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Database: UniProt
Entry: A0A1D6KVC3_MAIZE
LinkDB: A0A1D6KVC3_MAIZE
Original site: A0A1D6KVC3_MAIZE 
ID   A0A1D6KVC3_MAIZE        Unreviewed;       372 AA.
AC   A0A1D6KVC3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN   ORFNames=ZEAMMB73_Zm00001d032974 {ECO:0000313|EMBL:ONM06482.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM06482.1};
RN   [1] {ECO:0000313|EMBL:ONM06482.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM06482.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CM007647; ONM06482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6KVC3; -.
DR   SMR; A0A1D6KVC3; -.
DR   IntAct; A0A1D6KVC3; 3.
DR   STRING; 4577.A0A1D6KVC3; -.
DR   PaxDb; 4577-GRMZM2G520535_P01; -.
DR   eggNOG; KOG1591; Eukaryota.
DR   InParanoid; A0A1D6KVC3; -.
DR   ExpressionAtlas; A0A1D6KVC3; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like 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; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10869:SF235; PROLYL 4-HYDROXYLASE 6-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SMART; SM00254; ShKT; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   372 AA;  41208 MW;  119C6B34496040D9 CRC64;
     METVRWAMEV GVWARCLGVG LLATARRFRR KRTFWDSGPR IGGSAVTGSS DITHRFFPSS
     SATPLVAFPS RRDMNFCRHL LLAAVFALLL AVCASAASRG AGSFDPSRVV QLSWRPRAFL
     HKGFLSDAEC DHLIALAKDK LEKSMVADNE SGKSVQSEVR TSSGMFLERK QDEVVTRIEE
     RISAWTFLPP ENGESIQILH YQNGEKYEPH YDYFHDKKNQ ALGGHRIATV LMYLSNVEKG
     GETIFPNAEG KLLQPKDNTW SDCARNGYAV KPVKGDALLF FSLHPDATTD SDSLHGSCPV
     IEGQKWSATK WIHVRSFDLP VKQPGSSDGC EDDNILCPQW AAVGECAKNP NYMVGTKEAP
     GFCRKSCKVC AE
//
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