[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(94)90188-0; PubMed=7959029 [NCBI, ExPASy, EBI, Israel, Japan] Hopkinson I., Smith S.A., Donne A., Gregory H., Franklin T.J., Grant M.E., Rosamond J.; "The complete cDNA derived sequence of the rat prolyl 4-hydroxylase alpha subunit."; Gene 149:391-392(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; 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 (By similarity).
CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O₂ = procollagen trans-4-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
COFACTOR: Ascorbate (By similarity).
SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI) (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
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

X78949; CAA55546.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078703; AAH78703.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S44204; S44204.

NP_742059.2; -.

3D structure databases

SMR

P54001; 161-254.

ModBase

P54001.

Protein-protein interaction databases

IntAct

P54001; -.

Organism-specific databases

RGD

621000; P4ha1.

Ontologies

GO:0005788;	Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
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.
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.
PF07719; TPR_2; 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

P54001.

Genome annotation databases

GeneID

64475; -.

KEGG

rno:64475; -.

Phylogenomic databases

HOVERGEN

P54001; -.

Other

ProtoNet

P54001.

UniRef

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

Keywords

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 17`	`17`	`By similarity.`
`CHAIN`	`18 534`	`517`	`Prolyl 4-hydroxylase subunit alpha-1.`	`PRO_0000022725`
`REPEAT`	`205 238`	`34`	`TPR.`
`DOMAIN`	`335 518`	`184`	`PKHD.`
`METAL`	`429 429`		`Iron (By similarity).`
`METAL`	`431 431`		`Iron (By similarity).`
`METAL`	`500 500`		`Iron (By similarity).`
`BINDING`	`510 510`		`2-oxoglutarate (Potential).`
`CARBOHYD`	`113 113`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`259 259`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`265 267`		`DQS -> ERA (in Ref. 1; CAA55546).`

Sequence information

Length: 534 AA [This is the length of the unprocessed precursor]

Molecular weight: 60898 Da [This is the MW of the unprocessed precursor]

CRC64: C44659978281FF30 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIWGVLMMGI LLPQCSAHPG FFTSIGQMTD LIHNEKDLVT SLKDYIKAEE DKLEQIKKWA 

        70         80         90        100        110        120 
EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LILKDMSDGF ISNLTIQRQY 

       130        140        150        160        170        180 
FPNDEDQVGA AKALFRLQDT YNLDTNTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY 

       190        200        210        220        230        240 
YHTELWMEQA LMQLEEGEMS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR 

       250        260        270        280        290        300 
ANGNLVYFEY IMSKEKDANK SASGDQSDQK TTPKKKGIAV DYLPERQKYE MLCRGEGIKM 

       310        320        330        340        350        360 
TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL 

       370        380        390        400        410        420 
SRATVHDPET GKLTTAQYRV SKSAWLSGYE DPVVSRINMR IQDLTGLDVS TAEELQVANY 

       430        440        450        460        470        480 
GVGGQYEPHF DFARKDEPDA FRELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG 

       490        500        510        520        530 
TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE

P54001 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