Reviewed, UniProtKB/Swiss-Prot Q60715 (P4HA1_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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 transcript level.

General annotation (Comments)

Function	Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic activity	Procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2.
Cofactor	Binds 1 Fe2+ ion per subunit. Ascorbate.
Subunit structure	Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI).
Subcellular location	Endoplasmic reticulum lumen.
Sequence similarities	Belongs to the P4HA family. Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. Contains 1 TPR repeat.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Signal TPR repeat
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	collagen fibril organization Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-proline hydroxylation to 4-hydroxy-L-proline Ref.3 Inferred from direct assay. Source: MGI
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 Ref.3 Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q60715-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q60715-2)

The sequence of this isoform differs from the canonical sequence as follows:
     361-380: RRATISNPVTGALETVHYRI → SRATVHDPETGKLTTAQYRV

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_0000022724
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...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	361 – 380	20	RRATI…VHYRI → SRATVHDPETGKLTTAQYRV in isoform 2.		VSP_004505
Experimental info
	Sequence conflict	69	1	T → R in AAC52197. Ref.3
	Sequence conflict	147	1	T → N in AAC52197. Ref.3
	Sequence conflict	354	1	D → Y in AAC52197. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: 81F6C61019E79460	FASTA	534	60,910
	10 20 30 40 50 60 MIWVVLMMAI LLPQSLAHPG FFTSIGQMTD LIHNEKDLVT SLKDYIKAEE DKLEQIKKWA 70 80 90 100 110 120 EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LILKDMSDGF ISNLTIQRQY 130 140 150 160 170 180 FPNDEDQVGA AKALFRLQDT YNLDTNTISK GNLPGVQHKS FLTAEDCFEL GKVAYTEADY 190 200 210 220 230 240 YHTELWMEQA LTQLEEGELS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR 250 260 270 280 290 300 ANGNLVYFEY IMSKEKDANK SASGDQSDQK TAPKKKGIAV DYLPERQKYE MLCRGEGIKM 310 320 330 340 350 360 TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL 370 380 390 400 410 420 RRATISNPVT GALETVHYRI SKSAWLSGYE DPVVSRINMR IQDLTGLDVS TAEELQVANY 430 440 450 460 470 480 GVGGQYEPHF DFARKDEPDA FRELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG 490 500 510 520 530 TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE
	Isoform 2. Checksum: CBDE1E9D6D261DD3	FASTA	534	60,886
	10 20 30 40 50 60 MIWVVLMMAI LLPQSLAHPG FFTSIGQMTD LIHNEKDLVT SLKDYIKAEE DKLEQIKKWA 70 80 90 100 110 120 EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LILKDMSDGF ISNLTIQRQY 130 140 150 160 170 180 FPNDEDQVGA AKALFRLQDT YNLDTNTISK GNLPGVQHKS FLTAEDCFEL GKVAYTEADY 190 200 210 220 230 240 YHTELWMEQA LTQLEEGELS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR 250 260 270 280 290 300 ANGNLVYFEY IMSKEKDANK SASGDQSDQK TAPKKKGIAV DYLPERQKYE MLCRGEGIKM 310 320 330 340 350 360 TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL 370 380 390 400 410 420 SRATVHDPET GKLTTAQYRV SKSAWLSGYE DPVVSRINMR IQDLTGLDVS TAEELQVANY 430 440 450 460 470 480 GVGGQYEPHF DFARKDEPDA FRELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG 490 500 510 520 530 TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J and NOD. Tissue: Embryo, Head and Thymus.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary tumor.
[3]	"Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit." Helaakoski T., Annunen P., Vuori K., Macneil I.A., Pihlajaniemi T., Kivirikko K.I. Proc. Natl. Acad. Sci. U.S.A. 92:4427-4431(1995) [PubMed: 7753822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-534 (ISOFORM 2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK045008 mRNA. Translation: BAC32183.1. AK160798 mRNA. Translation: BAE36020.1. AK169726 mRNA. Translation: BAE41331.1. BC009654 mRNA. Translation: AAH09654.1. U16162 mRNA. Translation: AAC52197.1.
IPI	IPI00272381. IPI00399959.
PIR	I49134.
RefSeq	NP_035160.1.
UniGene	Mm.2212
3D structure databases
SMR	Q60715. Positions 161-254.
ModBase	Search...
Protein-protein interaction databases
STRING	Q60715.
Proteomic databases
PRIDE	Q60715.
Genome annotation databases
Ensembl	ENSMUST00000009789; ENSMUSP00000009789; ENSMUSG00000019916; Mus musculus. [Genome view] ENSMUST00000105466; ENSMUSP00000101106; ENSMUSG00000019916; Mus musculus. [Genome view]
GeneID	18451.
KEGG	mmu:18451.
NMPDR	fig|10090.3.peg.13713.
UCSC	uc007fdo.1. mouse. uc007fdp.1. mouse.
Organism-specific databases
CTD	18451.
MGI	MGI:97463. P4ha1.
Phylogenomic databases
HOVERGEN	Q60715.
OMA	RRATVQN.
Enzyme and pathway databases
BRENDA	1.14.11.2. 244.
Gene expression databases
ArrayExpress	Q60715.
Bgee	Q60715.
Genevestigator	Q60715.
GermOnline	ENSMUSG00000019916. Mus musculus.
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...
Other Resources
NextBio	294136.
SOURCE	Search...

Entry information

Entry name

P4HA1_MOUSE

Accession

Primary (citable) accession number: Q60715
Secondary accession number(s): Q3TEB7, Q80T05, Q91VJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 2, 2002
Last modified:	November 3, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)