ID   OPT2_YEAST              Reviewed;         877 AA.
AC   Q06593; D6W4J4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Oligopeptide transporter 2;
GN   Name=OPT2; OrderedLocusNames=YPR194C; ORFNames=P9677.13;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
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   [3]
RP   FUNCTION.
RX   PubMed=9643541; DOI=10.1046/j.1365-2958.1998.00827.x;
RA   Lubkowitz M.A., Barnes D., Breslav M., Burchfield A., Naider F.,
RA   Becker J.M.;
RT   "Schizosaccharomyces pombe isp4 encodes a transporter representing a novel
RT   family of oligopeptide transporters.";
RL   Mol. Microbiol. 28:729-741(1998).
RN   [4]
RP   FUNCTION.
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   [5]
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).
CC   -!- FUNCTION: Transports tetra- and pentapeptides. Does not transport
CC       glutathione. {ECO:0000269|PubMed:10788431, ECO:0000269|PubMed:9643541}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the oligopeptide OPT transporter family.
CC       {ECO:0000305}.
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DR   EMBL; U25841; AAB64623.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11610.1; -; Genomic_DNA.
DR   PIR; S58824; S58824.
DR   RefSeq; NP_015520.1; NM_001184291.1.
DR   AlphaFoldDB; Q06593; -.
DR   BioGRID; 36366; 108.
DR   DIP; DIP-5482N; -.
DR   IntAct; Q06593; 2.
DR   STRING; 4932.YPR194C; -.
DR   TCDB; 2.A.67.1.4; the oligopeptide transporter (opt) family.
DR   GlyCosmos; Q06593; 2 sites, No reported glycans.
DR   GlyGen; Q06593; 2 sites.
DR   PaxDb; 4932-YPR194C; -.
DR   PeptideAtlas; Q06593; -.
DR   EnsemblFungi; YPR194C_mRNA; YPR194C; YPR194C.
DR   GeneID; 856324; -.
DR   KEGG; sce:YPR194C; -.
DR   AGR; SGD:S000006398; -.
DR   SGD; S000006398; OPT2.
DR   VEuPathDB; FungiDB:YPR194C; -.
DR   eggNOG; KOG2262; Eukaryota.
DR   GeneTree; ENSGT00940000176656; -.
DR   HOGENOM; CLU_004965_1_0_1; -.
DR   InParanoid; Q06593; -.
DR   OMA; WTITIRG; -.
DR   OrthoDB; 2782392at2759; -.
DR   BioCyc; YEAST:G3O-34316-MONOMER; -.
DR   BioGRID-ORCS; 856324; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q06593; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06593; Protein.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0000138; C:Golgi trans cisterna; IDA:SGD.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0045454; P:cell redox homeostasis; IMP:SGD.
DR   GO; GO:0006857; P:oligopeptide transport; IDA:SGD.
DR   GO; GO:0051515; P:positive regulation of monopolar cell growth; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0061091; P:regulation of phospholipid translocation; IGI:SGD.
DR   GO; GO:0044088; P:regulation of vacuole organization; IGI:SGD.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR   InterPro; IPR004648; Oligpept_transpt.
DR   InterPro; IPR004813; OPT.
DR   NCBIfam; TIGR00727; ISP4_OPT; 1.
DR   NCBIfam; TIGR00728; OPT_sfam; 1.
DR   PANTHER; PTHR22601; ISP4 LIKE PROTEIN; 1.
DR   PANTHER; PTHR22601:SF9; OLIGOPEPTIDE TRANSPORTER 2; 1.
DR   Pfam; PF03169; OPT; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Peptide transport; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..877
FT                   /note="Oligopeptide transporter 2"
FT                   /id="PRO_0000262733"
FT   TOPO_DOM        1..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..272
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..374
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        426..480
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        502..553
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        575..582
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        604..614
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        615..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        636..671
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        672..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        693..730
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        731..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        752..766
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        767..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        790..811
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        812..832
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        833..877
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        860
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   877 AA;  101261 MW;  3524D342E7EE4B50 CRC64;
     MSETVKDKVI IDEKVSTKGT VDYAEGAEYS ERLSNHSSDF SQWYTDEQIL HFMKKLGYEN
     RTLYDIPEDV AYILKKMPEL TLEDSFKILK DSIIYFKDDE NIPHDQYEEW KRLVDLEDLD
     SKEGIDEYDS FDIRAFASAI KFHSPYQEVR AVVDPEDDPT IPVETFRAYF LAIIWSVIGS
     GFNEFFSHRV VSISLNTPII QMFLYICGKA WAKTIPCWTI TIRGRKYGIN IDKPWTQKEQ
     MFSTLLYAIC QGAFYTHYNI LTQKLFYHSA FSFGYQFLLS LSVQFIGFGF AGILRKFVVY
     PARALWPTVM PTIAINKALL GKEKHESGMS RYKFFFLTFF IMFIYNWFPT YIINILNTFN
     WMTWIKPSNI NLANITGGVT GLGINPISSF DWNVISFNSP LVYPFWSYLT QYLGCILAAL
     IVIAVYYSNY MSCQYLPIFT NSLYTNTGHS FKVTEVLDSD NKLDVKKYQS YSPPYYSAGN
     LVSYGAFICA YPLMITWSFI VHSKLLFNAF KDWALNLWAM RKLKSWVTMF KSDYRALDDY
     DDPHSNAMKN YKEVPDWWYF AILIGSLVVG IAVVEHYPTN TPVWGLFVCL GFNFVFLIPT
     TILQATTGYS FGLNLLIEMV MGYALPGNPI AIMILKAFGY NIDGQADNYV SNLKIAHYCK
     IPPMALFRGQ CVIVFIQIFV NLGVLNWQIS NIKDFCTPHQ NAKFTCPDAV TYYNASVVWG
     AIGPKRIFNY IYPIFKWCWL IGACIGIFFG VWKRWGKFYP RYFDPMLFVG GMLNMSPPYN
     LMYYTSGMIV SYISQYYMKR HHLNLWEKYN YVLSAGFSTG LVLSAIIIFF AVQYKDTAFN
     WWGNTVPYAG ADGVGYPLKN ITDTANGYFG YAPGHYP
//