[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1074/jbc.M312807200; PubMed=15044469 [NCBI, ExPASy, EBI, Israel, Japan] Vranka J.A., Sakai L.Y., Bachinger H.P.; "Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes."; J. Biol. Chem. 279:23615-23621(2004).

Comments

FUNCTION: Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V.
CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O₂ = procollagen trans-3-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Iron (By similarity).
COFACTOR: Ascorbate (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus (By similarity).
SIMILARITY: Belongs to the leprecan family.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
SIMILARITY: Contains 4 TPR repeats.

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

AY463529; AAS45238.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001001530.1; -.

UniGene

Gga.20087

3D structure databases

ModBase

Q6JHU7.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from electronic annotation from InterPro).
GO:0005794;	Cellular component: Golgi apparatus (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0019797;	Molecular function: procollagen-proline 3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019538;	Biological process: protein metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR000886; ER_targeting_sequence.
IPR006620; Pro_4_hyd_alph.
IPR013026; TPR_region.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

SMART

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

PROSITE

PS00014; ER_TARGET; 1.
PS50005; TPR; FALSE_NEG.
PS50293; TPR_REGION; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q6JHU7.

Genome annotation databases

Ensembl

ENSGALG00000007303; Gallus gallus. [Contig view]

GeneID

414143; -.

KEGG

gga:414143; -.

Phylogenomic databases

HOVERGEN

Q6JHU7; -.

Other

UniRef

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

Keywords

Coiled coil; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Iron; Metal-binding; Oxidoreductase; Repeat; Signal; TPR repeat; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 694`	`671`	`Prolyl 3-hydroxylase 2.`	`PRO_0000240359`
`REPEAT`	`35 68`	`34`	`TPR 1.`
`REPEAT`	`136 169`	`34`	`TPR 2.`
`REPEAT`	`196 229`	`34`	`TPR 3.`
`REPEAT`	`292 325`	`34`	`TPR 4.`
`DOMAIN`	`448 656`	`209`	`PKHD.`
`COILED`	`386 418`	`33`	`Potential.`
`MOTIF`	`691 694`	`4`	`Prevents secretion from ER (Potential).`
`ACT_SITE`	`648 648`		`By similarity.`
`METAL`	`566 566`		`Iron.`
`METAL`	`568 568`		`Iron.`
`METAL`	`638 638`		`Iron.`
`CARBOHYD`	`446 446`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`535 535`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 694 AA [This is the length of the unprocessed precursor]

Molecular weight: 78430 Da [This is the MW of the unprocessed precursor]

CRC64: 6263153C4577AFBD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPGSRSWGA VLLLAAMLPA ACGSCGADGG PLEPFDALYA SGVEAYYGGD FAGAARCLEQ 

        70         80         90        100        110        120 
ALRSRRELRA ERLRCRRRCR GQVRLAALGA GPAGELPFFG ALLRRAGCLR SCEEPRLGAA 

       130        140        150        160        170        180 
SRHRAAEEVR SDFQRRVPYS YLQRAYIQLN KLEEAANAAH TFFMANPEHM EIQQDIENYK 

       190        200        210        220        230        240 
TTAGKVSLID LEAKPHMEDY SAGVRHYDKE EYGLAITFLE RALEGYYAED EDCQIMCEGP 

       250        260        270        280        290        300 
QRFEEHEYLE YKAGLYEAIA DHYMQVLACK HDCIRELATR SGRISPIENF LPLHYDYLQF 

       310        320        330        340        350        360 
AYYRVGDYVK ALECARSYLL FHPDDEDVLE NAAYYEGLLE GTVDPATIKP RKEAKALLRR 

       370        380        390        400        410        420 
HKLESHLLRV AAVGLGFTYT EPNYWKRYGA RQDEHSVPSS ISSEPEDGPR LSLTKKPTPK 

       430        440        450        460        470        480 
PDRELKEGGP LLYSDVKFVY NSQQLNGTQR VLLDNVISEE QCRELHRVAS GIMLAGDGYR 

       490        500        510        520        530        540 
GKTSPHTPNE RFEGATVLKA LKYGYEGRVP LKSARLFYDI SEKARRIVES YFMLNSTLYF 

       550        560        570        580        590        600 
SYTHLVCRTA LSGQQERRND LSHPIHADNC LLDPEANECW KEPPAYTFRD YSALLYMNAD 

       610        620        630        640        650        660 
FEGGEFIFTE MDAKTVTASI KPKCGRMVSF SSGGENPHGV KAVTKGQRCA VALWFTLDPL 

       670        680        690 
YRELERIQAD EVIAMLDQEH VGRSEMNINP KDEL

Q6JHU7 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