[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB). PubMed=7753822 [NCBI, ExPASy, EBI, Israel, Japan] Helaakoski T., Annunen P., Vuori K., Macneil I.A., Pihlajaniemi T., Kivirikko K.I.; "Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit."; Proc. Natl. Acad. Sci. U.S.A. 92:4427-4431(1995).
[2]	NUCLEOTIDE SEQUENCE (ISOFORMS IIA AND IIB). PubMed=11606192 [NCBI, ExPASy, EBI, Israel, Japan] Nokelainen M., Nissi R., Kukkola L., Helaakoski T., Myllyharju J.; "Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues."; Eur. J. Biochem. 268:5300-5309(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA). DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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.
ENZYME REGULATION: In contrast to the subunit alpha-1, alpha-2 is inhibited by poly(L-proline) only at very high concentrations.
SUBUNIT: Heterotetramer of two alpha-2 chains and two beta chains (the beta chain is the multi-functional PDI).
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name IIb

Isoform ID Q60716-1

This is the isoform sequence displayed in this entry.

Name IIa

Isoform ID Q60716-2

Features which should be applied to build the isoform sequence: VSP_004507.
TISSUE SPECIFICITY: Expressed in a variety of tissues.
SIMILARITY: Belongs to the P4HA family.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
SIMILARITY: Contains 1 TPR repeat.

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

U16163; AAC52198.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ314858; CAC85690.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ314858; CAC85691.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018411; AAH18411.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I49135; I49135.

NP_035161.1; -.

3D structure databases

ModBase

Q60716.

Protein-protein interaction databases

IntAct

Q60716; -.

Organism-specific databases

MGI

MGI:894286; P4ha2.

Gene expression databases

ArrayExpress

Q60716; -.

GermOnline

ENSMUSG00000018906; Mus musculus.

Ontologies

GO:0004656;	Molecular function: procollagen-proline 4-dioxygenase activity (inferred from direct assay from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0018401;	Biological process: peptidyl-proline hydroxylation to 4-hydroxy-L-proline (inferred from direct assay from MGI).
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.
IPR013026; TPR_region.
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.
Pfam graphical view of domain structure.

SMART

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

PROSITE

PS50005; TPR; 1.
PS50293; TPR_REGION; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q60716.

Genome annotation databases

Ensembl

ENSMUSG00000018906; Mus musculus. [Contig view]

GeneID

18452; -.

KEGG

mmu:18452; -.

Phylogenomic databases

HOGENOM

Q60716; -.

HOVERGEN

Q60716; -.

Other

P4ha2; Mus musculus.

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

Keywords

Alternative splicing; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Signal; TPR repeat; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 537`	`514`	`Prolyl 4-hydroxylase subunit alpha-2.`	`PRO_0000022727`
`REPEAT`	`209 242`	`34`	`TPR.`
`DOMAIN`	`338 521`	`184`	`PKHD.`
`ACT_SITE`	`513 513`		`Potential.`
`METAL`	`432 432`		`Iron (By similarity).`
`METAL`	`434 434`		`Iron (By similarity).`
`METAL`	`503 503`		`Iron (By similarity).`
`CARBOHYD`	`117 117`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`266 266`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`438 453`		`SDDEDAFKRLGTGNRV -> RPFDSGLKTEGNRL (in isoform IIa).`	`VSP_004507`

Sequence information

Length: 537 AA [This is the length of the unprocessed precursor]

Molecular weight: 61002 Da [This is the MW of the unprocessed precursor]

CRC64: C47D976C75E82518 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLQVLVLVL LMSWFGVLSW VQAEFFTSIG HMTDLIYAEK DLVQSLKEYI LVEEAKLAKI 

        70         80         90        100        110        120 
KSWASKMEAL TSRSAADPEG YLAHPVNAYK LVKRLNTDWP ALGDLVLQDA SAGFVANLSV 

       130        140        150        160        170        180 
QRQFFPTDED ESGAARALMR LQDTYKLDPD TISRGELPGT KYQAMLSVDD CFGLGRSAYN 

       190        200        210        220        230        240 
EGDYYHTVLW MEQVLKQLDA GEEATVTKSL VLDYLSYAVF QLGDLHRAVE LTRRLLSLDP 

       250        260        270        280        290        300 
SHERAGGNLR YFERLLEEER GKSLSNQTDA GLATQENLYE RPTDYLPERD VYESLCRGEG 

       310        320        330        340        350        360 
VKLTPRRQKK LFCRYHHGNR VPQLLIAPFK EEDEWDSPHI VRYYDVMSDE EIERIKEIAK 

       370        380        390        400        410        420 
PKLARATVRD PKTGVLTVAS YRVSKSSWLE EDDDPVVARV NRRMQHITGL TVKTAELLQV 

       430        440        450        460        470        480 
ANYGMGGQYE PHFDFSRSDD EDAFKRLGTG NRVATFLNYM SDVEAGGATV FPDLGAAIWP 

       490        500        510        520        530 
KKGTAVFWYN LLRSGEGDYR TRHAACPVLV GCKWVSNKWF HERGQEFLRP CGTTEVD

Q60716 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