ID   G4VTC9_SCHMA            Unreviewed;       584 AA.
AC   G4VTC9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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; Trematoda;
OC   Digenea; Strigeidida; 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=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}.
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DR   RefSeq; XP_018654586.1; XM_018789110.1.
DR   AlphaFoldDB; G4VTC9; -.
DR   STRING; 6183.G4VTC9; -.
DR   EnsemblMetazoa; Smp_068280.1; Smp_068280.1; Smp_068280.
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; NWEMKDI; -.
DR   OrthoDB; 2899308at2759; -.
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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW   Signal {ECO:0000256|SAM:SignalP}.
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"
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
//