ID A0A1J7FXD2_LUPAN Unreviewed; 2008 AA.
AC A0A1J7FXD2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=TanjilG_18006 {ECO:0000313|EMBL:OIV92655.1};
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:OIV92655.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV92655.1, 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:OIV92655.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MCTP family.
CC {ECO:0000256|ARBA:ARBA00007923}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CM007378; OIV92655.1; -; Genomic_DNA.
DR STRING; 3871.A0A1J7FXD2; -.
DR EnsemblPlants; OIV92655; OIV92655; TanjilG_18006.
DR Gramene; OIV92655; OIV92655; TanjilG_18006.
DR Proteomes; UP000188354; Chromosome LG18.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd04022; C2A_MCTP_PRT_plant; 1.
DR CDD; cd08378; C2B_MCTP_PRT_plant; 1.
DR CDD; cd04019; C2C_MCTP_PRT_plant; 1.
DR CDD; cd08379; C2D_MCTP_PRT_plant; 1.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 2.60.40.150; C2 domain; 4.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR047257; C2B_MCTP_PRT_plant.
DR InterPro; IPR047258; C2C_MCTP_PRT_plant.
DR InterPro; IPR047255; C2D_MCTP_PRT_plant.
DR InterPro; IPR006598; CAP10.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR013583; MCTP_C.
DR InterPro; IPR047259; QUIRKY-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR31425:SF52; C2 CALCIUM/LIPID-BINDING PLANT PHOSPHORIBOSYLTRANSFERASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR31425; PHOSPHORIBOSYLANTHRANILATE TRANSFERASE ISOFORM 1; 1.
DR Pfam; PF00168; C2; 4.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR Pfam; PF00255; GSHPx; 1.
DR Pfam; PF08372; PRT_C; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SMART; SM00239; C2; 4.
DR SMART; SM00672; CAP10; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 4.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50004; C2; 4.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1111..1129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1195..1213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1225..1257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1339..1369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..498
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 647..767
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 811..932
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 973..1095
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1822..2008
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 2008 AA; 230125 MW; 4C89BF62B29BB528 CRC64;
MQRFIEQRSK TQFISGTLVK KGPAHVAAYT SILLLLIFFS ASTVSSLWAT LSTTTNSKRI
SIGNKTIVAS ISPNHNRKRL FQNTLNCTTT RNQTCSTLDP TTSTTFEIND DVCPEYFRWI
HEDLRAWKAT GINRDMVERA RNTAHFRESI QTRDIFTMWG IMQLVRKYKG MVPDLELMFD
CDDQPVVLAR DYDHHDDPNN ITGPPPLFRY CADRWTRDIV FPDWSFWGWA EINIRPWEHV
LKDIKESNKR INWNDREPFA YWKGNPSVAV TRQDLLKCNV SNEHDWNARL FVQAQEIGRA
ASKFIQEDLK MDYVYDYMFH LLNEYSKLLK FEPIVPEGAV ELCSEAMACK RSGLEKKFMT
ESFVSEPSIK APCSLPPPFE PNSLRIFYGN KLNFKLGVDV VSAHNLLPKD GEGSSSSFVE
LYFDGQKYRT TIKERDLNPV WNESFYFNIS DPSNLNHLTL DAYVHCHTRA TNSSSFLGKV
SLTGTSFVAY ADAVVLHYPL EKRRIFSRVR GEIGLKVYIT NDSTIKSSIP TPAVESMHTN
NPSLADTQVN AAGNTMANPL SNGKVESARH TFHHLPNPNH QHHQHHSNGF GDTHYVTKYE
ADEMVSGGPQ PMKLVHMHSV SSAQPVDYAL KETSPFLGGG RVVGGRIIHK DKTSSTYDLV
ERMYFLYVRV VKARELPAMD LTGSLDPFVV VRIGNYKGIT RHFDKNQHPE WNQVFAFSKE
RMQASILEVR IKDKDLVKDD FVGLVRFDIN EVPLRVPPDS PLAPEWYRLE DKKGEKIKGE
LMLAVWIGTQ ADEAFSDAWH SDAATPVDST PAATTVIRSK VYHAPRLWYV RVNIVEAQDL
VPTEKNRFPD VYVKAQIGNQ VLKTKTVPAR TLSPLWNEDL LFVAAEPFED HLVLSVEDRI
GSGKDEIIGR VIIPLNAVER RADDRMIHSR WFNLEKPVAV DVDQLKKEKF SSRIHLHLCL
DGGYHVLDES THYSSDLRPT AKQLWRPPIG ILELGVLKAV GLHPMKTREG RGASDTYCVA
KYGHKWIRTR TIVDNLSPKF NEQYTWEVFD QATVITVGVF DNSHIGEKGS KDLKIGKVRI
RISTLETGRI YTHSYPLLVL HPTGVKKMGE LHLAIRFSCT SFANMLYLYS KPLLPKMHYV
RPFSVMQVDM LRHQAVNIVA ARLGRAEPPL RKEVVEYMSD VDSHLWSMRR SKANFFRLMT
LFSGVFAVGK WFGDICMWRN PITTVLVHVL FLMLVCFPEL ILPTVFLYMF LIGVWNFRYR
ARYPPHMNTR LSQADAVQPD ELDEEFDTFP TSRNPDIVRM RYDRLRSVAG RIQTVVGDLA
SQGERIQALL SWRDPRATAL FITLCLVSAL VLYVTPFQAL AGLVGFYVMR HPRFRHRLPS
APINFFRRLP AKTDRTNPSF EIPTSIANDS FIPLQIEGNA TRHGKFPASN ISYTVSGRDV
NYNDKDEEIA NAVKVVEEHL QVHRSWISDK NYAACDGRGI FVYDMPSMFN KDLLGQCRDM
VPWQDFCRYF SNEGLGEPIT NLGKGWYQTH QYSLELIFHS RVLKHPCRVY NENEAKLFYV
PVYAGLDILR WHFKNVSNDV KDTLALDLVK WLERQRPWKN NQGKDHVFVL GKISWDFRRS
NESPWGSRLL ELDKMQNPIK LLIERQPWHV NDIGIPHPTY FHPQSDNDIV SWQLKIIRSN
RKNLVSFAGA ARPEAKDNIR SMLIDQCSSS YNNGKCQFLN CSSAKCNEPE SITQVFMESE
FCMQPPGDSP TRKSVFDSLI SGCIPVLFDP FTAYYQYPWH LPKDHDKYSV FIDKKEVKQM
NVNVVERLSN ISSRERENMR RFIVYELLPG LVYRDQNGEL EKFQDAFDIT INNLLERDAR
GNDVNLGDYK GKVLLIVNVA SQCGLTNSNY TELNQVYDKY KGKGLEILAF PCNQFGAQEP
GSNEEIVEFA CTRFKAEFPI FDKVDVNGDS ATPLYKFLKS SKGGLFGDSI KWNFSKFLVD
KEGNVVERYA PTTSPLSIEK DIKKLLDA
//