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Q60715

- P4HA1_MOUSE

UniProt

Q60715 - P4HA1_MOUSE

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Protein

Prolyl 4-hydroxylase subunit alpha-1

Gene

P4ha1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.

Catalytic activityi

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactori

Binds 1 Fe2+ ion per subunit.
Ascorbate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi429 – 4291IronPROSITE-ProRule annotation
Metal bindingi431 – 4311IronPROSITE-ProRule annotation
Metal bindingi500 – 5001IronPROSITE-ProRule annotation
Binding sitei510 – 51012-oxoglutaratePROSITE-ProRule annotation

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. L-ascorbic acid binding Source: UniProtKB-KW
  3. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: InterPro
  4. procollagen-proline 4-dioxygenase activity Source: MGI

GO - Biological processi

  1. collagen fibril organization Source: MGI
  2. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl 4-hydroxylase subunit alpha-1 (EC:1.14.11.2)
Short name:
4-PH alpha-1
Alternative name(s):
Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Gene namesi
Name:P4ha1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:97463. P4ha1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
  2. procollagen-proline 4-dioxygenase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Chaini18 – 534517Prolyl 4-hydroxylase subunit alpha-1PRO_0000022724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ60715.
PaxDbiQ60715.
PRIDEiQ60715.

PTM databases

PhosphoSiteiQ60715.

Expressioni

Gene expression databases

BgeeiQ60715.
ExpressionAtlasiQ60715. baseline and differential.
GenevestigatoriQ60715.

Interactioni

Subunit structurei

Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI).

Protein-protein interaction databases

BioGridi202006. 2 interactions.
IntActiQ60715. 4 interactions.
MINTiMINT-4106073.

Structurei

3D structure databases

ProteinModelPortaliQ60715.
SMRiQ60715. Positions 18-254, 335-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati205 – 23834TPRAdd
BLAST
Domaini411 – 519109Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the P4HA family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
Contains 1 TPR repeat.PROSITE-ProRule annotation

Keywords - Domaini

Signal, TPR repeat

Phylogenomic databases

eggNOGiNOG78926.
GeneTreeiENSGT00390000018885.
HOGENOMiHOG000230465.
HOVERGENiHBG006834.
InParanoidiQ60715.
KOiK00472.
OMAiNDEDQIG.
OrthoDBiEOG7W6WKC.
PhylomeDBiQ60715.
TreeFamiTF313393.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q60715-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MIWVVLMMAI LLPQSLAHPG FFTSIGQMTD LIHNEKDLVT SLKDYIKAEE
60 70 80 90 100
DKLEQIKKWA EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN
110 120 130 140 150
LILKDMSDGF ISNLTIQRQY FPNDEDQVGA AKALFRLQDT YNLDTNTISK
160 170 180 190 200
GNLPGVQHKS FLTAEDCFEL GKVAYTEADY YHTELWMEQA LTQLEEGELS
210 220 230 240 250
TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR ANGNLVYFEY
260 270 280 290 300
IMSKEKDANK SASGDQSDQK TAPKKKGIAV DYLPERQKYE MLCRGEGIKM
310 320 330 340 350
TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE
360 370 380 390 400
IVKDLAKPRL RRATISNPVT GALETVHYRI SKSAWLSGYE DPVVSRINMR
410 420 430 440 450
IQDLTGLDVS TAEELQVANY GVGGQYEPHF DFARKDEPDA FRELGTGNRI
460 470 480 490 500
ATWLFYMSDV SAGGATVFPE VGASVWPKKG TAVFWYNLFA SGEGDYSTRH
510 520 530
AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE
Length:534
Mass (Da):60,910
Last modified:May 2, 2002 - v2
Checksum:i81F6C61019E79460
GO
Isoform 2 (identifier: Q60715-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:534
Mass (Da):60,886
Checksum:iCBDE1E9D6D261DD3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691T → R in AAC52197. (PubMed:7753822)Curated
Sequence conflicti147 – 1471T → N in AAC52197. (PubMed:7753822)Curated
Sequence conflicti354 – 3541D → Y in AAC52197. (PubMed:7753822)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei361 – 38020RRATI…VHYRI → SRATVHDPETGKLTTAQYRV in isoform 2. 2 PublicationsVSP_004505Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23863.1. [Q60715-1]
PIRiI49134.
RefSeqiNP_035160.1. NM_011030.2. [Q60715-1]
XP_006513403.1. XM_006513340.1. [Q60715-2]
UniGeneiMm.2212.

Genome annotation databases

EnsembliENSMUST00000009789; ENSMUSP00000009789; ENSMUSG00000019916. [Q60715-1]
ENSMUST00000105466; ENSMUSP00000101106; ENSMUSG00000019916. [Q60715-2]
GeneIDi18451.
KEGGimmu:18451.
UCSCiuc007fdo.2. mouse. [Q60715-1]
uc007fdp.2. mouse. [Q60715-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23863.1. [Q60715-1 ]
PIRi I49134.
RefSeqi NP_035160.1. NM_011030.2. [Q60715-1 ]
XP_006513403.1. XM_006513340.1. [Q60715-2 ]
UniGenei Mm.2212.

3D structure databases

ProteinModelPortali Q60715.
SMRi Q60715. Positions 18-254, 335-518.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202006. 2 interactions.
IntActi Q60715. 4 interactions.
MINTi MINT-4106073.

PTM databases

PhosphoSitei Q60715.

Proteomic databases

MaxQBi Q60715.
PaxDbi Q60715.
PRIDEi Q60715.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000009789 ; ENSMUSP00000009789 ; ENSMUSG00000019916 . [Q60715-1 ]
ENSMUST00000105466 ; ENSMUSP00000101106 ; ENSMUSG00000019916 . [Q60715-2 ]
GeneIDi 18451.
KEGGi mmu:18451.
UCSCi uc007fdo.2. mouse. [Q60715-1 ]
uc007fdp.2. mouse. [Q60715-2 ]

Organism-specific databases

CTDi 5033.
MGIi MGI:97463. P4ha1.

Phylogenomic databases

eggNOGi NOG78926.
GeneTreei ENSGT00390000018885.
HOGENOMi HOG000230465.
HOVERGENi HBG006834.
InParanoidi Q60715.
KOi K00472.
OMAi NDEDQIG.
OrthoDBi EOG7W6WKC.
PhylomeDBi Q60715.
TreeFami TF313393.

Miscellaneous databases

ChiTaRSi P4HA1. mouse.
NextBioi 294136.
PROi Q60715.
SOURCEi Search...

Gene expression databases

Bgeei Q60715.
ExpressionAtlasi Q60715. baseline and differential.
Genevestigatori Q60715.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR013547. Pro_4_hyd_alph_N.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
PF08336. P4Ha_N. 1 hit.
[Graphical view ]
SMARTi SM00702. P4Hc. 1 hit.
[Graphical view ]
PROSITEi PS51471. FE2OG_OXY. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-534 (ISOFORM 2).

Entry informationi

Entry nameiP4HA1_MOUSE
AccessioniPrimary (citable) accession number: Q60715
Secondary accession number(s): Q3TEB7, Q80T05, Q91VJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 2, 2002
Last modified: October 29, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3