P4HA3_HUMAN
ID P4HA3_HUMAN Reviewed; 544 AA.
AC Q7Z4N8; A0AV13; B4DUD3; Q5EBL3; Q5JPA9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-3;
DE Short=4-PH alpha-3;
DE EC=1.14.11.2 {ECO:0000269|PubMed:14500733};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3;
DE Flags: Precursor;
GN Name=P4HA3; ORFNames=UNQ711/PRO1374;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, TISSUE
RP SPECIFICITY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Umbilical vein endothelial cell;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Vascular smooth muscle;
RX PubMed=12874193; DOI=10.1161/01.cir.0000080883.53863.5c;
RA Van Den Diepstraten C., Papay K., Bolender Z., Brown A., Pickering J.G.;
RT "Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous
RT cap of human atherosclerotic plaque.";
RL Circulation 108:508-511(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-400.
RC TISSUE=Colon;
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:0000269|PubMed:12874193, ECO:0000269|PubMed:14500733}.
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:0000269|PubMed:14500733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18946;
CC Evidence={ECO:0000305|PubMed:14500733};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:14500733};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000305|PubMed:14500733};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for Fe(2+) {ECO:0000269|PubMed:14500733};
CC KM=20 uM for 2-oxoglutarate {ECO:0000269|PubMed:14500733};
CC KM=24 uM for (Pro-Pro-Gly) {ECO:0000269|PubMed:14500733};
CC KM=370 uM for L-ascorbate {ECO:0000269|PubMed:14500733};
CC -!- SUBUNIT: Heterotetramer of two alpha-3 chains and two beta chains (the
CC beta chain is the multi-functional PDI). {ECO:0000269|PubMed:12874193,
CC ECO:0000269|PubMed:14500733}.
CC -!- INTERACTION:
CC Q7Z4N8; O14734: ACOT8; NbExp=3; IntAct=EBI-10181968, EBI-1237371;
CC Q7Z4N8; P18825: ADRA2C; NbExp=3; IntAct=EBI-10181968, EBI-12015266;
CC Q7Z4N8; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-10181968, EBI-12224467;
CC Q7Z4N8; Q86V38: ATN1; NbExp=3; IntAct=EBI-10181968, EBI-11954292;
CC Q7Z4N8; Q9BPU9: B9D2; NbExp=3; IntAct=EBI-10181968, EBI-6958971;
CC Q7Z4N8; O95429: BAG4; NbExp=3; IntAct=EBI-10181968, EBI-2949658;
CC Q7Z4N8; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-10181968, EBI-465872;
CC Q7Z4N8; Q9NSG2: C1orf112; NbExp=3; IntAct=EBI-10181968, EBI-11128910;
CC Q7Z4N8; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-10181968, EBI-2817707;
CC Q7Z4N8; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-10181968, EBI-12261896;
CC Q7Z4N8; P17540: CKMT2; NbExp=3; IntAct=EBI-10181968, EBI-712973;
CC Q7Z4N8; Q16740: CLPP; NbExp=3; IntAct=EBI-10181968, EBI-1056029;
CC Q7Z4N8; Q8WUE5: CT55; NbExp=3; IntAct=EBI-10181968, EBI-6873363;
CC Q7Z4N8; P78358: CTAG1B; NbExp=3; IntAct=EBI-10181968, EBI-1188472;
CC Q7Z4N8; Q9NSA3: CTNNBIP1; NbExp=3; IntAct=EBI-10181968, EBI-747082;
CC Q7Z4N8; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-10181968, EBI-465804;
CC Q7Z4N8; Q96C01: FAM136A; NbExp=3; IntAct=EBI-10181968, EBI-373319;
CC Q7Z4N8; Q9NZ52-2: GGA3; NbExp=3; IntAct=EBI-10181968, EBI-12075758;
CC Q7Z4N8; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-10181968, EBI-347538;
CC Q7Z4N8; O14964: HGS; NbExp=6; IntAct=EBI-10181968, EBI-740220;
CC Q7Z4N8; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-10181968, EBI-1048945;
CC Q7Z4N8; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-10181968, EBI-12111050;
CC Q7Z4N8; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-10181968, EBI-10261141;
CC Q7Z4N8; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-10181968, EBI-18273118;
CC Q7Z4N8; P43356: MAGEA2B; NbExp=4; IntAct=EBI-10181968, EBI-5650739;
CC Q7Z4N8; Q96E03: MAGEA2B; NbExp=3; IntAct=EBI-10181968, EBI-10239285;
CC Q7Z4N8; Q9UBF1: MAGEC2; NbExp=4; IntAct=EBI-10181968, EBI-5651487;
CC Q7Z4N8; P59942: MCCD1; NbExp=3; IntAct=EBI-10181968, EBI-11987923;
CC Q7Z4N8; P50222: MEOX2; NbExp=3; IntAct=EBI-10181968, EBI-748397;
CC Q7Z4N8; Q9UJ68: MSRA; NbExp=3; IntAct=EBI-10181968, EBI-19157918;
CC Q7Z4N8; A0A0S2Z3Y6: NDN; NbExp=3; IntAct=EBI-10181968, EBI-16435852;
CC Q7Z4N8; A0A0S2Z442: NDN; NbExp=3; IntAct=EBI-10181968, EBI-16435864;
CC Q7Z4N8; Q9BSH3: NICN1; NbExp=3; IntAct=EBI-10181968, EBI-13324229;
CC Q7Z4N8; Q86Y26: NUTM1; NbExp=4; IntAct=EBI-10181968, EBI-10178410;
CC Q7Z4N8; O43482: OIP5; NbExp=3; IntAct=EBI-10181968, EBI-536879;
CC Q7Z4N8; O75360: PROP1; NbExp=3; IntAct=EBI-10181968, EBI-9027467;
CC Q7Z4N8; P28070: PSMB4; NbExp=3; IntAct=EBI-10181968, EBI-603350;
CC Q7Z4N8; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-10181968, EBI-12123390;
CC Q7Z4N8; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-10181968, EBI-6257312;
CC Q7Z4N8; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-10181968, EBI-12823227;
CC Q7Z4N8; Q53GC0: SERTAD1; NbExp=3; IntAct=EBI-10181968, EBI-2826300;
CC Q7Z4N8; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-10181968, EBI-748621;
CC Q7Z4N8; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-10181968, EBI-725557;
CC Q7Z4N8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10181968, EBI-11741437;
CC Q7Z4N8; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-10181968, EBI-12815137;
CC Q7Z4N8; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-10181968, EBI-2559305;
CC Q7Z4N8; O43379: WDR62; NbExp=3; IntAct=EBI-10181968, EBI-714790;
CC Q7Z4N8; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-10181968, EBI-11522250;
CC Q7Z4N8; Q5D1E8: ZC3H12A; NbExp=6; IntAct=EBI-10181968, EBI-747793;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z4N8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4N8-2; Sequence=VSP_031146, VSP_031147;
CC Name=3;
CC IsoId=Q7Z4N8-3; Sequence=VSP_054131;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, liver and fetal skin.
CC Weakly expressed in fetal epiphyseal cartilage, fetal liver,
CC fibroblast, lung and skeletal muscle. Expressed also in fibrous cap of
CC carotid atherosclerotic lesions. {ECO:0000269|PubMed:12874193,
CC ECO:0000269|PubMed:14500733}.
CC -!- PTM: N-glycosylation plays no role in the catalytic activity.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AY313448; AAQ87603.1; -; mRNA.
DR EMBL; AY327887; AAP97874.1; -; mRNA.
DR EMBL; AY358521; AAQ88885.1; -; mRNA.
DR EMBL; AK300598; BAG62295.1; -; mRNA.
DR EMBL; AP000577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833965; CAI46215.1; -; mRNA.
DR EMBL; CH471076; EAW74935.1; -; Genomic_DNA.
DR EMBL; BC089446; AAH89446.1; -; mRNA.
DR EMBL; BC117333; AAI17334.1; -; mRNA.
DR EMBL; BC126170; AAI26171.1; -; mRNA.
DR CCDS; CCDS73347.1; -. [Q7Z4N8-3]
DR CCDS; CCDS8230.1; -. [Q7Z4N8-1]
DR RefSeq; NP_001275677.1; NM_001288748.1. [Q7Z4N8-3]
DR RefSeq; NP_878907.1; NM_182904.4. [Q7Z4N8-1]
DR AlphaFoldDB; Q7Z4N8; -.
DR SMR; Q7Z4N8; -.
DR BioGRID; 129495; 141.
DR CORUM; Q7Z4N8; -.
DR IntAct; Q7Z4N8; 103.
DR MINT; Q7Z4N8; -.
DR STRING; 9606.ENSP00000401749; -.
DR GlyGen; Q7Z4N8; 2 sites.
DR iPTMnet; Q7Z4N8; -.
DR PhosphoSitePlus; Q7Z4N8; -.
DR BioMuta; P4HA3; -.
DR DMDM; 74738714; -.
DR MassIVE; Q7Z4N8; -.
DR MaxQB; Q7Z4N8; -.
DR PaxDb; Q7Z4N8; -.
DR PeptideAtlas; Q7Z4N8; -.
DR PRIDE; Q7Z4N8; -.
DR ProteomicsDB; 5178; -.
DR ProteomicsDB; 69217; -. [Q7Z4N8-1]
DR ProteomicsDB; 69218; -. [Q7Z4N8-2]
DR Antibodypedia; 2002; 151 antibodies from 24 providers.
DR DNASU; 283208; -.
DR Ensembl; ENST00000331597.9; ENSP00000332170.4; ENSG00000149380.12. [Q7Z4N8-1]
DR Ensembl; ENST00000427714.2; ENSP00000401749.2; ENSG00000149380.12. [Q7Z4N8-3]
DR Ensembl; ENST00000524388.5; ENSP00000433860.1; ENSG00000149380.12. [Q7Z4N8-2]
DR GeneID; 283208; -.
DR KEGG; hsa:283208; -.
DR MANE-Select; ENST00000331597.9; ENSP00000332170.4; NM_182904.5; NP_878907.1.
DR UCSC; uc001ouz.5; human. [Q7Z4N8-1]
DR CTD; 283208; -.
DR DisGeNET; 283208; -.
DR GeneCards; P4HA3; -.
DR HGNC; HGNC:30135; P4HA3.
DR HPA; ENSG00000149380; Tissue enhanced (smooth).
DR MIM; 608987; gene.
DR neXtProt; NX_Q7Z4N8; -.
DR OpenTargets; ENSG00000149380; -.
DR PharmGKB; PA134870931; -.
DR VEuPathDB; HostDB:ENSG00000149380; -.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000158967; -.
DR HOGENOM; CLU_024155_0_0_1; -.
DR InParanoid; Q7Z4N8; -.
DR OMA; EFAEPWL; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; Q7Z4N8; -.
DR TreeFam; TF313393; -.
DR BRENDA; 1.14.11.2; 2681.
DR PathwayCommons; Q7Z4N8; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; Q7Z4N8; -.
DR BioGRID-ORCS; 283208; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; P4HA3; human.
DR GenomeRNAi; 283208; -.
DR Pharos; Q7Z4N8; Tbio.
DR PRO; PR:Q7Z4N8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q7Z4N8; protein.
DR Bgee; ENSG00000149380; Expressed in decidua and 134 other tissues.
DR ExpressionAtlas; Q7Z4N8; baseline and differential.
DR Genevisible; Q7Z4N8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 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; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..544
FT /note="Prolyl 4-hydroxylase subunit alpha-3"
FT /id="PRO_0000317766"
FT REPEAT 227..260
FT /note="TPR"
FT DOMAIN 422..529
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 107..131
FT /evidence="ECO:0000255"
FT BINDING 440
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 442
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 510
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 520
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 257
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031146"
FT VAR_SEQ 258..544
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031147"
FT VAR_SEQ 490..544
FT /note="NAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSSS
FT PED -> HCFGGTCTGVVKGTVTHFMLAVLSWWEISGWPTSGYMSMDRNSADPAAPALK
FT TELLAERSWWSPVAFQRSQEPKAGVGEEKAEQPPGRRPCQLCLCLANQRQGRGCYQGTL
FT RMYI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054131"
FT VARIANT 400
FT /note="D -> N (in dbSNP:rs2282488)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038675"
FT CONFLICT 222
FT /note="D -> Y (in Ref. 8; AAH89446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 61126 MW; 1C88C168A268572F CRC64;
MGPGARLAAL LAVLALGTGD PERAAARGDT FSALTSVARA LAPERRLLGL LRRYLRGEEA
RLRDLTRFYD KVLSLHEDST TPVANPLLAF TLIKRLQSDW RNVVHSLEAS ENIRALKDGY
EKVEQDLPAF EDLEGAARAL MRLQDVYMLN VKGLARGVFQ RVTGSAITDL YSPKRLFSLT
GDDCFQVGKV AYDMGDYYHA IPWLEEAVSL FRGSYGEWKT EDEASLEDAL DHLAFAYFRA
GNVSCALSLS REFLLYSPDN KRMARNVLKY ERLLAESPNH VVAEAVIQRP NIPHLQTRDT
YEGLCQTLGS QPTLYQIPSL YCSYETNSNA YLLLQPIRKE VIHLEPYIAL YHDFVSDSEA
QKIRELAEPW LQRSVVASGE KQLQVEYRIS KSAWLKDTVD PKLVTLNHRI AALTGLDVRP
PYAEYLQVVN YGIGGHYEPH FDHATSPSSP LYRMKSGNRV ATFMIYLSSV EAGGATAFIY
ANLSVPVVRN AALFWWNLHR SGEGDSDTLH AGCPVLVGDK WVANKWIHEY GQEFRRPCSS
SPED
