Reviewed, UniProtKB/Swiss-Prot Q1RMU3 (P4HA1_BOVIN)

Names and origin

Protein names

Recommended name:
    Prolyl 4-hydroxylase subunit alpha-1
    EC=1.14.11.2
Alternative name(s):
    4-PH alpha-1
    Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1

Gene names

Name:

P4HA1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	534 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	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 + O(2) = procollagen trans-4-hydroxy-L-proline + succinate + CO(2).
Cofactor	Binds 1 Fe(2+) ion per subunit By similarity. Ascorbate By similarity.
Subunit structure	Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI) By similarity.
Subcellular location	Endoplasmic reticulum lumenBy 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 protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumen 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: 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 4-dioxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	By similarity
	Chain	18 – 534	517	Prolyl 4-hydroxylase subunit alpha-1		PRO_0000288111
Regions
	Repeat	205 – 238	34	TPR
	Domain	335 – 518	184	PKHD
Sites
	Metal binding	429	1	Iron By similarity
	Metal binding	431	1	Iron By similarity
	Metal binding	500	1	Iron By similarity
	Binding site	510	1	2-oxoglutarate Potential
Amino acid modifications
	Glycosylation	113	1	N-linked (GlcNAc...)
	Glycosylation	259	1	N-linked (GlcNAc...)

Sequences

	Sequence		Length	Mass (Da)
	Q1RMU3-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: D6AF8ECEA1447C62	FASTA	534	61,010
	10 20 30 40 50 60 MIWYILVVGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA 70 80 90 100 110 120 EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY 130 140 150 160 170 180 FPNDEDQVGA AKALLRLQDT YNLDTDTISK GDLPGVKHKS FLTVEDCFEL GKVAYTEADY 190 200 210 220 230 240 YHTELWMEQA LRQLDEGEVS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR 250 260 270 280 290 300 ANGNLKYFEY IMAKEKDANK SSSDDQSDQK TTLKKKGAAV DYLPERQKYE MLCRGEGIKM 310 320 330 340 350 360 TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE VVKDLAKPRL 370 380 390 400 410 420 RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY 430 440 450 460 470 480 GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV LAGGATVFPE VGASVWPKKG 490 500 510 520 530 TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC114708 mRNA. Translation: AAI14709.1.
RefSeq	NP_001069238.1.
UniGene	Bt.41027
3D structure databases
SMR	Q1RMU3. Positions 161-254.
ModBase	Search...
Genome annotation databases
GeneID	518288.
KEGG	bta:518288.
Phylogenomic databases
HOVERGEN	Q1RMU3.
Family and domain databases
InterPro	IPR005123. 2OG-FeII_Oase. IPR006620. Pro_4_hyd_alph. IPR013547. Pro_4_hyd_alph_N. IPR011990. TPR-like_helical. IPR013105. TPR_2. IPR013026. TPR_region. [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. PF07719. TPR_2. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS50005. TPR. 1 hit. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P4HA1_BOVIN

Accession

Primary (citable) accession number: Q1RMU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 16, 2006
Last modified:	November 25, 2008
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)