ID   LYP1_YEAST              Reviewed;         611 AA.
AC   P32487; D6W0S6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   04-NOV-2026, entry version 199.
DE   RecName: Full=Lysine-specific permease;
GN   Name=LYP1; OrderedLocusNames=YNL268W; ORFNames=N0790;
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 28383 / FL100 / VTT C-80102;
RX   PubMed=8368011; DOI=10.1002/yea.320090711;
RA   Sychrova H., Chevallier M.R.;
RT   "Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding
RT   for a lysine-specific permease.";
RL   Yeast 9:771-782(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8740425;
RX   DOI=10.1002/(sici)1097-0061(199604)12:5%3c505::aid-yea932%3e3.0.co;2-f;
RA   Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT   "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT   from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL   Yeast 12:505-514(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
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   FUNCTION.
RX   PubMed=10654085; DOI=10.1007/s002940050506;
RA   Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
RT   "Substrate specificity and gene expression of the amino-acid permeases in
RT   Saccharomyces cerevisiae.";
RL   Curr. Genet. 36:317-328(1999).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND THR-90, AND
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-75; THR-77; SER-79;
RP   SER-87 AND THR-90, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
RN   [11]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-54, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: High-affinity permease for lysine.
CC       {ECO:0000269|PubMed:10654085}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Present with 2580 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR   EMBL; X67315; CAA47729.1; -; Genomic_DNA.
DR   EMBL; X92494; CAA63230.1; -; Genomic_DNA.
DR   EMBL; Z71544; CAA96175.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10292.1; -; Genomic_DNA.
DR   PIR; S60914; S60914.
DR   RefSeq; NP_014131.1; NM_001183106.1.
DR   AlphaFoldDB; P32487; -.
DR   SMR; P32487; -.
DR   BioGRID; 35572; 44.
DR   FunCoup; P32487; 172.
DR   IntAct; P32487; 4.
DR   STRING; 4932.YNL268W; -.
DR   TCDB; 2.A.3.10.10; the amino acid-polyamine-organocation (apc) family.
DR   iPTMnet; P32487; -.
DR   PaxDb; 4932-YNL268W; -.
DR   PeptideAtlas; P32487; -.
DR   EnsemblFungi; YNL268W_mRNA; YNL268W; YNL268W.
DR   GeneID; 855453; -.
DR   KEGG; sce:YNL268W; -.
DR   AGR; SGD:S000005212; -.
DR   SGD; S000005212; LYP1.
DR   VEuPathDB; FungiDB:YNL268W; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   HOGENOM; CLU_007946_12_1_1; -.
DR   InParanoid; P32487; -.
DR   OMA; AAFWVFI; -.
DR   OrthoDB; 3900342at2759; -.
DR   BioCyc; YEAST:G3O-33262-MONOMER; -.
DR   BioGRID-ORCS; 855453; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P32487; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P32487; protein.
DR   GO; GO:0032126; C:eisosome; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IGI:SGD.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015802; P:basic amino acid transport; IDA:SGD.
DR   FunFam; 1.20.1740.10:FF:000006; General amino acid permease; 1.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR004840; Amino_acid_permease_CS.
DR   InterPro; IPR004762; Amino_acid_permease_fungi.
DR   InterPro; IPR050524; APC_YAT.
DR   NCBIfam; TIGR00913; 2A0310; 1.
DR   PANTHER; PTHR43341; AMINO ACID PERMEASE; 1.
DR   PANTHER; PTHR43341:SF19; LYSINE-SPECIFIC PERMEASE; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Isopeptide bond; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..611
FT                   /note="Lysine-specific permease"
FT                   /id="PRO_0000054156"
FT   TOPO_DOM        1..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..223
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..344
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        366..398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        419..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        465..473
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        495..513
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        533..547
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        548..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        567..611
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         77
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         90
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CROSSLNK        54
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        90
FT                   /note="T -> P (in Ref. 1; CAA47729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="N -> D (in Ref. 1; CAA47729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        561
FT                   /note="V -> M (in Ref. 1; CAA47729)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   611 AA;  68090 MW;  4E7AF6F7F5F1461B CRC64;
     MGRFSNIITS NKWDEKQNNI GEQSMQELPE DQIEHEMEAI DPSNKTTPYS IDEKQYNTKK
     KHGSLQGGAI ADVNSITNSL TRLQVVSHET DINEDEEEAH YEDKHVKRAL KQRHIGMIAL
     GGTIGTGLFV GISTPLSNAG PVGSLIAYIF MGTIVYFVTQ SLGEMATFIP VTSSITVFSK
     RFLSPAFGVS NGYMYWFNWA ITYAVEVSVI GQVIEYWTDK VPLAAWIAIF WVIITLMNFF
     PVKVYGEFEF WVASVKVLAI MGYLIYALII VCGGSHQGPI GFRYWRNPGA WGPGIISSDK
     SEGRFLGWVS SLINAAFTYQ GTELVGITAG EAANPRKTVP RAINKVVFRI VLFYIMSLFF
     IGLLVPYNDS RLSASSAVIA SSPFVISIQN AGTYALPDIF NAVVLITVVS AANSNVYVGS
     RVLYSLARTG NAPKQFGYVT RQGVPYLGVV CTAALGLLAF LVVNNNANTA FNWLINISTL
     AGLCAWLFIS LAHIRFMQAL KHRGISRDDL PFKAKLMPYG AYYAAFFVTV IIFIQGFQAF
     CPFKVSEFFT SYISLILLAV VFIGCQIYYK CRFIWKLEDI DIDSDRREIE AIIWEDDEPK
     NLWEKFWAAV A
//