[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=7929409 [NCBI, ExPASy, EBI, Israel, Japan] Veijola J., Koivunen P., Annunen P., Pihlajaniemi T., Kivirikko K.I.; "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."; J. Biol. Chem. 269:26746-26753(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. STRAIN=Bristol N2; 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]	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).
[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).
[5]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, AND MASS SPECTROMETRY. DOI=10.1038/nbt829; PubMed=12754521 [NCBI, ExPASy, EBI, Israel, Japan] Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.; "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."; Nat. Biotechnol. 21:667-672(2003).
[6]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M600392-MCP200; PubMed=17761667 [NCBI, ExPASy, EBI, Israel, Japan] Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.; "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."; Mol. Cell. Proteomics 6:2100-2109(2007).

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: Binds 1 Fe(2+) ion per subunit.
COFACTOR: Ascorbate.
SUBUNIT: 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.
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

U12762; AAA62207.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ270999; CAB71298.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031635; CAA21045.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z81134; CAA21045.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z81134; CAB03452.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031635; CAB03452.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55069; A55069.
T25418; T25418.

RefSeq

NP_499464.1; -.

UniGene

Cel.19527

3D structure databases

ModBase

Q10576.

Organism-specific databases

WormBase

WBGene00001077; dpy-18.

WormPep

Y47D3B.10; CE20261. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

Q10576; -.

Ontologies

GO:0010171;	Biological process: body morphogenesis (inferred from mutant phenotype from WormBase).
GO:0040002;	Biological process: collagen and cuticulin-based cuticle development (inferred from mutant phenotype from WormBase).
GO:0009790;	Biological process: embryonic development (inferred from mutant phenotype from WormBase).
GO:0040011;	Biological process: locomotion (inferred from mutant phenotype from WormBase).
GO:0040018;	Biological process: positive regulation of multicellular organism growth (inferred from mutant phenotype from WormBase).
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

Q10576.

Genome annotation databases

Ensembl

Y47D3B.10; Caenorhabditis elegans. [Contig view]

GeneID

176569; -.

KEGG

cel:Y47D3B.10; -.

Other

ProtoNet

Q10576.

UniRef

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

Keywords

Complete proteome; Dioxygenase; Direct protein sequencing; 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`
`CHAIN`	`17 559`	`543`	`Prolyl 4-hydroxylase subunit alpha-1.`	`PRO_0000022728`
`DOMAIN`	`328 511`	`184`	`PKHD.`
`METAL`	`422 422`		`Iron (By similarity).`
`METAL`	`424 424`		`Iron (By similarity).`
`METAL`	`493 493`		`Iron (By similarity).`
`BINDING`	`503 503`		`2-oxoglutarate (Potential).`
`CARBOHYD`	`158 158`		`N-linked (GlcNAc...).`
`CONFLICT`	`297 301`		`QKDIS -> RRHL (in Ref. 1; AAA62207).`
`CONFLICT`	`308 312`		`KRDRP -> LAGPS (in Ref. 1; AAA62207).`

Sequence information

Length: 559 AA [This is the length of the unprocessed precursor]

Molecular weight: 63927 Da [This is the MW of the unprocessed precursor]

CRC64: F3681F4560A2B83D [This is a checksum on the sequence]

        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

Q10576 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