PTR2_YEAST
ID PTR2_YEAST Reviewed; 601 AA.
AC P32901; D6VXF3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Peptide transporter PTR2;
DE AltName: Full=Peptide permease PTR2;
GN Name=PTR2; OrderedLocusNames=YKR093W; ORFNames=YKR413;
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].
RX PubMed=8264579; DOI=10.1128/mcb.14.1.104-115.1994;
RA Perry J.R., Basrai M.A., Steiner H.-Y., Naider F., Becker J.M.;
RT "Isolation and characterization of a Saccharomyces cerevisiae peptide
RT transport gene.";
RL Mol. Cell. Biol. 14:104-115(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154186; DOI=10.1002/yea.320091209;
RA Bou G., Esteban P.F., Baladron V., Gonzalez G.A., Cantalejo J.G.,
RA Remacha M.A., Jimenez A., del Rey F., Ballesta J.P.G., Revuelta J.L.;
RT "The complete sequence of a 15,820 bp segment of Saccharomyces cerevisiae
RT chromosome XI contains the UBI2 and MPL1 genes and three new open reading
RT frames.";
RL Yeast 9:1349-1354(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-37; SER-39; SER-45 AND
RP SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-594, 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: Uptake of small peptides.
CC -!- INTERACTION:
CC P32901; Q04182: PDR15; NbExp=2; IntAct=EBI-20799497, EBI-13072;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; L11994; AAC37368.1; -; Unassigned_DNA.
DR EMBL; X73541; CAA51947.1; -; Genomic_DNA.
DR EMBL; Z28318; CAA82172.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09243.1; -; Genomic_DNA.
DR PIR; S38171; S38171.
DR RefSeq; NP_013019.1; NM_001179883.1.
DR AlphaFoldDB; P32901; -.
DR SMR; P32901; -.
DR BioGRID; 34224; 122.
DR DIP; DIP-5311N; -.
DR IntAct; P32901; 3.
DR MINT; P32901; -.
DR STRING; 4932.YKR093W; -.
DR TCDB; 2.A.17.2.2; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR CarbonylDB; P32901; -.
DR iPTMnet; P32901; -.
DR MaxQB; P32901; -.
DR PaxDb; P32901; -.
DR PRIDE; P32901; -.
DR DNASU; 853968; -.
DR EnsemblFungi; YKR093W_mRNA; YKR093W; YKR093W.
DR GeneID; 853968; -.
DR KEGG; sce:YKR093W; -.
DR SGD; S000001801; PTR2.
DR VEuPathDB; FungiDB:YKR093W; -.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_004790_4_2_1; -.
DR InParanoid; P32901; -.
DR OMA; QMMGVWF; -.
DR BioCyc; YEAST:G3O-32056-MON; -.
DR Reactome; R-SCE-427975; Proton/oligopeptide cotransporters.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P32901; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32901; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:SGD.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IMP:SGD.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IDA:SGD.
DR GO; GO:0042938; P:dipeptide transport; IDA:SGD.
DR GO; GO:0015833; P:peptide transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042939; P:tripeptide transport; IDA:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Peptide transport; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..601
FT /note="Peptide transporter PTR2"
FT /id="PRO_0000064317"
FT TOPO_DOM 1..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..412
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..554
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 39
FT /note="S -> T (in Ref. 1; AAC37368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 68044 MW; 2BD50723B1A3B310 CRC64;
MLNHPSQGSD DAQDEKQGDF PVIEEEKTQA VTLKDSYVSD DVANSTERYN LSPSPEDEDF
EGPTEEEMQT LRHVGGKIPM RCWLIAIVEL SERFSYYGLS APFQNYMEYG PNDSPKGVLS
LNSQGATGLS YFFQFWCYVT PVFGGYVADT FWGKYNTICC GTAIYIAGIF ILFITSIPSV
GNRDSAIGGF IAAIILIGIA TGMIKANLSV LIADQLPKRK PSIKVLKSGE RVIVDSNITL
QNVFMFFYFM INVGSLSLMA TTELEYHKGF WAAYLLPFCF FWIAVVTLIF GKKQYIQRPI
GDKVIAKSFK VCWILTKNKF DFNAAKPSVH PEKNYPWNDK FVDEIKRALA ACKVFIFYPI
YWTQYGTMIS SFITQASMME LHGIPNDFLQ AFDSIALIIF IPIFEKFVYP FIRRYTPLKP
ITKIFFGFMF GSFAMTWAAV LQSFVYKAGP WYNEPLGHNT PNHVHVCWQI PAYVLISFSE
IFASITGLEY AYSKAPASMK SFIMSIFLLT NAFGSAIGCA LSPVTVDPKF TWLFTGLAVA
CFISGCLFWL CFRKYNDTEE EMNAMDYEEE DEFDLNPISA PKANDIEILE PMESLRSTTK
Y
