OPT1_YEAST
ID OPT1_YEAST Reviewed; 799 AA.
AC P40897; D6VVY3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Oligopeptide transporter 1;
DE AltName: Full=High affinity glutathione transporter 1;
GN Name=OPT1; Synonyms=GSH11, HGT1; OrderedLocusNames=YJL212C;
GN ORFNames=HRD799, J0236;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7725802; DOI=10.1002/yea.320101216;
RA Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere
RT of yeast chromosome X.";
RL Yeast 10:1657-1662(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10652283; DOI=10.1074/jbc.275.5.3037;
RA Hauser M., Donhardt A.M., Barnes D., Naider F., Becker J.M.;
RT "Enkephalins are transported by a novel eukaryotic peptide uptake system.";
RL J. Biol. Chem. 275:3037-3041(2000).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10788431; DOI=10.1074/jbc.275.18.13259;
RA Bourbouloux A., Shahi P., Chakladar A., Delrot S., Bachhawat A.K.;
RT "Hgt1p, a high affinity glutathione transporter from the yeast
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:13259-13265(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND THR-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: High affinity transporter for glutathione. Also transports
CC tetra- and pentapeptides like the opioids leucine enkephalin (Tyr-Gly-
CC Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly_Phe-Met) across the
CC cell membrane. {ECO:0000269|PubMed:10652283,
CC ECO:0000269|PubMed:10788431}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53.9 uM for glutathione {ECO:0000269|PubMed:10652283,
CC ECO:0000269|PubMed:10788431};
CC KM=310 uM for leucine enkephalin {ECO:0000269|PubMed:10652283,
CC ECO:0000269|PubMed:10788431};
CC Vmax=10 nmol/min/mg enzyme for glutathione
CC {ECO:0000269|PubMed:10652283, ECO:0000269|PubMed:10788431};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:10652283,
CC ECO:0000269|PubMed:10788431};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 2870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the oligopeptide OPT transporter family.
CC {ECO:0000305}.
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DR EMBL; Z34098; CAA83999.1; -; Genomic_DNA.
DR EMBL; Z49487; CAA89509.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08599.1; -; Genomic_DNA.
DR PIR; S50773; S50773.
DR RefSeq; NP_012323.1; NM_001181645.1.
DR AlphaFoldDB; P40897; -.
DR BioGRID; 33547; 58.
DR DIP; DIP-5691N; -.
DR STRING; 4932.YJL212C; -.
DR TCDB; 2.A.67.1.3; the oligopeptide transporter (opt) family.
DR iPTMnet; P40897; -.
DR MaxQB; P40897; -.
DR PaxDb; P40897; -.
DR PRIDE; P40897; -.
DR EnsemblFungi; YJL212C_mRNA; YJL212C; YJL212C.
DR GeneID; 853218; -.
DR KEGG; sce:YJL212C; -.
DR SGD; S000003748; OPT1.
DR VEuPathDB; FungiDB:YJL212C; -.
DR eggNOG; KOG2262; Eukaryota.
DR GeneTree; ENSGT00940000176656; -.
DR HOGENOM; CLU_004965_1_1_1; -.
DR InParanoid; P40897; -.
DR OMA; RWIVYPA; -.
DR BioCyc; YEAST:G3O-31639-MON; -.
DR SABIO-RK; P40897; -.
DR PRO; PR:P40897; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40897; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; IDA:SGD.
DR GO; GO:0006857; P:oligopeptide transport; IDA:SGD.
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; Glycoprotein; Membrane; Peptide transport; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..799
FT /note="Oligopeptide transporter 1"
FT /id="PRO_0000213788"
FT TOPO_DOM 1..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..659
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..736
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..799
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 799 AA; 91616 MW; AF81676CC9B30759 CRC64;
MSTIYRESDS LESEPSPTPT TIPIQINMEE EKKDAFVKNI DEDVNNLTAT TDEEDRDPES
QKFDRHSIQE EGLVWKGDPT YLPNSPYPEV RSAVSIEDDP TIRLNHWRTW FLTTVFVVVF
AGVNQFFSLR YPSLEINFLV AQVVCYPIGR ILALLPDWKC SKVPFFDLNP GPFTKKEHAV
VTIAVALTSS TAYAMYILNA QGSFYNMKLN VGYQFLLVWT SQMIGYGAAG LTRRWVVNPA
SSIWPQTLIS VSLFDSLHSR KVEKTVANGW TMPRYRFFLI VLIGSFIWYW VPGFLFTGLS
YFNVILWGSK TRHNFIANTI FGTQSGLGAL PITFDYTQVS QAMSGSVFAT PFYVSANTYA
SVLIFFVIVL PCLYFTNTWY AKYMPVISGS TYDNTQNKYN VTKILNEDYS INLEKYKEYS
PVFVPFSYLL SYALNFAAVI AVFVHCILYH GKDIVAKFKD RKNGGTDIHM RIYSKNYKDC
PDWWYLLLQI VMIGLGFVAV CCFDTKFPAW AFVIAILISL VNFIPQGILE AMTNQHVGLN
IITELICGYM LPLRPMANLL FKLYGFIVMR QGLNLSRDLK LAMYMKVSPR LIFAVQIYAT
IISGMVNVGV QEWMMHNIDG LCTTDQPNGF TCANGRTVFN ASIIWSLPKY LFSSGRIYNP
LMWFFLIGLL FPLAVYAVQW KFPKFKFAKH IHTPVFFTGP GNIPPSTPYN YSLFFAMSFC
LNLIRKRWRA WFNKYNFVMG AGVEAGVAIS VVIIFLCVQY PGGKLSWWGN NVWKRTYDND
YKKFYTLKKG ETFGYDKWW
