ID B4NGW2_DROWI Unreviewed; 550 AA. AC B4NGW2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269}; DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269}; GN Name=Dwil\GK14136 {ECO:0000313|EMBL:EDW84459.1}; GN ORFNames=Dwil_GK14136 {ECO:0000313|EMBL:EDW84459.1}; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW84459.1, ECO:0000313|Proteomes:UP000007798}; RN [1] {ECO:0000313|EMBL:EDW84459.1, ECO:0000313|Proteomes:UP000007798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). 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=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 EMBL; CH964272; EDW84459.1; -; Genomic_DNA. DR RefSeq; XP_002073473.1; XM_002073437.2. DR AlphaFoldDB; B4NGW2; -. DR STRING; 7260.B4NGW2; -. DR EnsemblMetazoa; FBtr0244787; FBpp0243279; FBgn0216142. DR GeneID; 6651537; -. DR KEGG; dwi:6651537; -. DR eggNOG; KOG1591; Eukaryota. DR HOGENOM; CLU_024155_1_1_1; -. DR InParanoid; B4NGW2; -. DR OMA; NLTQYRN; -. DR OrthoDB; 2899308at2759; -. DR PhylomeDB; B4NGW2; -. DR Proteomes; UP000007798; 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 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:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 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. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:EDW84459.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007798}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..550 FT /note="procollagen-proline 4-dioxygenase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002816956" FT DOMAIN 422..530 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000259|PROSITE:PS51471" FT COILED 50..77 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 550 AA; 62876 MW; AF8CB5CF067B62F0 CRC64; MLPIWTNLGL VGLLLLCISG VRGELYTALA EMEELLETES VLINNLEGYI RVQEDKLSYL KNKMDEYQRE HADASSDITA YVSNPINAYL LTKRLTTDWR QVENLMEHDV GGAFLQNLTQ YRNVLKFPSD EDLNGAAVAL LRLQDTYQLD TSSVARGKLN GIQYSTAMSS DDCFELGRQS YVNHDYYHTV LWMNEAMSRM LEETHNQTQT FTRADILEYL AFSTYKQGNV ESALLMTNEL LQLLPYHERA NGNKKFYEKE IAHLKEMKRM KGDDGSDEMP VSDLPVAKSD PGVYDITERK AYEMLCRGEL KPSPADLRPL RCRYVTNNVP FLRLGPLKLE EAHMDPYIVI YHDAMYDSEM DLIKRMARPR FRRATVQNSV TGALETANYR ISKSAWLKTE EDQVIGTVVQ RTADMTGLDM DSAEELQVVN YGIGGHYEPH FDFARREEKR AFEGLNLGNR IATVLFYMSD VEQGGATVFT SLHAALWPKK GTAAFWMNLH RDGEGDVRTR HAACPVLTGT KWVSNKWIHE RGQEFRRSCD LTEDHGDFAI //