ID P4HA1_HUMAN Reviewed; 534 AA. AC P13674; C9JL12; Q15082; Q15083; Q5VSQ5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 10-JUN-2026, entry version 243. DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1; DE Short=4-PH alpha-1; DE EC=1.14.11.2 {ECO:0000269|PubMed:9211872}; DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1; DE Flags: Precursor; GN Name=P4HA1; Synonyms=P4HA; 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] (ISOFORMS 1 AND 2). RX PubMed=2543975; DOI=10.1073/pnas.86.12.4392; RA Helaakoski T., Vuori K., Myllylae R., Kivirikko K.I., Pihlajaniemi T.; RT "Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the RT complete cDNA-derived amino acid sequence and evidence for alternative RT splicing of RNA transcripts."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4392-4396(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=7961714; DOI=10.1016/s0021-9258(18)46864-0; RA Helaakoski T., Veijola J., Vuori K., Rehn M., Chow L.T., Taillon-Miller P., RA Kivirikko K.I., Pihlajaniemi T.; RT "Structure and expression of the human gene for the alpha subunit of prolyl RT 4-hydroxylase. The two alternatively spliced types of mRNA correspond to RT two homologous exons the sequences of which are expressed in a variety of RT tissues."; RL J. Biol. Chem. 269:27847-27854(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023; RA Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J., RA Stuve L.L.; RT "PCR isolation and cloning of novel splice variant mRNAs from known drug RT target genes."; RL Genomics 83:566-571(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC 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). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBUNIT, COFACTOR, AND TISSUE SPECIFICITY. RX PubMed=9211872; DOI=10.1074/jbc.272.28.17342; RA Annunen P., Helaakoski T., Myllyharju J., Veijola J., Pihlajaniemi T., RA Kivirikko K.I.; RT "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) RT and characterization of the type II enzyme tetramer. The alpha(I) and RT alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer."; RL J. Biol. Chem. 272:17342-17348(1997). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-17, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-261, SUBUNIT, AND MUTAGENESIS RP OF TYR-210; TYR-213 AND TYR-247. RX PubMed=15456751; DOI=10.1074/jbc.m410007200; RA Pekkala M., Hieta R., Bergmann U., Kivirikko K.I., Wierenga R.K., RA Myllyharju J.; RT "The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is RT a tetratricopeptide repeat domain with functional aromatic residues."; RL J. Biol. Chem. 279:52255-52261(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:9211872}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-prolyl-[collagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L- CC prolyl-[collagen] + succinate + CO2; 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:9211872}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000305|PubMed:9211872}; CC Note=Binds 1 Fe(2+) ion per subunit.; CC -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC Evidence={ECO:0000305|PubMed:9211872}; CC -!- ACTIVITY REGULATION: Inhibited by poly(L-proline). CC {ECO:0000269|PubMed:9211872}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=22 uM for 2-oxoglutarate {ECO:0000269|PubMed:9211872}; CC -!- SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains CC (P4HB)(the beta chain is the multi-functional PDI), where P4HB plays CC the role of a structural subunit; this tetramer catalyzes the formation CC of 4-hydroxyproline in collagen. {ECO:0000269|PubMed:15456751, CC ECO:0000269|PubMed:9211872}. CC -!- INTERACTION: CC P13674; P42858: HTT; NbExp=5; IntAct=EBI-1237386, EBI-466029; CC P13674; P13674: P4HA1; NbExp=5; IntAct=EBI-1237386, EBI-1237386; CC P13674; O15460: P4HA2; NbExp=2; IntAct=EBI-1237386, EBI-348033; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P13674-1; Sequence=Displayed; CC Name=2; CC IsoId=P13674-2; Sequence=VSP_004504; CC Name=3; CC IsoId=P13674-3; Sequence=VSP_004504, VSP_044578; CC -!- TISSUE SPECIFICITY: Expressed in the heart, liver, skeletal muscle, CC kidney, placenta, lung and pancreas. {ECO:0000269|PubMed:9211872}. 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; M24486; AAA36534.1; -; mRNA. DR EMBL; M24487; AAA36535.1; -; mRNA. DR EMBL; U14620; AAA59068.1; -; Genomic_DNA. DR EMBL; U14607; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14605; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14608; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14609; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14611; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14610; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14612; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14614; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14615; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14616; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14617; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14618; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14619; AAA59068.1; JOINED; Genomic_DNA. DR EMBL; U14620; AAA59069.1; -; Genomic_DNA. DR EMBL; U14607; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14605; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14608; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14609; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14611; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14610; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14612; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14613; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14615; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14616; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14617; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14618; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; U14619; AAA59069.1; JOINED; Genomic_DNA. DR EMBL; CD013929; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL731563; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034998; AAH34998.1; -; mRNA. DR CCDS; CCDS41537.1; -. [P13674-1] DR CCDS; CCDS44432.1; -. [P13674-3] DR CCDS; CCDS7320.1; -. [P13674-2] DR PIR; A33919; DAHUA1. DR PIR; I37173; DAHUA2. DR RefSeq; NP_000908.2; NM_000917.4. [P13674-2] DR RefSeq; NP_001017962.1; NM_001017962.3. [P13674-1] DR RefSeq; NP_001136067.1; NM_001142595.2. [P13674-1] DR RefSeq; NP_001136068.1; NM_001142596.2. [P13674-3] DR PDB; 1TJC; X-ray; 2.30 A; A/B=161-261. DR PDB; 2V5F; X-ray; 2.03 A; A=161-263. DR PDB; 2YQ8; X-ray; 2.99 A; A/B=18-255. DR PDB; 4BT8; X-ray; 2.20 A; A/B=18-255. DR PDB; 4BT9; X-ray; 1.90 A; A/B=18-255. DR PDB; 4BTA; X-ray; 2.95 A; A/B=18-261. DR PDB; 4BTB; X-ray; 1.90 A; A=18-255. DR PDB; 9HPQ; X-ray; 2.17 A; A/B/C/D=160-255. DR PDB; 9HRE; X-ray; 2.05 A; A/B/C/D=160-255. DR PDB; 9HT8; X-ray; 2.15 A; A/B=160-255. DR PDBsum; 1TJC; -. DR PDBsum; 2V5F; -. DR PDBsum; 2YQ8; -. DR PDBsum; 4BT8; -. DR PDBsum; 4BT9; -. DR PDBsum; 4BTA; -. DR PDBsum; 4BTB; -. DR PDBsum; 9HPQ; -. DR PDBsum; 9HRE; -. DR PDBsum; 9HT8; -. DR AlphaFoldDB; P13674; -. DR SMR; P13674; -. DR BioGRID; 111072; 324. DR CORUM; P13674; -. DR DIP; DIP-38180N; -. DR FunCoup; P13674; 1913. DR IntAct; P13674; 162. DR MINT; P13674; -. DR NDEx; IQUERY-CP-P4HA1; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000263556; -. DR BindingDB; P13674; -. DR ChEMBL; CHEMBL1250350; -. DR DrugBank; DB00126; Ascorbic acid. DR DrugBank; DB01275; Hydralazine. DR DrugBank; DB20345; Lufironil. DR DrugBank; DB00172; Proline. DR DrugBank; DB20553; Safironil. DR DrugBank; DB00139; Succinic acid. DR DrugCentral; P13674; -. DR GlyConnect; P13674; 9 N-Linked glycans (1 site). DR GlyCosmos; P13674; 2 sites, 8 glycans. DR GlyGen; P13674; 4 sites, 24 N-linked glycans (2 sites), 2 O-linked glycans (2 sites). DR iPTMnet; P13674; -. DR MetOSite; P13674; -. DR PhosphoSitePlus; P13674; -. DR SwissPalm; P13674; -. DR BioMuta; P4HA1; -. DR DMDM; 2507090; -. DR jPOST; P13674; -. DR MassIVE; P13674; -. DR PaxDb; 9606-ENSP00000263556; -. DR PeptideAtlas; P13674; -. DR ProteomicsDB; 10641; -. DR ProteomicsDB; 52957; -. [P13674-1] DR ProteomicsDB; 52958; -. [P13674-2] DR Pumba; P13674; -. DR Antibodypedia; 2000; 253 antibodies from 32 providers. DR DNASU; 5033; -. DR Ensembl; ENST00000263556.3; ENSP00000263556.3; ENSG00000122884.14. [P13674-2] DR Ensembl; ENST00000307116.6; ENSP00000307318.2; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000373008.7; ENSP00000362099.1; ENSG00000122884.14. [P13674-2] DR Ensembl; ENST00000394890.7; ENSP00000378353.2; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000440381.5; ENSP00000414464.1; ENSG00000122884.14. [P13674-3] DR Ensembl; ENST00000886200.1; ENSP00000556259.1; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000886201.1; ENSP00000556260.1; ENSG00000122884.14. [P13674-2] DR Ensembl; ENST00000886207.1; ENSP00000556266.1; ENSG00000122884.14. [P13674-2] DR Ensembl; ENST00000886209.1; ENSP00000556268.1; ENSG00000122884.14. [P13674-2] DR Ensembl; ENST00000886210.1; ENSP00000556269.1; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000924332.1; ENSP00000594391.1; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000924333.1; ENSP00000594392.1; ENSG00000122884.14. [P13674-3] DR Ensembl; ENST00000951393.1; ENSP00000621452.1; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000951394.1; ENSP00000621453.1; ENSG00000122884.14. [P13674-1] DR Ensembl; ENST00000951395.1; ENSP00000621454.1; ENSG00000122884.14. [P13674-1] DR GeneID; 5033; -. DR KEGG; hsa:5033; -. DR MANE-Select; ENST00000394890.7; ENSP00000378353.2; NM_001017962.3; NP_001017962.1. DR UCSC; uc001jtg.4; human. [P13674-1] DR AGR; HGNC:8546; -. DR ClinPGx; PA32874; -. DR CTD; 5033; -. DR DisGeNET; 5033; -. DR GeneCards; P4HA1; -. DR HGNC; HGNC:8546; P4HA1. DR HPA; ENSG00000122884; Low tissue specificity. DR MalaCards; P4HA1; -. DR MIM; 176710; gene. DR OpenTargets; ENSG00000122884; -. DR VEuPathDB; HostDB:ENSG00000122884; -. DR eggNOG; KOG1591; Eukaryota. DR GeneTree; ENSGT00940000156635; -. DR HOGENOM; CLU_024155_1_1_1; -. DR InParanoid; P13674; -. DR OMA; YLPHFDF; -. DR OrthoDB; 420380at2759; -. DR PAN-GO; P13674; 3 GO annotations based on evolutionary models. DR PhylomeDB; P13674; -. DR BioCyc; MetaCyc:HS04613-MONOMER; -. DR BRENDA; 1.14.11.2; 2681. DR PathwayCommons; P13674; -. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-9918432; Maturation of DENV proteins. DR SignaLink; P13674; -. DR Agora; ENSG00000122884; -. DR BioGRID-ORCS; 5033; 25 hits in 1163 CRISPR screens. DR ChiTaRS; P4HA1; human. DR EvolutionaryTrace; P13674; -. DR GeneWiki; P4HA1; -. DR GenomeRNAi; 5033; -. DR Pharos; P13674; Tchem. DR PRO; PR:P13674; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P13674; protein. DR Bgee; ENSG00000122884; Expressed in cartilage tissue and 207 other cell types or tissues. DR ExpressionAtlas; P13674; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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; IDA:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR DisProt; DP03259; -. DR FunFam; 1.25.40.10:FF:000006; Prolyl 4-hydroxylase subunit alpha 2; 1. DR FunFam; 2.60.120.620:FF:000001; Prolyl 4-hydroxylase subunit alpha 2; 1. 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_dom. DR InterPro; IPR013547; P4H_N. DR InterPro; IPR045054; P4HA-like. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR059068; TPR_P4H. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1. DR PANTHER; PTHR10869:SF101; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1; 1. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR Pfam; PF08336; P4Ha_N; 1. DR Pfam; PF23558; TPR_P4H; 1. DR SMART; SM00702; P4Hc; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Dioxygenase; Endoplasmic reticulum; KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; KW Proteomics identification; Reference proteome; Signal; TPR repeat; KW Vitamin C. FT SIGNAL 1..17 FT /evidence="ECO:0007744|PubMed:25944712" FT CHAIN 18..534 FT /note="Prolyl 4-hydroxylase subunit alpha-1" FT /id="PRO_0000022723" FT REPEAT 205..238 FT /note="TPR" FT DOMAIN 411..519 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 429 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 431 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 500 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 510 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT VAR_SEQ 361..380 FT /note="RRATISNPITGDLETVHYRI -> SRATVHDPETGKLTTAQYRV (in FT isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15028279, FT ECO:0000303|PubMed:2543975" FT /id="VSP_004504" FT VAR_SEQ 417..434 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15028279" FT /id="VSP_044578" FT MUTAGEN 210 FT /note="Y->A: Strongly reduced affinity for peptide FT substrate." FT /evidence="ECO:0000269|PubMed:15456751" FT MUTAGEN 213 FT /note="Y->A: Strongly reduced affinity for peptide FT substrate." FT /evidence="ECO:0000269|PubMed:15456751" FT MUTAGEN 247 FT /note="Y->A: Strongly reduced affinity for peptide FT substrate." FT /evidence="ECO:0000269|PubMed:15456751" FT CONFLICT 119..122 FT /note="QYFP -> PVLS (in Ref. 1; AAA36534/AAA36535)" FT /evidence="ECO:0000305" FT HELIX 21..71 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 74..79 FT /evidence="ECO:0007829|PDB:4BT9" FT HELIX 81..89 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 90..94 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 95..103 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 124..141 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 145..149 FT /evidence="ECO:0007829|PDB:4BTB" FT STRAND 153..156 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 164..176 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 180..195 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 204..217 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 221..234 FT /evidence="ECO:0007829|PDB:4BTB" FT HELIX 239..252 FT /evidence="ECO:0007829|PDB:4BTB" SQ SEQUENCE 534 AA; 61049 MW; EBAFA8CCF09A1DDB CRC64; MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY FPNDEDQVGA AKALLRLQDT YNLDTDTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY YHTELWMEQA LRQLDEGEIS TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR ANGNLKYFEY IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE //