ID G4VTC9_SCHMA Unreviewed; 584 AA. AC G4VTC9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 02-SEP-2026, entry version 73. DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269}; DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269}; OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; OC Rhabditophora; Neodermata; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_068280.1}; RN [1] {ECO:0000313|Proteomes:UP000008854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854}; RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455; RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A., RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C., RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J., RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A., RA Zerlotini A., Dunne D.W., Berriman M.; RT "A systematically improved high quality genome and transcriptome of the RT human blood fluke Schistosoma mansoni."; RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012). RN [2] {ECO:0000313|WBParaSite:Smp_068280.1} RP IDENTIFICATION. RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_068280.1}; RG WormBaseParasite; RL Submitted (DEC-2018) to UniProtKB. CC -!- FUNCTION: Catalyzes the post-translational formation of 4- CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other CC proteins. {ECO:0000256|ARBA:ARBA00002035}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU00805}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU00805}; CC -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC Evidence={ECO:0000256|ARBA:ARBA00001961}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000256|ARBA:ARBA00004319}. CC -!- SIMILARITY: Belongs to the P4HA family. CC {ECO:0000256|ARBA:ARBA00006511}. 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 RefSeq; XP_018654586.1; XM_018789110.1. DR AlphaFoldDB; G4VTC9; -. DR FunCoup; G4VTC9; 354. DR STRING; 6183.G4VTC9; -. DR GeneID; 8354649; -. DR KEGG; smm:Smp_068280; -. DR WBParaSite; Smp_068280.1; Smp_068280.1; Smp_068280. DR CTD; 8354649; -. DR eggNOG; KOG1591; Eukaryota. DR HOGENOM; CLU_024155_1_1_1; -. DR InParanoid; G4VTC9; -. DR OMA; YLPHFDF; -. DR OrthoDB; 420380at2759; -. DR PhylomeDB; G4VTC9; -. DR Proteomes; UP000008854; Unassembled WGS sequence. 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:InterPro. DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC. 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 PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1. DR PANTHER; PTHR10869:SF244; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 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. PE 3: Inferred from homology; KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|PROSITE- KW ProRule:PRU00805}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00805}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00805}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE- KW ProRule:PRU00805}; Reference proteome {ECO:0000313|Proteomes:UP000008854}; KW Signal {ECO:0000256|SAM:SignalP}; KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..584 FT /note="procollagen-proline 4-dioxygenase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030172039" FT DOMAIN 455..562 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000259|PROSITE:PS51471" FT BINDING 473 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00805" FT BINDING 475 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00805" FT BINDING 543 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00805" FT BINDING 553 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00805" SQ SEQUENCE 584 AA; 66246 MW; 8A6FCA4BEF3A47AB CRC64; MALLSFTVTW LLLFQQKYIN AEYYTAVVDI TKAWRLSQEL VSDLNSYIAL EEGRLNRIRK VVKVLDSNGS ISDASSTLNQ QNNDLEEYLG NPINAYLTMK RLSSSWKSQL SQLVDNVPNG FQKGDTDGSD YLNISDAQNT ITMNTIRSRV KQHTDMLPGD NDVSGAVDAI LRLQSTYKLP ARRLAYGQLI DNLSTPQLSA AQCLEVGRHA YLQGDFEQSE EWFRVAYDRL FDELEEKREV DAQGTTIAND ETEENGETEP TVGQILDYLA YSLGRQGRYA EALNVTRLLI EEEPTNTRAI NNEAYYVEQI DRGEGRIGPN PRSQAISKHD QETELYESLC RNENPFPTVP SHHLTCRYYT PHAFFKIGPV KEETLNPDPR IVMWYDLIFP SEIEKIKELA TPRLRRATVK NPVTGILEIA FYRTSKSAWL PHSMSEITDQ ISQRIRAVTG LSLETAEDLQ VGNYGLGGHY APHFDFGRKR EKDAFEVKNG NRIATIIFYL SDVQAGGATV FNRIGTRVVP KKGAAGFWFN LLPNGEGDLR TRHAACPVLA GSKWVMNLWF HERGQEFRRP CELERGTVET DDDF //