modifying enzymes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl 3-hydroxylase 2 (EC:1.14.11.7)
    Alternative name(s):
    Leprecan-like protein 1
    Gene namesi
    Name:Leprel1
    Synonyms:P3h2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1304568. Leprel1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 703682Prolyl 3-hydroxylase 2PRO_0000240358Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ4KLM6.
    PRIDEiQ4KLM6.

    PTM databases

    PhosphoSiteiQ4KLM6.

    Expressioni

    Gene expression databases

    GenevestigatoriQ4KLM6.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000002639.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4KLM6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati42 – 7534TPR 1Add
    BLAST
    Repeati144 – 17734TPR 2Add
    BLAST
    Repeati205 – 23834TPR 3Add
    BLAST
    Repeati301 – 33434TPR 4Add
    BLAST
    Domaini552 – 666115Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi700 – 7034Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the leprecan family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
    Contains 4 TPR repeats.Curated

    Keywords - Domaini

    Repeat, Signal, TPR repeat

    Phylogenomic databases

    eggNOGiNOG269251.
    HOGENOMiHOG000231087.
    HOVERGENiHBG053224.
    InParanoidiQ4KLM6.
    PhylomeDBiQ4KLM6.

    Family and domain databases

    Gene3Di1.25.40.10. 3 hits.
    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR011990. TPR-like_helical.
    IPR013105. TPR_2.
    [Graphical view]
    PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
    PF07719. TPR_2. 2 hits.
    [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.

    Q4KLM6-1 [UniParc]FASTAAdd to Basket

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    MRESTWVSLL LLLLLPAPQR GGPQDGRGSP EPEPERGPLQ PFDLLYASGV    50
    AAYYSGDYEG AVRDLEAALR SHRRLRDIRT RCARHCAARR PLAPPGAGPG 100
    AELPFFRAVL ERARCSRSCQ SQRLGGPASR HRVSEDVRSD FQRRVPYNYL 150
    QRAYIKLNQL DKAMEAAHTF FMANPEHMEM QQNIEDYKAT ARVEAPLVDR 200
    EAKPHLESYN AGVKHYEADD FEAAIKYFEQ ALREYFNEDM VCRALCEGPQ 250
    RFEEYEYLGS KGSLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL 300
    PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDDQDVLDN VDFYESLLDD 350
    STDPASIEAR EDLTAFVKRH KLEAELIKSA AEGLGFSYSE PNYWISYGGR 400
    QDENRVPSGV NMDGAEVHGL SMGKKSPPKI GRDLREGGPL LYENITFVYN 450
    SEQLNGTQRV LLDNVLSEEQ CRELHSVASG IMLVGDGYRG KTSPHTPNEK 500
    FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY FMLNSTLYFS 550
    YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY 600
    SALLYMNDDF EGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK 650
    AVTRGQRCAV ALWFTLDPLY RELERIQADE VIAILDQEQH GKHGLNINPK 700
    DEL 703
    Length:703
    Mass (Da):79,833
    Last modified:August 2, 2005 - v1
    Checksum:iEFE57CEF5F209B63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC099107 mRNA. Translation: AAH99107.1.
    RefSeqiNP_001020798.1. NM_001025627.1.
    UniGeneiRn.213595.

    Genome annotation databases

    GeneIDi288016.
    KEGGirno:288016.
    UCSCiRGD:1304568. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC099107 mRNA. Translation: AAH99107.1 .
    RefSeqi NP_001020798.1. NM_001025627.1.
    UniGenei Rn.213595.

    3D structure databases

    ProteinModelPortali Q4KLM6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000002639.

    PTM databases

    PhosphoSitei Q4KLM6.

    Proteomic databases

    PaxDbi Q4KLM6.
    PRIDEi Q4KLM6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 288016.
    KEGGi rno:288016.
    UCSCi RGD:1304568. rat.

    Organism-specific databases

    CTDi 55214.
    RGDi 1304568. Leprel1.

    Phylogenomic databases

    eggNOGi NOG269251.
    HOGENOMi HOG000231087.
    HOVERGENi HBG053224.
    InParanoidi Q4KLM6.
    PhylomeDBi Q4KLM6.

    Enzyme and pathway databases

    Reactomei REACT_198584. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    NextBioi 627416.
    PROi Q4KLM6.

    Gene expression databases

    Genevestigatori Q4KLM6.

    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.
    IPR013105. TPR_2.
    [Graphical view ]
    Pfami PF13640. 2OG-FeII_Oxy_3. 1 hit.
    PF07719. TPR_2. 2 hits.
    [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. "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: Placenta.
    2. "A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens."
      Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.
      J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PROLYL-3-HYDROXYLASE.

    Entry informationi

    Entry nameiP3H2_RAT
    AccessioniPrimary (citable) accession number: Q4KLM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: August 2, 2005
    Last modified: October 1, 2014
    This is version 77 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