NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, COMPONENT OF A UNFOLDED COLLAGEN-BINDING COMPLEX INCLUDING P3H1; CYPB AND CRTAP, CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Embryonic fibroblast;
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. May be involved in the secretoty pathway of cells. Has growth suppressive activity in fibroblasts (By similarity).
CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O₂ = procollagen trans-3-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Iron (By similarity).
COFACTOR: Ascorbate (By similarity).
SUBUNIT: Binds unfolded collagen in a complex with CYPB and CRTAP.
INTERACTION:
Q90830:CRTAP; NbExp=1; IntAct=EBI-1169258, EBI-1169253;
SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity).
TISSUE SPECIFICITY: Expressed in embryonic dermis, tendon, cartilage, liver and kidney. Expression in the kidney is restricted to the calyx. In the liver, expression is restricted to the interlobular septum.
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

AY463528; AAS45237.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001001529.1; -.

UniGene

Gga.9766

3D structure databases

ModBase

Q6JHU8.

Protein-protein interaction databases

IntAct

Q6JHU8; -.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from electronic annotation from InterPro).
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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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

Q6JHU8.

Genome annotation databases

GeneID

414142; -.

KEGG

gga:414142; -.

Phylogenomic databases

HOVERGEN

Q6JHU8; -.

Other

UniRef

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

Keywords

Coiled coil; Dioxygenase; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Repeat; Signal; TPR repeat; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 14`	`14`	`Potential.`
`CHAIN`	`15 725`	`711`	`Prolyl 3-hydroxylase 1.`	`PRO_0000240355`
`REPEAT`	`36 69`	`34`	`TPR 1.`
`REPEAT`	`136 169`	`34`	`TPR 2.`
`REPEAT`	`198 231`	`34`	`TPR 3.`
`REPEAT`	`294 327`	`34`	`TPR 4.`
`DOMAIN`	`462 670`	`209`	`PKHD.`
`COILED`	`394 441`	`48`	`Potential.`
`MOTIF`	`722 725`	`4`	`Prevents secretion from ER (Potential).`
`ACT_SITE`	`662 662`		`By similarity.`
`METAL`	`580 580`		`Iron.`
`METAL`	`582 582`		`Iron.`
`METAL`	`652 652`		`Iron.`
`CARBOHYD`	`82 82`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`460 460`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`533 533`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 725 AA [This is the length of the unprocessed precursor]

Molecular weight: 81676 Da [This is the MW of the unprocessed precursor]

CRC64: 2D227635DA36B605 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALLLPLLPL LVWAAGPPGP LGPPEHSEPP LPAEPPDALF AAGAEAYARG DWPAVVLQME 

        70         80         90        100        110        120 
RALRARAAIR ARSVRCRLRC ANATAVVPTD GLEPTLHDLL FFRGLLRRAA CLRGCGPTQP 

       130        140        150        160        170        180 
SRYRLGEELE REFRKRSPYN YLQVAYFKIN KVAKAVAAAH TFFVANPEHV EMKQNLEYYQ 

       190        200        210        220        230        240 
MMAGVRESDF ADLEARPHMT EFRLGVRFYS EEQPAAAVLH LEKALQEYFV ADTECRALCE 

       250        260        270        280        290        300 
GPYDYEGYNY LEYNADLFQA MTDHYMQVLS CKQGCVTELA SQPGREKPLE DFLPSHFNYL 

       310        320        330        340        350        360 
QFAYYNNGNY EKAIECAKTY LLFFPNDEVM NQNLAYYTAV LGEDLARPIE PRKEIQAYRQ 

       370        380        390        400        410        420 
RSLMEKELLF FSYDVFGIPF VDPDTWTPEE VIPKRLREKQ KVERETAARI SEEIGNLMKE 

       430        440        450        460        470        480 
IETLVEEKAK ESAEMSKFIR EGGPLVYEGA SVTMNSKSLN GSQRVVVDGV LSAEECRELQ 

       490        500        510        520        530        540 
RLTNAAASAG DGYRGKTSPH TPSETFYGVT VLKALKLGQE GKVPLQSAHL YYNVTEKVRH 

       550        560        570        580        590        600 
MMESYFRLEV PLHFSYSHLV CRTAIDEKQE GRSDNSHEVH VDNCILNAEA LVCVKEPPAY 

       610        620        630        640        650        660 
TFRDYSAILY LNGDFEGGAF YFTELDAKTQ TAEVQPQCGR AVGFSSGSEN PHGVKAVTKG 

       670        680        690        700        710        720 
QRCAIALWFT LDPRHSERER VQADDLVKML FRTEEVDLLQ ETSAEQEPTA ATSTAGLHAA 


GKDEL

Q6JHU8 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