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 27-MAR-2024, entry version 190.
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<505::aid-yea932>3.0.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;
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; 42.
DR IntAct; P32487; 4.
DR MINT; P32487; -.
DR STRING; 4932.YNL268W; -.
DR TCDB; 2.A.3.10.10; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P32487; -.
DR MaxQB; 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; LFKALWY; -.
DR OrthoDB; 1366269at2759; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015802; P:basic amino acid transport; IDA:SGD.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
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
//
