Reviewed, UniProtKB/Swiss-Prot Q10576 (P4HA1_CAEEL)

Names and origin

Protein names

Recommended 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

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

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.

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 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 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 component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW 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: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16
	Chain	17 – 559	543	Prolyl 4-hydroxylase subunit alpha-1		PRO_0000022728
Regions
	Domain	328 – 511	184	PKHD
Sites
	Metal binding	422	1	Iron By similarity
	Metal binding	424	1	Iron By similarity
	Metal binding	493	1	Iron By similarity
	Binding site	503	1	2-oxoglutarate Potential
Amino acid modifications
	Glycosylation	158	1	N-linked (GlcNAc...)
Experimental info
	Sequence conflict	297 – 301	5	QKDIS → RRHL in AAA62207. Ref.1
	Sequence conflict	308 – 312	5	KRDRP → LAGPS in AAA62207. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10576-1 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: F3681F4560A2B83D	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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
ModBase	Search...
Genome annotation databases
Ensembl	Y47D3B.10. Caenorhabditis elegans. [Contig view]
GeneID	176569.
KEGG	cel:Y47D3B.10.
Organism-specific databases
WormBase	WBGene00001077. dpy-18.
WormPep	Y47D3B.10. CE20261. [WorfDB]
Gene expression databases
ArrayExpress	Q10576.
Family and domain databases
InterPro	IPR005123. 2OG-FeII_Oase. IPR006620. Pro_4_hyd_alph. IPR013547. Pro_4_hyd_alph_N. IPR011990. TPR-like_helical. IPR013105. TPR_2. [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. PF07719. TPR_2. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	893122.

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:	November 25, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project