Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6JHU8

- P3H1_CHICK

UniProt

Q6JHU8 - P3H1_CHICK

Protein

Prolyl 3-hydroxylase 1

Gene

LEPRE1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 secretoty pathway of cells. Has growth suppressive activity in fibroblasts By similarity.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 bindingi580 – 5801Iron
    Metal bindingi582 – 5821Iron
    Metal bindingi652 – 6521Iron
    Active sitei662 – 6621By 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: MGI
    4. protein binding Source: IntAct
    5. protein complex binding Source: UniProt

    GO - Biological processi

    1. cell growth Source: Ensembl
    2. chaperone-mediated protein folding Source: UniProt
    3. collagen fibril organization Source: Ensembl
    4. collagen metabolic process Source: MGI
    5. peptidyl-proline hydroxylation Source: GOC
    6. regulation of ossification Source: Ensembl

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    ReactomeiREACT_198187. Collagen biosynthesis and modifying enzymes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl 3-hydroxylase 1 (EC:1.14.11.7)
    Alternative name(s):
    Leucine- and proline-enriched proteoglycan 1 homolog
    Short name:
    Leprecan-1 homolog
    Gene namesi
    Name:LEPRE1
    Synonyms:P3H1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 21

    Subcellular locationi

    Endoplasmic reticulum PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. macromolecular complex Source: UniProt
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 725711Prolyl 3-hydroxylase 1PRO_0000240355Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi533 – 5331N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ6JHU8.

    Expressioni

    Tissue specificityi

    Expressed in embryonic dermis, tendon, cartilage, liver and kidney. Expression in the kidney is restricted to the calyx. In the liver, expression is restricted to the interlobular septum.1 Publication

    Interactioni

    Subunit structurei

    Binds unfolded collagen in a complex with CYPB and CRTAP.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRTAPQ908303EBI-1169258,EBI-1169253

    Protein-protein interaction databases

    IntActiQ6JHU8. 1 interaction.
    STRINGi9031.ENSGALP00000007707.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6JHU8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati36 – 6934TPR 1Add
    BLAST
    Repeati136 – 16934TPR 2Add
    BLAST
    Repeati198 – 23134TPR 3Add
    BLAST
    Repeati294 – 32734TPR 4Add
    BLAST
    Domaini557 – 671115Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili394 – 44148Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi722 – 7254Prevents 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

    Coiled coil, Repeat, Signal, TPR repeat

    Phylogenomic databases

    eggNOGiNOG269251.
    GeneTreeiENSGT00550000074573.
    HOVERGENiHBG053224.
    KOiK08134.
    PhylomeDBiQ6JHU8.

    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]
    PfamiPF13640. 2OG-FeII_Oxy_3. 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.

    Q6JHU8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLLPLLPL LVWAAGPPGP LGPPEHSEPP LPAEPPDALF AAGAEAYARG    50
    DWPAVVLQME RALRARAAIR ARSVRCRLRC ANATAVVPTD GLEPTLHDLL 100
    FFRGLLRRAA CLRGCGPTQP SRYRLGEELE REFRKRSPYN YLQVAYFKIN 150
    KVAKAVAAAH TFFVANPEHV EMKQNLEYYQ MMAGVRESDF ADLEARPHMT 200
    EFRLGVRFYS EEQPAAAVLH LEKALQEYFV ADTECRALCE GPYDYEGYNY 250
    LEYNADLFQA MTDHYMQVLS CKQGCVTELA SQPGREKPLE DFLPSHFNYL 300
    QFAYYNNGNY EKAIECAKTY LLFFPNDEVM NQNLAYYTAV LGEDLARPIE 350
    PRKEIQAYRQ RSLMEKELLF FSYDVFGIPF VDPDTWTPEE VIPKRLREKQ 400
    KVERETAARI SEEIGNLMKE IETLVEEKAK ESAEMSKFIR EGGPLVYEGA 450
    SVTMNSKSLN GSQRVVVDGV LSAEECRELQ RLTNAAASAG DGYRGKTSPH 500
    TPSETFYGVT VLKALKLGQE GKVPLQSAHL YYNVTEKVRH MMESYFRLEV 550
    PLHFSYSHLV CRTAIDEKQE GRSDNSHEVH VDNCILNAEA LVCVKEPPAY 600
    TFRDYSAILY LNGDFEGGAF YFTELDAKTQ TAEVQPQCGR AVGFSSGSEN 650
    PHGVKAVTKG QRCAIALWFT LDPRHSERER VQADDLVKML FRTEEVDLLQ 700
    ETSAEQEPTA ATSTAGLHAA GKDEL 725
    Length:725
    Mass (Da):81,676
    Last modified:July 5, 2004 - v1
    Checksum:i2D227635DA36B605
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY463528 mRNA. Translation: AAS45237.1.
    RefSeqiNP_001001529.1. NM_001001529.1.
    UniGeneiGga.9766.

    Genome annotation databases

    EnsembliENSGALT00000007719; ENSGALP00000007707; ENSGALG00000004833.
    GeneIDi414142.
    KEGGigga:414142.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY463528 mRNA. Translation: AAS45237.1 .
    RefSeqi NP_001001529.1. NM_001001529.1.
    UniGenei Gga.9766.

    3D structure databases

    ProteinModelPortali Q6JHU8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q6JHU8. 1 interaction.
    STRINGi 9031.ENSGALP00000007707.

    Proteomic databases

    PaxDbi Q6JHU8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000007719 ; ENSGALP00000007707 ; ENSGALG00000004833 .
    GeneIDi 414142.
    KEGGi gga:414142.

    Organism-specific databases

    CTDi 64175.

    Phylogenomic databases

    eggNOGi NOG269251.
    GeneTreei ENSGT00550000074573.
    HOVERGENi HBG053224.
    KOi K08134.
    PhylomeDBi Q6JHU8.

    Enzyme and pathway databases

    Reactomei REACT_198187. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    NextBioi 20818679.
    PROi Q6JHU8.

    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 PF13640. 2OG-FeII_Oxy_3. 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. "Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes."
      Vranka J.A., Sakai L.Y., Bachinger H.P.
      J. Biol. Chem. 279:23615-23621(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, COMPONENT OF A UNFOLDED COLLAGEN-BINDING COMPLEX INCLUDING P3H1; CYPB AND CRTAP, CHARACTERIZATION, TISSUE SPECIFICITY.
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiP3H1_CHICK
    AccessioniPrimary (citable) accession number: Q6JHU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: July 5, 2004
    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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3