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Protein

Prolyl 3-hydroxylase 1

Gene

P3H1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi580 – 5801Iron
Metal bindingi582 – 5821Iron
Metal bindingi652 – 6521Iron
Active sitei662 – 6621By similarity

GO - Molecular functioni

  • iron ion binding Source: InterPro
  • L-ascorbic acid binding Source: UniProtKB-KW
  • procollagen-proline 3-dioxygenase activity Source: MGI
  • protein complex binding Source: UniProtKB

GO - Biological processi

  • bone development Source: Ensembl
  • chaperone-mediated protein folding Source: UniProtKB
  • collagen metabolic process Source: MGI
  • negative regulation of post-translational protein modification Source: Ensembl
  • peptidyl-proline hydroxylation Source: GOC
  • protein stabilization Source: Ensembl
  • regulation of protein secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BRENDAi1.14.11.7. 1306.
ReactomeiR-GGA-1650814. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl 3-hydroxylase 1By similarity (EC:1.14.11.7)
Alternative name(s):
Leucine- and proline-enriched proteoglycan 1 homologBy similarity
Short name:
Leprecan-1 homologBy similarity
Gene namesi
Name:P3H1By similarity
Synonyms:LEPRE1By similarity
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 21

Subcellular locationi

  • Endoplasmic reticulum PROSITE-ProRule annotation

GO - Cellular componenti

  • endoplasmic reticulum Source: MGI
  • extracellular exosome Source: Ensembl
  • macromolecular complex Source: UniProtKB
  • membrane Source: Ensembl
Complete GO annotation...

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

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

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ6JHU8. 1 interaction.

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

GeneTreeiENSGT00550000074573.
HOVERGENiHBG053224.
InParanoidiQ6JHU8.
KOiK08134.
OMAiFNYLQFS.
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_dom.
[Graphical view]
PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
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

        10         20         30         40         50
MALLLPLLPL LVWAAGPPGP LGPPEHSEPP LPAEPPDALF AAGAEAYARG
60 70 80 90 100
DWPAVVLQME RALRARAAIR ARSVRCRLRC ANATAVVPTD GLEPTLHDLL
110 120 130 140 150
FFRGLLRRAA CLRGCGPTQP SRYRLGEELE REFRKRSPYN YLQVAYFKIN
160 170 180 190 200
KVAKAVAAAH TFFVANPEHV EMKQNLEYYQ MMAGVRESDF ADLEARPHMT
210 220 230 240 250
EFRLGVRFYS EEQPAAAVLH LEKALQEYFV ADTECRALCE GPYDYEGYNY
260 270 280 290 300
LEYNADLFQA MTDHYMQVLS CKQGCVTELA SQPGREKPLE DFLPSHFNYL
310 320 330 340 350
QFAYYNNGNY EKAIECAKTY LLFFPNDEVM NQNLAYYTAV LGEDLARPIE
360 370 380 390 400
PRKEIQAYRQ RSLMEKELLF FSYDVFGIPF VDPDTWTPEE VIPKRLREKQ
410 420 430 440 450
KVERETAARI SEEIGNLMKE IETLVEEKAK ESAEMSKFIR EGGPLVYEGA
460 470 480 490 500
SVTMNSKSLN GSQRVVVDGV LSAEECRELQ RLTNAAASAG DGYRGKTSPH
510 520 530 540 550
TPSETFYGVT VLKALKLGQE GKVPLQSAHL YYNVTEKVRH MMESYFRLEV
560 570 580 590 600
PLHFSYSHLV CRTAIDEKQE GRSDNSHEVH VDNCILNAEA LVCVKEPPAY
610 620 630 640 650
TFRDYSAILY LNGDFEGGAF YFTELDAKTQ TAEVQPQCGR AVGFSSGSEN
660 670 680 690 700
PHGVKAVTKG QRCAIALWFT LDPRHSERER VQADDLVKML FRTEEVDLLQ
710 720
ETSAEQEPTA ATSTAGLHAA GKDEL
Length:725
Mass (Da):81,676
Last modified:July 5, 2004 - v1
Checksum:i2D227635DA36B605
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AY463528 mRNA. Translation: AAS45237.1.
RefSeqiNP_001001529.1. NM_001001529.1.
UniGeneiGga.9766.

3D structure databases

ProteinModelPortaliQ6JHU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6JHU8. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi103181352.

Phylogenomic databases

GeneTreeiENSGT00550000074573.
HOVERGENiHBG053224.
InParanoidiQ6JHU8.
KOiK08134.
OMAiFNYLQFS.
PhylomeDBiQ6JHU8.

Enzyme and pathway databases

BRENDAi1.14.11.7. 1306.
ReactomeiR-GGA-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

PROiQ6JHU8.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: June 8, 2016
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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.