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Database: UniProt
Entry: A0A4P1RCD6_LUPAN
LinkDB: A0A4P1RCD6_LUPAN
Original site: A0A4P1RCD6_LUPAN 
ID   A0A4P1RCD6_LUPAN        Unreviewed;       309 AA.
AC   A0A4P1RCD6;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN   ORFNames=TanjilG_20138 {ECO:0000313|EMBL:OIW08037.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW08037.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIW08037.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIW08037.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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; CM007367; OIW08037.1; -; Genomic_DNA.
DR   RefSeq; XP_019449668.1; XM_019594123.1.
DR   AlphaFoldDB; A0A4P1RCD6; -.
DR   STRING; 3871.A0A4P1RCD6; -.
DR   GeneID; 109352235; -.
DR   OrthoDB; 5488227at2759; -.
DR   Proteomes; UP000188354; Chromosome LG07.
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; 1.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10869:SF102; PROLYL 4-HYDROXYLASE 12-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SMART; SM00254; ShKT; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188354};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..309
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020023627"
FT   DOMAIN          269..309
FT                   /note="ShKT"
FT                   /evidence="ECO:0000259|PROSITE:PS51670"
SQ   SEQUENCE   309 AA;  34738 MW;  8C7877A9A3363B67 CRC64;
     MVMASVSLLL TLSLIASSLH TSFSDSRKEL RNKDLLKQEN AFKQQLEHKV YPNRIDPSRV
     VQISWQPRVF LYKDFISDKE CDYLISLAHS VKEKSSGNED VTANGRLTSE ISLDVEDDIV
     ARIEERISVW TFLPKENSKP LQVMHYGVEQ NGQNLDYFSN KTKLELSEPL MATVVLYLSN
     ATQGGQILFP ESQSKSSSWS DCGKSSEILQ PVKGNAILFF SLHLNTAPDK NSFHARCPIL
     KGDMWSAIKF FSVRSISGRN VSTISYDDCT DEDDQCPAWA ATGECQRNPV YMVGSPDYYG
     TCRKSCNAC
//
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