YGO0_YEAST
ID YGO0_YEAST Reviewed; 1219 AA.
AC P53120; D6VU09;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Uncharacterized membrane protein YGL140C;
GN OrderedLocusNames=YGL140C;
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 96604 / S288c / FY1679;
RX PubMed=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1167, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1167; SER-1198 AND SER-1199,
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198 AND SER-1199, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1167; TYR-1191; SER-1198 AND
RP SER-1199, AND 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 -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X99960; CAA68222.1; -; Genomic_DNA.
DR EMBL; Z72662; CAA96852.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07970.1; -; Genomic_DNA.
DR PIR; S64154; S64154.
DR RefSeq; NP_011375.1; NM_001181005.1.
DR AlphaFoldDB; P53120; -.
DR SMR; P53120; -.
DR BioGRID; 33112; 24.
DR MINT; P53120; -.
DR STRING; 4932.YGL140C; -.
DR iPTMnet; P53120; -.
DR MaxQB; P53120; -.
DR PaxDb; P53120; -.
DR PRIDE; P53120; -.
DR EnsemblFungi; YGL140C_mRNA; YGL140C; YGL140C.
DR GeneID; 852737; -.
DR KEGG; sce:YGL140C; -.
DR SGD; S000003108; YGL140C.
DR VEuPathDB; FungiDB:YGL140C; -.
DR eggNOG; KOG4711; Eukaryota.
DR HOGENOM; CLU_007711_0_0_1; -.
DR InParanoid; P53120; -.
DR OMA; MLFFHGW; -.
DR BioCyc; YEAST:G3O-30635-MON; -.
DR PRO; PR:P53120; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53120; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR018823; ArAE_2_N.
DR InterPro; IPR023244; Brefeldin_A-sensitivity_4.
DR Pfam; PF10337; ArAE_2_N; 1.
DR PRINTS; PR02047; BREFELDNASP4.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1219
FT /note="Uncharacterized membrane protein YGL140C"
FT /id="PRO_0000202737"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..629
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..732
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..796
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 818..1219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 567..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 1191
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1219 AA; 137476 MW; 76D840C220CC9802 CRC64;
MSLKSKLTKI QKLWLYYFPC DRILAKRICK STVNTTVAFI FCLIPKITAH LGAAPAMLPM
ISVIVHPGRR VGGTIHGAIY CITGLIFGLA YAIFGRFLAQ RCLGSSWHEL TEAQQHVLHY
KRYEAGLAIL AVFEVIMLFF HGWMRSVSHY YFGIVFPLFV VVHFAFMDPL NETAGTIAKA
YSTPFYLGIA MSIFWNLVLF PEWGTTYLGN TTIDAMNELH KSIDYSINFF IAVDPHNSSQ
LYSRDPVSLG KLLKMKSLIS SKVNNCRVVL HECIYEFTYA YVSPTKLKPI ISTLENLTVF
INGLVNTCQL EFILLARHDN KLRPDDVAAL TLPKNKEISF ANAEKLLKVI DKLHPVIYSL
HRTMSECMYI AKLVLAHAFD VKVSRVHSCS MFKDGNFPTF SNNANNLPND VDIQNKINDL
KQALEECKAK FKSEMLSFDI DIMSPSDEMF LLSSFLLNFR QTADSTLVIM ESVKDILVKR
QIQEKKGWLR GKRLWFLVLT NYETFSIWLK GDRNSVTEND TLKGTFNGNT NGFAHDTVIR
RPDYEENELL SQKVSSNKNI VKDDASLDLP MTSEPKGNSS STSDTSSSPL TLTKTTTFGT
NRTSRRQGRF SFMSMLISID KFCEVSHPHF RFGFQVAIAL MLASFPMFIP KTRQWYIDYR
GTWIGFVCIL CLEPSVGGTF WVFFLRAVGV IFGAAWGYLS YVAAVNQTNP YLETVITVFG
AIPGFYYLLG TPYVKAAIIE IISIYIVMLA AILPSQDDIL TSFAKRCLAV GYGGGVALIV
QVFFFPLKAR EQLNEEISFV CGCISEMELL YATGLEGEQV ASSMSEEKYK KIEKISKSAK
EALARATAYK GLTRQEPRLK GEYTELENVF TQVIFIQKQI IERIDTISLL RKQNGSAVIE
EFNSVVYPYR RQMVGSISCL MRALQEAFIN KTPLPQFLPS ARIAHRRLIN KVRQTLRIRY
PGQISNLSDK ARKPNEGDYA DGKDEDDDDN EGLVMKMNRR GQANTTANPH EYVLKEKFLS
WNASSAASEE IIEYIEELLN LTKILVGVNE FKYGFLSRPL YEDWAAEAVT GFDNFINGKS
NPMNTRRNRT PFDGTSIISE GNESLQSTNS NESQISPDST RSYEPECPVA YEKNDNPAAL
NLLRIASHKA GQNADGLPKT FRNRAFSITS TSGQLSSLSR HSTLGNADPN YLNDDDESSD
DDLPLALKMV LSHMKEKKD
