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 27-MAR-2024, entry version 170. 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; 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; Q9NSG2: FIRRM; NbExp=3; IntAct=EBI-10181968, EBI-11128910; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 143. DR CORUM; Q7Z4N8; -. DR IntAct; Q7Z4N8; 103. DR MINT; Q7Z4N8; -. DR STRING; 9606.ENSP00000401749; -. DR GlyCosmos; Q7Z4N8; 2 sites, No reported glycans. 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; 9606-ENSP00000401749; -. DR PeptideAtlas; Q7Z4N8; -. DR ProteomicsDB; 5178; -. DR ProteomicsDB; 69217; -. [Q7Z4N8-1] DR ProteomicsDB; 69218; -. [Q7Z4N8-2] DR Pumba; Q7Z4N8; -. DR Antibodypedia; 2002; 165 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 AGR; HGNC:30135; -. 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; DVYMPAV; -. DR OrthoDB; 2899308at2759; -. 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 1152 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 136 other cell types or tissues. DR ExpressionAtlas; Q7Z4N8; baseline and differential. 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 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. DR Genevisible; Q7Z4N8; HS. 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 //