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Reviewed, UniProtKB/Swiss-Prot Q10576 (P4HA1_CAEEL)

Last modified November 25, 2008. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl 4-hydroxylase subunit alpha-1
    EC=1.14.11.2
Alternative name(s):
    4-PH alpha-1
    Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
    Protein dumpy-18
Gene names
Name: dpy-18
Synonyms: phy-1
ORF Names: Y47D3B.10
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen trans-4-hydroxy-L-proline + succinate + CO(2).

Cofactor

Binds 1 Fe(2+) ion per subunit.

Ascorbate.

Subunit structure

Heterotetramer of two alpha chains and two beta chains. Exist either as a phy-1(2)/pdi-2(2) tetramer or as a phy-1/phy-2/pdi-2(2) tetramer.

Subcellular location

Endoplasmic reticulum lumen.

Sequence similarities

Belongs to the P4HA family.

Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.

Ontologies

Keywords

   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandIron
Metal-binding
Vitamin C
   Molecular functionDioxygenase
Oxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processbody morphogenesis

Inferred from mutant phenotype. Source: WormBase

collagen and cuticulin-based cuticle development Ref.2

Inferred from mutant phenotype. Source: WormBase

embryonic development Ref.2

Inferred from mutant phenotype. Source: WormBase

locomotion

Inferred from mutant phenotype. Source: WormBase

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of multicellular organism growth

Inferred from mutant phenotype. Source: WormBase

protein metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from electronic annotation. Source: UniProtKB-KW

procollagen-proline 4-dioxygenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Chain17 – 559543Prolyl 4-hydroxylase subunit alpha-1
PRO_0000022728

Regions

Domain328 – 511184PKHD

Sites

Metal binding4221Iron By similarity
Metal binding4241Iron By similarity
Metal binding4931Iron By similarity
Binding site50312-oxoglutarate Potential

Amino acid modifications

Glycosylation1581N-linked (GlcNAc...)

Experimental info

Sequence conflict297 – 3015QKDIS → RRHL in AAA62207. Ref.1
Sequence conflict308 – 3125KRDRP → LAGPS in AAA62207. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q10576-1 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: F3681F4560A2B83D

FASTA55963,927
        10         20         30         40         50         60 
MRLALLVLAT IGYAVADLFT SIADMQNLLE TERNIPKILD KYIHDEEERL VQLKKLSEEY 

        70         80         90        100        110        120 
SKKNEISIEN GLKDITNPIN AFLLIKRKIF DWKEIESKMN ANKAGNVVSS ITDDSYGVRY 

       130        140        150        160        170        180 
PTADDLSGAA IGLLRLQDTY RLDTKDLADG KIYADQGNYT FSAKDCFEIA RAAYNEHDFY 

       190        200        210        220        230        240 
HTVMWMEEAQ RRLGDEVEPT VEVEDILEYL AFALYKQNNL KHALKLTEEL YKMNPTHPRA 

       250        260        270        280        290        300 
KGNVKWYEDL LEQEGVRRSD MRKNLPPIQN RRPDSVLGNT ERTMYEALCR NEVPVSQKDI 

       310        320        330        340        350        360 
SRLYCYYKRD RPFLVYAPIK VEIKRFNPLA VLFKDVISDD EVAAIQELAK PKLARATVHD 

       370        380        390        400        410        420 
SVTGKLVTAT YRISKSAWLK EWEGDVVETV NKRIGYMTNL EMETAEELQI ANYGIGGHYD 

       430        440        450        460        470        480 
PHFDHAKKEE SKSFESLGTG NRIATVLFYM SQPSHGGGTV FTEAKSTILP TKNDALFWYN 

       490        500        510        520        530        540 
LYKQGDGNPD TRHAACPVLV GIKWVSNKWI HEKGNEFRRP CGLKSSDYER FVGDLGYGPE 

       550 
PRNAPNVSPN LAKDVWETL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, baculovirus expression, and characterization of the alpha subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This alpha subunit forms an active alpha beta dimer with the human protein disulfide isomerase/beta subunit."
Veijola J., Koivunen P., Annunen P., Pihlajaniemi T., Kivirikko K.I.
J. Biol. Chem. 269:26746-26753(1994) [PubMed: 7929409] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans."
Winter A.D., Page A.P.
Mol. Cell. Biol. 20:4084-4093(2000) [PubMed: 10805750] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: Bristol N2.
[3]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[4]"The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits."
Myllyharju J., Kukkola L., Winter A.D., Page A.P.
J. Biol. Chem. 277:29187-29196(2002) [PubMed: 12036960] [Abstract]
Cited for: SUBUNIT.
[5]"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, MASS SPECTROMETRY.
[6]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U12762 mRNA. Translation: AAA62207.1.
AJ270999 mRNA. Translation: CAB71298.1.
AL031635, Z81134 Genomic DNA. Translation: CAA21045.1.
Z81134, AL031635 Genomic DNA. Translation: CAB03452.1.
PIRA55069.
T25418.
RefSeqNP_499464.1.
UniGeneCel.19527

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblY47D3B.10. Caenorhabditis elegans. [Contig view]
GeneID176569.
KEGGcel:Y47D3B.10.

Organism-specific databases

WormBaseWBGene00001077. dpy-18.
WormPepY47D3B.10. CE20261. [WorfDB]

Gene expression databases

ArrayExpressQ10576.

Family and domain databases

InterProIPR005123. 2OG-FeII_Oase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
PF08336. P4Ha_N. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio893122.

Entry information

Entry nameP4HA1_CAEEL
AccessionPrimary (citable) accession number: Q10576
Secondary accession number(s): O18153
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 2, 2002
Last modified: November 25, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents