Reviewed, UniProtKB/Swiss-Prot Q6JHU7 (P3H2_CHICK)

Names and origin

Protein names

Recommended name:
    Prolyl 3-hydroxylase 2
    EC=1.14.11.7
Alternative name(s):
    Leprecan-like protein 1

Gene names

Name:	LEPREL1
Synonyms:	P3H2

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	694 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Catalytic activity	Procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Cofactor	Iron By similarity. Ascorbate By similarity.
Subcellular location	Endoplasmic reticulum. Golgi apparatus By similarity.
Sequence similarities	Belongs to the leprecan family. Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. Contains 4 TPR repeats.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus
Domain	Coiled coil Repeat Signal TPR repeat
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 694	671	Prolyl 3-hydroxylase 2		PRO_0000240359
Regions
	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 coil	386 – 418	33	Potential
	Motif	691 – 694	4	Prevents secretion from ER Potential
Sites
	Active site	648	1	By similarity
	Metal binding	566	1	Iron
	Metal binding	568	1	Iron
	Metal binding	638	1	Iron
Amino acid modifications
	Glycosylation	446	1	N-linked (GlcNAc...) Potential
	Glycosylation	535	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6JHU7-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6263153C4577AFBD	FASTA	694	78,430
	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

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY463529 mRNA. Translation: AAS45238.1.
IPI	IPI00602752.
RefSeq	NP_001001530.1.
UniGene	Gga.20087
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSGALG00000007303. Gallus gallus. [Contig view]
GeneID	414143.
KEGG	gga:414143.
Phylogenomic databases
HOVERGEN	Q6JHU7.
Enzyme and pathway databases
BRENDA	1.14.11.7. 4.
Family and domain databases
InterPro	IPR000886. ER_targeting_sequence. IPR005123. Oxoglutarate/Fe-dep_Oase. IPR006620. Pro_4_hyd_alph. [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

P3H2_CHICK

Accession

Primary (citable) accession number: Q6JHU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)