PGT1_SCHPO
ID PGT1_SCHPO Reviewed; 851 AA.
AC O14031;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Glutathione transporter 1;
GN Name=pgt1; ORFNames=SPAC29B12.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB16254.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INDUCTION.
RX PubMed=12529438; DOI=10.1091/mbc.e02-08-0499;
RA Chen D., Toone W.M., Mata J., Lyne R., Burns G., Kivinen K., Brazma A.,
RA Jones N., Baehler J.;
RT "Global transcriptional responses of fission yeast to environmental
RT stress.";
RL Mol. Biol. Cell 14:214-229(2003).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18662319; DOI=10.1111/j.1567-1364.2008.00423.x;
RA Thakur A., Kaur J., Bachhawat A.K.;
RT "Pgt1, a glutathione transporter from the fission yeast Schizosaccharomyces
RT pombe.";
RL FEMS Yeast Res. 8:916-929(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: High-affinity glutathione transporter which plays a role in
CC scavenging glutathione from the extracellular environment for the
CC maintenance of sulfur homeostasis. {ECO:0000269|PubMed:18662319}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for glutathione {ECO:0000269|PubMed:18662319};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Expression is increased by cadmium ans repressed by
CC cysteine. {ECO:0000269|PubMed:12529438, ECO:0000269|PubMed:18662319}.
CC -!- SIMILARITY: Belongs to the oligopeptide OPT transporter family.
CC {ECO:0000255}.
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DR EMBL; CU329670; CAB16254.1; -; Genomic_DNA.
DR PIR; T38497; T38497.
DR RefSeq; NP_594987.1; NM_001020418.2.
DR AlphaFoldDB; O14031; -.
DR BioGRID; 278559; 31.
DR STRING; 4896.SPAC29B12.10c.1; -.
DR TCDB; 2.A.67.1.5; the oligopeptide transporter (opt) family.
DR iPTMnet; O14031; -.
DR MaxQB; O14031; -.
DR PaxDb; O14031; -.
DR PRIDE; O14031; -.
DR EnsemblFungi; SPAC29B12.10c.1; SPAC29B12.10c.1:pep; SPAC29B12.10c.
DR GeneID; 2542082; -.
DR KEGG; spo:SPAC29B12.10c; -.
DR PomBase; SPAC29B12.10c; pgt1.
DR VEuPathDB; FungiDB:SPAC29B12.10c; -.
DR eggNOG; KOG2262; Eukaryota.
DR HOGENOM; CLU_004965_1_1_1; -.
DR InParanoid; O14031; -.
DR OMA; RWIVYPA; -.
DR PhylomeDB; O14031; -.
DR PRO; PR:O14031; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IDA:PomBase.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0098709; P:glutathione import across plasma membrane; IDA:PomBase.
DR GO; GO:0034775; P:glutathione transmembrane transport; IDA:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004648; Oligpept_transpt.
DR InterPro; IPR004813; OPT.
DR PANTHER; PTHR22601; PTHR22601; 1.
DR Pfam; PF03169; OPT; 1.
DR TIGRFAMs; TIGR00727; ISP4_OPT; 1.
DR TIGRFAMs; TIGR00728; OPT_sfam; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Peptide transport; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..851
FT /note="Glutathione transporter 1"
FT /id="PRO_0000315922"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 757..777
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..134
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 851 AA; 96302 MW; EF3F886170FD8401 CRC64;
MTARNSASIP TSIRKTSENE VSGDETPAGV GNLSTKTASK TSLTFRQSSS DESTSSYSGN
HHNINIQHHP NRPFRTNSSS FSPNDYSISE SPSKSKKDGV HVSAVQLDNE TDSEVESEVE
ELERELEAIE DSVYPEVRAA VNPTDDVNLP VNTWRTWVLT TIFVIVFAAV NQFFSLRYPA
LSISFIVAQL ILFPLGKLLN LLPNWKIGYG RFSFYLNSSP FNVKEHAAIT IAVSLTSSTA
YATNILSAQT SFYKQNLSWG YKILIVLTSQ MLGYGFAGLT RRWIVYPAAM IWPQTLVSTV
LFRTLHGNSG NDIGVLKNNR ISANGWTISR YRFFAYVMIG SFVFYWFPGF IFKGLSYFTV
LCWIWPKNRV VNQLFGYNSG LGILPLTFDW QQVVYNSNPL ASPWWVICNT FGSVVLIFWI
VVPILYYKGV WFSNYLPMLS SSTFDHTGVS YNSSRVLNSD YSFNHTKYES YSPLYMPMSY
SMSTALNFAA VTAIFTHCAL YNGKDIWQRL WKESGKDECI HRKLMRNYKE APQWWYATLF
IVVFGLTIFT VRYYDTQCPV WALIVALLIF IVNFIPQGVL EGITNQHVGL NIITELIGGY
ILPGKPLANL MIKLYGFIPM RQGLEFSRDL KLAQYMKIPP RILFFVQLFA TILGGITQVA
VQEWMNYHIP GICTTSQSNG FTCPNGRSIY NASLIWGAIG PAKMFSKGKP YYPLIFFFLI
GAVAPFITWG LRKRFPKSWI GKLNAPVLFT GPGNIPPATG INYSSWAIVG FIFNYVIRKR
AIHWWRKYNY VLAAAMDSGV AVAGVVIFLC VSYPGGKITW WGNTVYTKTY DWKSVPYRSL
GPNETFGYTN W
