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Protein

Prolyl 4-hydroxylase subunit alpha-3

Gene

P4HA3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.By similarity

Catalytic activityi

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • Fe2+PROSITE-ProRule annotationNote: Binds 1 Fe2+ ion per subunit.PROSITE-ProRule annotation
  • L-ascorbateBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi440 – 4401IronPROSITE-ProRule annotation
Metal bindingi442 – 4421IronPROSITE-ProRule annotation
Metal bindingi510 – 5101IronPROSITE-ProRule annotation
Binding sitei520 – 52012-oxoglutaratePROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl 4-hydroxylase subunit alpha-3 (EC:1.14.11.2)
Short name:
4-PH alpha-3
Alternative name(s):
Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3
Gene namesi
Name:P4HA3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 544525Prolyl 4-hydroxylase subunit alpha-3PRO_0000317765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylation plays no role in the catalytic activity.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ75UG4.

Interactioni

Subunit structurei

Heterotetramer of two alpha-3 chains and two beta chains (the beta chain is the multi-functional PDI).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008644.

Structurei

3D structure databases

ProteinModelPortaliQ75UG4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati227 – 26034TPRAdd
BLAST
Domaini422 – 529108Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili107 – 13125Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the P4HA family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
Contains 1 TPR repeat.Curated

Keywords - Domaini

Coiled coil, Signal, TPR repeat

Phylogenomic databases

eggNOGiKOG1591. Eukaryota.
ENOG410XS5J. LUCA.
GeneTreeiENSGT00390000018885.
HOGENOMiHOG000230465.
HOVERGENiHBG006834.
InParanoidiQ75UG4.
KOiK00472.
OMAiHLEPYIA.
OrthoDBiEOG7W6WKC.
TreeFamiTF313393.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q75UG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPAARLAAL LAVLAFRAGD PAEVAARGDT FSALTSVARA LAPERRLLGL
60 70 80 90 100
LRRYLRGEEA RLRDLTRFYH KVLSLHEDSA TPVSNPLLAF TLIKRLQSDW
110 120 130 140 150
KNVVHSLEAS ENIRALKDGY ERVEQDLPAF EDLEGAARAL MRLQDVYMLN
160 170 180 190 200
VKGLARGVFQ RVTGSAVTDL YSPRRLFSLT GDDCFQVGKV AYDMGDYYHA
210 220 230 240 250
IPWLEEAVSL FRGSYGEWKT EDEASLEDAL DHLAFAYFQA GNVLCALNLS
260 270 280 290 300
REFLLYSPDN KRVARNVLKY EKLLAESPNQ AVAETVMQRP NVPHLQTRDT
310 320 330 340 350
YEGLCQTLGS QPTHYRIPSL YCSYETSSSP YLLLQPVRKE VIHLEPYVVL
360 370 380 390 400
YHDFVSDAEA QTIRGLAEPW LQRSVVASGE KQLPVEYRIS KSAWLKDTVD
410 420 430 440 450
PVLVTLDHRI AALTGLDVQP PYAEYLQVVN YGIGGHYEPH FDHATSPSSP
460 470 480 490 500
LYRMNSGNRV ATFMIYLSSV EAGGATAFIY GNFSVPVVKN AALFWWNLHR
510 520 530 540
SGEGDGDTLH AACPVLVGDK WVANKWIHEY GQEFRRPCSS RPED
Length:544
Mass (Da):61,023
Last modified:July 5, 2004 - v1
Checksum:iD996D34D44A6F230
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126035 mRNA. Translation: BAD18888.1.
RefSeqiNP_001001598.1. NM_001001598.2.
UniGeneiBt.88095.

Genome annotation databases

EnsembliENSBTAT00000008644; ENSBTAP00000008644; ENSBTAG00000006579.
GeneIDi414348.
KEGGibta:414348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126035 mRNA. Translation: BAD18888.1.
RefSeqiNP_001001598.1. NM_001001598.2.
UniGeneiBt.88095.

3D structure databases

ProteinModelPortaliQ75UG4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008644.

Proteomic databases

PaxDbiQ75UG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008644; ENSBTAP00000008644; ENSBTAG00000006579.
GeneIDi414348.
KEGGibta:414348.

Organism-specific databases

CTDi283208.

Phylogenomic databases

eggNOGiKOG1591. Eukaryota.
ENOG410XS5J. LUCA.
GeneTreeiENSGT00390000018885.
HOGENOMiHOG000230465.
HOVERGENiHBG006834.
InParanoidiQ75UG4.
KOiK00472.
OMAiHLEPYIA.
OrthoDBiEOG7W6WKC.
TreeFamiTF313393.

Miscellaneous databases

NextBioi20818703.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of collagen prolyl 4-hydroxylase during bovine adipogenesis."
    Tahara K., Aso H., Yamasaki T., Takano S.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adipose tissue.

Entry informationi

Entry nameiP4HA3_BOVIN
AccessioniPrimary (citable) accession number: Q75UG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 2004
Last modified: December 9, 2015
This is version 87 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

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.