Reviewed, UniProtKB/Swiss-Prot P16924 (P4HA1_CHICK)

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
Synonyms:	P4HA

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	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 + 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 chains and two beta chains (the beta chain is the multi-functional PDI) By similarity.
Subcellular location	Endoplasmic reticulum lumen 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	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
Cellular component	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: 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 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 516	516	Prolyl 4-hydroxylase subunit alpha-1		PRO_0000206659
Regions
	Repeat	189 – 222	34	TPR
	Domain	317 – 500	184	PKHD
Sites
	Metal binding	411	1	Iron By similarity
	Metal binding	413	1	Iron By similarity
	Metal binding	482	1	Iron By similarity
	Binding site	492	1	2-oxoglutarate Potential
Amino acid modifications
	Glycosylation	97	1	N-linked (GlcNAc...) Probable
	Glycosylation	243	1	N-linked (GlcNAc...) Probable

Sequences

	Sequence		Length	Mass (Da)
	P16924-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 49EB14163CDE347B	FASTA	516	59,440
	10 20 30 40 50 60 HTDFFTSIGH MTDLINTEKD LVISKLKDYI KAEESKLEQI KKWAEKLDKL TDTATKDPEG 70 80 90 100 110 120 FLGHPANAFK LMKRLNTEWG ELESLVLKDM SDGFISNMTI QRQFFPNDED QTGARKALLR 130 140 150 160 170 180 LQDTYNLDTD TLSRGNLPGV KHKSFLTAED CFELGKIRYT EADYYHTELW MEQALKQLDE 190 200 210 220 230 240 GEVSSADKVY ILDYLSYAVY QQGDLSKAMM LTKRLLELDP EHQRANGNMK YFEYIMAKEK 250 260 270 280 290 300 EANKSSTDAE DQTDKETEVK KKDYLPERRK YEMLCRGEGL KMTPRRQKRL FCRYYDGNRN 310 320 330 340 350 360 PRYILGPVKQ EDEWDKPRIV RFLDIISDEE IETVKELAKP RLSRATVHDP ETGKLTTAHY 370 380 390 400 410 420 RVSKSAWLSG YESPVVSRIN TRIQDLTGLD VSTAEELQVA NYGVGGQYEP HFDFGRKDEP 430 440 450 460 470 480 DAFKELGTGN RIATWLFYMS DVSAGGATVF PEVGASVWPK KGTAVFWYNL FPSGEGDYST 490 500 510 RHAACPVLVG NKWVSNKWLH ERGQEFRRPC TLSELE

References

[1]

"Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryo." Bassuk J.A., Kao W.W.-Y., Herzer P., Kedersha N., Seyer J., Demartino J.A., Daugherty B.L., Mark G.E. III, Berg R.A. Proc. Natl. Acad. Sci. U.S.A. 86:7382-7386(1989) [PubMed: 2552442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-516, PROTEIN SEQUENCE OF 1-42.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M26217 mRNA. Translation: AAA49002.1.
IPI	IPI00598417.
PIR	DACHA. A33832.
UniGene	Gga.17975
3D structure databases
SMR	P16924. Positions 145-238.
ModBase	Search...
Protein-protein interaction databases
STRING	P16924.
Genome annotation databases
Ensembl	ENSGALT00000006896; ENSGALP00000006885; ENSGALG00000004325; Gallus gallus. [Genome view] ENSGALT00000040712; ENSGALP00000039915; ENSGALG00000004325; Gallus gallus. [Genome view]
Phylogenomic databases
HOGENOM	P16924.
HOVERGEN	P16924.
Enzyme and pathway databases
BRENDA	1.14.11.2. 4.
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. IPR013026. TPR_region. IPR019734. TPR_repeat. [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. 1 hit. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P4HA1_CHICK

Accession

Primary (citable) accession number: P16924

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	September 22, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)