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Database: UniProt
Entry: A0A1D6GFB9_MAIZE
LinkDB: A0A1D6GFB9_MAIZE
Original site: A0A1D6GFB9_MAIZE 
ID   A0A1D6GFB9_MAIZE        Unreviewed;       358 AA.
AC   A0A1D6GFB9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN   ORFNames=ZEAMMB73_Zm00001d013053 {ECO:0000313|EMBL:AQK62266.1};
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:AQK62266.1};
RN   [1] {ECO:0000313|EMBL:AQK62266.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK62266.1};
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; CM000781; AQK62266.1; -; Genomic_DNA.
DR   EMBL; CM000781; AQK62268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6GFB9; -.
DR   SMR; A0A1D6GFB9; -.
DR   STRING; 4577.A0A1D6GFB9; -.
DR   InParanoid; A0A1D6GFB9; -.
DR   ExpressionAtlas; A0A1D6GFB9; 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:SF222; PROCOLLAGEN-PROLINE 4-DIOXYGENASE; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF01549; ShK; 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 {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..358
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010804419"
FT   DOMAIN          179..301
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          316..356
FT                   /note="ShKT"
FT                   /evidence="ECO:0000259|PROSITE:PS51670"
SQ   SEQUENCE   358 AA;  38926 MW;  098ADE70EA41FAE2 CRC64;
     MAPPLALLLL AAIVLSRAVS HAHGGGGGFY DPASVTQLSS RPRAFLYSGF LSDTECDHLV
     SLVGWVGVGF ANRPFCSAAA RVVAMIRGAL TYGAVSILLS VGFQAKGSME KSMVADNDSG
     KSVASQARTS SGTFLAKREL LMWGTDIYLF MLSPPQPKDE IVSAIEKRVA AWTFLPEENA
     ESLQVLRYET GQKYDAHFDY FHDRNNLKLG GQRVATVLMY LTDVNKGGET VFPNAEGSHL
     QYKDETWSEC SRSGLAVKPK KGDALLFFNL HVNATADTGS LHGSCPVIEG EKWSATKWIH
     VRSFDNPPDV RTDAPCSDDK ELCPRWAAIG ECHRNPTYMV GTKDTLGFCR KSCGICDA
//
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