ID P4HA1_PONAB Reviewed; 534 AA. AC Q5RAG8; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 02-SEP-2026, entry version 106. DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1; DE Short=4-PH alpha-1; DE EC=1.14.11.2 {ECO:0000250|UniProtKB:P13674}; DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1; DE Flags: Precursor; GN Name=P4HA1; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex, and Heart; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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:P13674}. 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:0000250|UniProtKB:P13674}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00805}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00805}; CC -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC Evidence={ECO:0000250|UniProtKB:P13674}; 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:0000250|UniProtKB:P13674}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. 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; CR859049; CAH91242.1; -; mRNA. DR EMBL; CR926085; CAI29712.1; -; mRNA. DR RefSeq; NP_001125733.1; NM_001132261.2. DR AlphaFoldDB; Q5RAG8; -. DR SMR; Q5RAG8; -. DR FunCoup; Q5RAG8; 1899. DR IntAct; Q5RAG8; 1. DR MINT; Q5RAG8; -. DR STRING; 9601.ENSPPYP00000002727; -. DR GlyCosmos; Q5RAG8; 2 sites, No reported glycans. DR Ensembl; ENSPPYT00000056106.1; ENSPPYP00000043789.1; ENSPPYG00000002348.3. DR GeneID; 100172658; -. DR KEGG; pon:100172658; -. DR CTD; 5033; -. DR eggNOG; KOG1591; Eukaryota. DR GeneTree; ENSGT00940000156635; -. DR InParanoid; Q5RAG8; -. DR OrthoDB; 420380at2759; -. DR Proteomes; UP000001595; Chromosome 10. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro. DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; ISS:UniProtKB. 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 2: Evidence at transcript level; KW Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C. FT SIGNAL 1..17 FT /evidence="ECO:0000250" FT CHAIN 18..534 FT /note="Prolyl 4-hydroxylase subunit alpha-1" FT /id="PRO_0000041835" 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:0000255" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" 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 //