Prolyl 4-hydroxylase subunit alpha-1 precursor

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Reviewed, UniProtKB/Swiss-Prot Q10576 (P4HA1_CAEEL)

Last modified February 9, 2010. Version 84. History...

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

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Names and origin

Protein names

Recommended name:
    Prolyl 4-hydroxylase subunit alpha-1
      Short name=4-PH alpha-1
    EC=1.14.11.2
Alternative name(s):
    Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
    Protein dumpy-18

Gene names

Name:	dpy-18
Synonyms:	phy-1
ORF Names:	Y47D3B.10

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. Ref.2
Catalytic activity	L-proline-[procollagen] + 2-oxoglutarate + O₂ = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO₂.
Cofactor	Binds 1 Fe²⁺ ion per subunit. Ascorbate.
Subunit structure	Heterotetramer of two alpha chains and two beta chains. Exist either as a phy-1₂/pdi-2₂ tetramer or as a phy-1/phy-2/pdi-2₂ tetramer. Ref.4
Subcellular location	Endoplasmic reticulum lumen.
Sequence similarities	Belongs to the P4HA family. Contains 1 Fe2OG dioxygenase domain.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	body morphogenesis 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
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Chain

17 – 559

543

Prolyl 4-hydroxylase subunit alpha-1

PRO_0000022728

Regions

Domain

404 – 512

109

Fe2OG dioxygenase

Sites

Metal binding

422

Iron By similarity

Metal binding

424

Iron By similarity

Metal binding

493

Iron By similarity

Binding site

503

2-oxoglutarate Potential

Amino acid modifications

Glycosylation

158

N-linked (GlcNAc...) Ref.5 Ref.6

Experimental info

Sequence conflict

297 – 301

QKDIS → RRHL in AAA62207. Ref.1

Sequence conflict

308 – 312

KRDRP → LAGPS in AAA62207. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q10576-1 [UniParc].

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

559

63,927

        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

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References

	« Hide 'large scale' referencesShow '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.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U12762 mRNA. Translation: AAA62207.1. AJ270999 mRNA. Translation: CAB71298.1. AL031635, Z81134 Genomic DNA. Translation: CAA21045.1. Z81134, AL031635 Genomic DNA. Translation: CAB03452.1.
PIR	A55069. T25418.
RefSeq	NP_499464.1.
UniGene	Cel.19527
3D structure databases
SMR	Q10576. Positions 161-252.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10576.
Genome annotation databases
Ensembl	Y47D3B.10.1; Y47D3B.10.1; Y47D3B.10; Caenorhabditis elegans. [Genome view] Y47D3B.10.2; Y47D3B.10.2; Y47D3B.10; Caenorhabditis elegans. [Genome view]
GeneID	176569.
KEGG	cel:Y47D3B.10.
UCSC	Y47D3B.10.2. c. elegans.
Organism-specific databases
CTD	176569.
WormBase	WBGene00001077. dpy-18.
WormPep	Y47D3B.10. CE20261. [WorfDB]
Phylogenomic databases
eggNOG	meNOG06393.
HOGENOM	HBG714077.
InParanoid	Q10576.
OMA	ERTMYEA.
PhylomeDB	Q10576.
Enzyme and pathway databases
BRENDA	1.14.11.2. 672.
Gene expression databases
ArrayExpress	Q10576.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_oxygenase. IPR006620. Pro_4_hyd_alph. IPR013547. Pro_4_hyd_alph_N. IPR011990. TPR-like_helical. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. PF08336. P4Ha_N. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	893122.

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Entry information

Entry name

P4HA1_CAEEL

Accession

Primary (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:	February 9, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project

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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)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents