ID P4HA3_MOUSE Reviewed; 542 AA.
AC Q6W3F0; Q640R2; Q8C3A6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 08-NOV-2023, entry version 115.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-3;
DE Short=4-PH alpha-3;
DE EC=1.14.11.2 {ECO:0000250|UniProtKB:Q7Z4N8};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3;
DE Flags: Precursor;
GN Name=P4ha3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Webster;
RX PubMed=14500733; DOI=10.1074/jbc.m306806200;
RA Kukkola L., Hieta R., Kivirikko K.I., Myllyharju J.;
RT "Identification and characterization of a third human, rat, and mouse
RT collagen prolyl 4-hydroxylase isoenzyme.";
RL J. Biol. Chem. 278:47685-47693(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC proteins. {ECO:0000250|UniProtKB:Q7Z4N8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18946;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q7Z4N8};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC -!- SUBUNIT: Heterotetramer of two alpha-3 chains and two beta chains (the
CC beta chain is the multi-functional PDI).
CC {ECO:0000250|UniProtKB:Q7Z4N8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6W3F0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6W3F0-2; Sequence=VSP_031148;
CC Name=3;
CC IsoId=Q6W3F0-3; Sequence=VSP_031148, VSP_031149;
CC -!- PTM: N-glycosylation plays no role in the catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AY313449; AAQ87604.1; -; mRNA.
DR EMBL; AK086468; BAC39675.1; -; mRNA.
DR EMBL; BC082538; AAH82538.1; -; mRNA.
DR CCDS; CCDS21496.1; -. [Q6W3F0-1]
DR AlphaFoldDB; Q6W3F0; -.
DR SMR; Q6W3F0; -.
DR STRING; 10090.ENSMUSP00000055297; -.
DR GlyCosmos; Q6W3F0; 2 sites, No reported glycans.
DR GlyGen; Q6W3F0; 2 sites.
DR iPTMnet; Q6W3F0; -.
DR PhosphoSitePlus; Q6W3F0; -.
DR EPD; Q6W3F0; -.
DR MaxQB; Q6W3F0; -.
DR PaxDb; 10090-ENSMUSP00000055297; -.
DR PeptideAtlas; Q6W3F0; -.
DR ProteomicsDB; 294362; -. [Q6W3F0-1]
DR ProteomicsDB; 294363; -. [Q6W3F0-2]
DR ProteomicsDB; 294364; -. [Q6W3F0-3]
DR Pumba; Q6W3F0; -.
DR UCSC; uc012fqc.1; mouse. [Q6W3F0-3]
DR AGR; MGI:2444049; -.
DR MGI; MGI:2444049; P4ha3.
DR eggNOG; KOG1591; Eukaryota.
DR InParanoid; Q6W3F0; -.
DR PhylomeDB; Q6W3F0; -.
DR BRENDA; 1.14.11.2; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR ChiTaRS; P4ha3; mouse.
DR PRO; PR:Q6W3F0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6W3F0; Protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; ISO:MGI.
DR Gene3D; 6.10.140.1460; -; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF223; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-3; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Dioxygenase; Endoplasmic reticulum;
KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..542
FT /note="Prolyl 4-hydroxylase subunit alpha-3"
FT /id="PRO_0000317767"
FT REPEAT 225..258
FT /note="TPR"
FT DOMAIN 420..527
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 105..129
FT /evidence="ECO:0000255"
FT BINDING 438
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 440
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 508
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 518
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031148"
FT VAR_SEQ 444..464
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031149"
SQ SEQUENCE 542 AA; 60975 MW; 76329127F1C7BA83 CRC64;
MGPGARLALL ALLALGGDPA AATGREDTFS ALTSVARALA PERRLLGTLR RYLRGEEARL
RDLTRFYDKV LSLHEDLKIP VVNPLLAFTV IKRLQSDWRN VVHSLEATEN IRALKDGYEK
VEQDLPAFED LEGAARALMR LQDVYMLNVK GLARGVFQRV TGSSITDLYS PRQLFSLTAD
DCFQVGKVAY DTGDYYHAIP WLEEAVSLFR RAHGEWKTED EASLEDALDY LAFACFQVGN
VSCALSLSRE FLVYSPDNKR MARNVLKYER LLAENGHQMA AETAIQRPNV PHLQTRDTYE
GLCQTLGSQP THYQIPSLYC SYETNSSPYL LLQPARKEVV HLRPLIALYH DFVSDEEAQK
IRELAEPWLQ RSVVASGEKQ LQVEYRISKS AWLKDTVDPM LVTLDHRIAA LTGLDIQPPY
AEYLQVVNYG IGGHYEPHFD HATSPSSPLY RMKSGNRVAT FMIYLSSVEA GGATAFIYGN
FSVPVVKNAA LFWWNLHRSG EGDGDTLHAG CPVLVGDKWV ANKWIHEYGQ EFRRPCSTNP
ED
//
