Reviewed, UniProtKB/Swiss-Prot Q20065 (P4HA2_CAEEL)

Names and origin

Protein names

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

Gene names

Name:	phy-2
ORF Names:	F35G2.4

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	539 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-2(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
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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	Potential
	Chain	17 – 539	523	Prolyl 4-hydroxylase subunit alpha-2		PRO_0000022729
Regions
	Domain	325 – 508	184	PKHD
Sites
	Metal binding	419	1	Iron By similarity
	Metal binding	421	1	Iron By similarity
	Metal binding	490	1	Iron By similarity
	Binding site	500	1	2-oxoglutarate Potential
Amino acid modifications
	Glycosylation	110	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q20065-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 718F76F84193B02B	FASTA	539	61,527
	10 20 30 40 50 60 MRAVLLVCLL AGLAHADLFT AIADLQHMLG AEKDVTTIID QYIEAERARL DDLRRYAHEY 70 80 90 100 110 120 VHRNAHAESV GPEFVTNPIN AYLLIKRLTT EWKKVENIML NNKASTFLKN ITDNRVRSEV 130 140 150 160 170 180 KFPGEEDLSG AATALLRLQD TYSLDTLDLS NGIIGGEKVS NKLSGHDTFE VGRSAYNQKD 190 200 210 220 230 240 YYHCLMWMQV ALVKIENENP PTIEEWEILE YLAYSLYQQG NVRRALSLTK RLAKIAPNHP 250 260 270 280 290 300 RAKGNVKWYE DMLQGKDMVG DLPPIVNKRV EYDGIVERDA YEALCRGEIP PVEPKWKNKL 310 320 330 340 350 360 RCYLKRDKPF LKLAPIKVEI LRFDPLAVLF KNVIHDSEIE VIKELASPKL KRATVQNSKT 370 380 390 400 410 420 GELEHATYRI SKSAWLKGDL DPVIDRVNRR IEDFTNLNQA TSEELQVANY GLGGHYDPHF 430 440 450 460 470 480 DFARKEEKNA FKTLNTGNRI ATVLFYMSQP ERGGATVFNH LGTAVFPSKN DALFWYNLRR 490 500 510 520 530 DGEGDLRTRH AACPVLLGVK WVSNKWIHEK GQEFTRPCGL EEEVQENFIG DLSPYANDP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[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: FUNCTION.
[3]	"Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans." Friedman L., Higgin J.J., Moulder G., Barstead R., Raines R.T., Kimble J. Proc. Natl. Acad. Sci. U.S.A. 97:4736-4741(2000) [PubMed: 10781079] [Abstract] Cited for: FUNCTION.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z69637 Genomic DNA. Translation: CAA93469.1.
PIR	T21816.
RefSeq	NP_502317.1.
UniGene	Cel.12536
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	F35G2.4. Caenorhabditis elegans. [Contig view]
GeneID	178170.
KEGG	cel:F35G2.4.
Organism-specific databases
WormBase	WBGene00004025. phy-2.
WormPep	F35G2.4. CE05811. [WorfDB]
Gene expression databases
ArrayExpress	Q20065.
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	900006.

Entry information

Entry name

P4HA2_CAEEL

Accession

Primary (citable) accession number: Q20065

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project