Reviewed, UniProtKB/Swiss-Prot Q6W3E9 (P4HA3_RAT)

Names and origin

Protein names

Recommended name:
    Prolyl 4-hydroxylase subunit alpha-3
    EC=1.14.11.2
Alternative name(s):
    4-PH alpha-3
    Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3

Gene names

Name:

P4ha3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	544 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	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 Fe2+ ion per subunit By similarity. Ascorbate By similarity.
Subunit structure	Heterotetramer of two alpha-3 chains and two beta chains (the beta chain is the multi-functional PDI) By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity.
Post-translational modification	N-glycosylation plays no role in the catalytic activity By similarity.
Sequence similarities	Belongs to the P4HA family. Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. Contains 1 TPR repeat.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	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	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell procollagen-proline 4-dioxygenase complex Ref.1 Traceable author statement. Source: RGD
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 4-dioxygenase activity Ref.1 Inferred from mutant phenotype. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 544	520	Prolyl 4-hydroxylase subunit alpha-3		PRO_0000317768
Regions
	Repeat	227 – 260	34	TPR
	Domain	422 – 529	108	PKHD
Sites
	Metal binding	440	1	Iron By similarity
	Metal binding	442	1	Iron By similarity
	Metal binding	510	1	Iron By similarity
	Binding site	520	1	2-oxoglutarate Potential
Amino acid modifications
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	482	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6W3E9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 9D972AD28EC35C05	FASTA	544	61,165
	10 20 30 40 50 60 MGPGARLAAL LVLLKLGVGD PAAAAGREDT FSALTSVARA LAPERRLLGT LRRYLRGEEA 70 80 90 100 110 120 RLRDLTRFYD KVLSLHEDLK IPVVNPLLVF TLIKRLPSDW RNVVHSLEAT ENIRAPKDGY 130 140 150 160 170 180 EKVEQDLPAF EDLEGAARAL MRLQDAYMLN VKGLAQGVFQ RVTGSSITDL YSPRQLFSLT 190 200 210 220 230 240 ADDCFQVGKV AYDTGDYYHA IPWLEEAVSL FRRSYGEWKT EDEASLEDAL DYLAFACYQV 250 260 270 280 290 300 GNVSCALSLS REFLVYSPDN KRMARNVLKY ERLLAENGHL MAAETAIQRP NVPHLQTRDT 310 320 330 340 350 360 YEGLCQTLGS QPTHYQIPSL YCSYETNSSP YLLLQPARKE VIHLRPLVAL YHDFVSDEEA 370 380 390 400 410 420 QKIRELAEPW LQRSVVASGE KQLQVEYRIS KSAWLKDTVD PVLVTLDRRI AALTGLDIQP 430 440 450 460 470 480 PYAEYLQVVN YGIGGHYEPH FDHATSPSSP LYKMKSGNRA ATLMIYLSSV EAGGATAFIY 490 500 510 520 530 540 GNFSVPVVKN AALFWWNLHR SGEGDDDTLH AGCPVLVGDK WVANKWIHEY GQEFRRPCDT NPED

References

[1]	"Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme." Kukkola L., Hieta R., Kivirikko K.I., Myllyharju J. J. Biol. Chem. 278:47685-47693(2003) [PubMed: 14500733] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY313450 mRNA. Translation: AAQ87605.1.
IPI	IPI00395295.
RefSeq	NP_942070.1.
UniGene	Rn.37765
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6W3E9.
Genome annotation databases
Ensembl	ENSRNOT00000046943; ENSRNOP00000049901; ENSRNOG00000017118; Rattus norvegicus. [Genome view]
GeneID	361612.
KEGG	rno:361612.
Organism-specific databases
CTD	361612.
RGD	735150. P4ha3.
Phylogenomic databases
HOVERGEN	Q6W3E9.
Enzyme and pathway databases
BRENDA	1.14.11.2. 248.
Gene expression databases
Genevestigator	Q6W3E9.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_oxygenase. IPR006620. Pro_4_hyd_alph. IPR013547. Pro_4_hyd_alph_N. IPR011990. TPR-like_helical. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. PF08336. P4Ha_N. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	676914.

Entry information

Entry name

P4HA3_RAT

Accession

Primary (citable) accession number: Q6W3E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 5, 2004
Last modified:	October 13, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)