Reviewed, UniProtKB/Swiss-Prot Q6JHU8 (P3H1_CHICK)

Names and origin

Protein names

Recommended name:
    Prolyl 3-hydroxylase 1
    EC=1.14.11.7
Alternative name(s):
    Leucine- and proline-enriched proteoglycan 1 homolog
      Short name=Leprecan-1 homolog

Gene names

Name:	LEPRE1
Synonyms:	P3H1

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 + O(2) = procollagen trans-3-hydroxy-L-proline + succinate + CO(2).
Cofactor	Iron By similarity. Ascorbate By similarity.
Subunit structure	Binds unfolded collagen in a complex with CYPB and CRTAP.
Subcellular location	Endoplasmic reticulumBy 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. Ref.1
Sequence similarities	Belongs to the leprecan family. Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. Contains 4 TPR repeats.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Coiled coil Repeat Signal TPR repeat
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: InterPro
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW procollagen-proline 3-dioxygenase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRTAP	Q90830	1	EBI-1169258,EBI-1169253

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 14	14	Potential
	Chain	15 – 725	711	Prolyl 3-hydroxylase 1		PRO_0000240355
Regions
	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 coil	394 – 441	48	Potential
	Motif	722 – 725	4	Prevents secretion from ER Potential
Sites
	Active site	662	1	By similarity
	Metal binding	580	1	Iron
	Metal binding	582	1	Iron
	Metal binding	652	1	Iron
Amino acid modifications
	Glycosylation	82	1	N-linked (GlcNAc...) Potential
	Glycosylation	460	1	N-linked (GlcNAc...) Potential
	Glycosylation	533	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6JHU8-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 2D227635DA36B605	FASTA	725	81,676
	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

References

[1]

"Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes." Vranka J.A., Sakai L.Y., Bachinger H.P. J. Biol. Chem. 279:23615-23621(2004) [PubMed: 15044469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, COMPONENT OF A UNFOLDED COLLAGEN-BINDING COMPLEX INCLUDING P3H1; CYPB AND CRTAP, CHARACTERIZATION, TISSUE SPECIFICITY. Tissue: Embryonic fibroblast.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY463528 mRNA. Translation: AAS45237.1.
RefSeq	NP_001001529.1.
UniGene	Gga.9766
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6JHU8. 1 interaction.
Genome annotation databases
GeneID	414142.
KEGG	gga:414142.
Phylogenomic databases
HOVERGEN	Q6JHU8.
Family and domain databases
InterPro	IPR005123. 2OG-FeII_Oase. IPR000886. ER_targeting_sequence. IPR006620. Pro_4_hyd_alph. IPR013026. TPR_region. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P3H1_CHICK

Accession

Primary (citable) accession number: Q6JHU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	July 5, 2004
Last modified:	December 16, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)