[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[2]	FUNCTION. DOI=10.1128/MCB.20.11.4084-4093.2000; PubMed=10805750 [NCBI, ExPASy, EBI, Israel, Japan] Winter A.D., Page A.P.; "Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans."; Mol. Cell. Biol. 20:4084-4093(2000).
[3]	FUNCTION. DOI=10.1073/pnas.97.9.4736; PubMed=10781079 [NCBI, ExPASy, EBI, Israel, Japan] Friedman L., Higgin J.J., Moulder G., Barstead R., Raines R.T., Kimble J.; "Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans."; Proc. Natl. Acad. Sci. U.S.A. 97:4736-4741(2000).
[4]	SUBUNIT. DOI=10.1074/jbc.M203824200; PubMed=12036960 [NCBI, ExPASy, EBI, Israel, Japan] Myllyharju J., Kukkola L., Winter A.D., Page A.P.; "The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits."; J. Biol. Chem. 277:29187-29196(2002).

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 + O₂ = procollagen trans-4-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Iron.
COFACTOR: Ascorbate.
SUBUNIT: 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.
SIMILARITY: Belongs to the P4HA family.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z69637; CAA93469.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T21816; T21816.

NP_502317.1; -.

3D structure databases

ModBase

Q20065.

Organism-specific databases

WormBase

WBGene00004025; phy-2.

WormPep

F35G2.4; CE05811. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

Q20065; -.

Ontologies

GO:0005788;	Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004656;	Molecular function: procollagen-proline 4-dioxygenase activity (inferred from electronic annotation from EC).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:1.25.40.10; TPR-like_helical; 1.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
PF08336; P4Ha_N; 1.
PF07719; TPR_2; 1.
Pfam graphical view of domain structure.

SMART

SM00702; P4Hc; 1.
SMART graphical view of domain structure.

BLOCKS

Q20065.

Genome annotation databases

Ensembl

F35G2.4; Caenorhabditis elegans. [Contig view]

GeneID

178170; -.

KEGG

cel:F35G2.4; -.

Other

ProtoNet

Q20065.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Signal; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`CHAIN`	`17 539`	`523`	`Prolyl 4-hydroxylase subunit alpha-2.`	`PRO_0000022729`
`DOMAIN`	`325 508`	`184`	`PKHD.`
`ACT_SITE`	`500 500`		`Potential.`
`METAL`	`419 419`		`Iron (By similarity).`
`METAL`	`421 421`		`Iron (By similarity).`
`METAL`	`490 490`		`Iron (By similarity).`
`CARBOHYD`	`110 110`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 539 AA [This is the length of the unprocessed precursor]

Molecular weight: 61527 Da [This is the MW of the unprocessed precursor]

CRC64: 718F76F84193B02B [This is a checksum on the sequence]

        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

Q20065 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools