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Database: UniProt
Entry: A0A0E0GHA1_ORYNI
LinkDB: A0A0E0GHA1_ORYNI
Original site: A0A0E0GHA1_ORYNI 
ID   A0A0E0GHA1_ORYNI        Unreviewed;       669 AA.
AC   A0A0E0GHA1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA03G04730.2};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA03G04730.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G04730.2};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA03G04730.2}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G04730.2};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC         trans-4-hydroxy-L-prolyl-[collagen]; 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:0000256|ARBA:ARBA00024151};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the P4HA family.
CC       {ECO:0000256|ARBA:ARBA00006511}.
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DR   AlphaFoldDB; A0A0E0GHA1; -.
DR   STRING; 4536.A0A0E0GHA1; -.
DR   EnsemblPlants; ONIVA03G04730.2; ONIVA03G04730.2; ONIVA03G04730.
DR   Gramene; ONIVA03G04730.2; ONIVA03G04730.2; ONIVA03G04730.
DR   eggNOG; KOG1591; Eukaryota.
DR   HOGENOM; CLU_450861_0_0_1; -.
DR   OMA; WTMLPTG; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; 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; 2.60.120.620; q2cbj1_9rhob like domain; 2.
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; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10869:SF219; OS03G0166100 PROTEIN; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 2.
DR   Pfam; PF01549; ShK; 2.
DR   SMART; SM00702; P4Hc; 2.
DR   SMART; SM00254; ShKT; 2.
DR   PROSITE; PS51471; FE2OG_OXY; 2.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..669
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002360518"
FT   TRANSMEM        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..265
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          491..613
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   669 AA;  73258 MW;  907584160B2D8D29 CRC64;
     MARLVLLAVL PLLLLFVAGD SYATAAGGGG GGGGRRFDAS RAVDVSWRPR AFLYEGFLSD
     AECDHLISLA KQGKMEKSTV VDGESGESVT SKVRTSSGMF LDKKQDEVVA RIEERIAAWT
     MLPTECIIFY CFANFAILKL SENGESMQIL RYGQGEKYEP HFDYISGRQG STREGDRVAT
     VLMYLSNVKM GGETIFPDCE ARLSQPKDET WSDCAEQGFA VKPAKGSAVL FFSLHPNATL
     DTDSLHGSCP VIEGEKWSAT KWIHVRSYSY RRRSAGKCED EHVLCSSWAA AGECAKNPGY
     MVGTSDSPPG FCRKSCNAGG ARLCRRRRRT GMARLVLLVA LLLLLSVTGE TSATGGGGEG
     GRFDASRAVD VSWSPRVFLY EGFLSDAECE HLIALAKQGR MERSTVVNGK SGESVMSKTR
     TSSGMFLIRK QDEVVARIEE RIAAWTMFPA GMVQGHRTLE NCLIGPCSKC SSECITFYCF
     ARFVILERSE NGESMQMLRY GQGEKYEPHF DYIRGRQASA RGGHRIATVL MYLSNVKMGG
     ETVFPDAEAR LSQPKDETWS DCAEQGFAVK PTKGSAVLFF SLYPNATFDP GSLHGSCPVI
     QGEKWSATKW IHVRSYDENG RRSSDKCEDE HALCSSWAAA GECAKNPGYM VGTSESPGFC
     RKSCNVCTS
//
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