YNL5_YEAST
ID YNL5_YEAST Reviewed; 644 AA.
AC P53925; B0KZS0; D6W167; Q6B2V3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Uncharacterized vacuolar membrane protein YNL115C;
GN OrderedLocusNames=YNL115C; ORFNames=N1929;
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=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-644.
RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270,
RC YJM 320, YJM 326, YJM 339, YJM 627, and YJM230;
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP 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-22; SER-56; SER-63 AND
RP SER-244, 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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
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DR EMBL; Z69382; CAA93392.1; -; Genomic_DNA.
DR EMBL; Z71391; CAA95995.1; -; Genomic_DNA.
DR EMBL; AY692627; AAT92646.1; -; Genomic_DNA.
DR EMBL; EF125216; ABN58542.1; -; Genomic_DNA.
DR EMBL; EF125217; ABN58551.1; -; Genomic_DNA.
DR EMBL; EF125218; ABN58560.1; -; Genomic_DNA.
DR EMBL; EF125219; ABN58569.1; -; Genomic_DNA.
DR EMBL; EF125220; ABN58577.1; -; Genomic_DNA.
DR EMBL; EF125221; ABN58587.1; -; Genomic_DNA.
DR EMBL; EF125222; ABN58596.1; -; Genomic_DNA.
DR EMBL; EF125223; ABN58605.1; -; Genomic_DNA.
DR EMBL; EF125224; ABN58614.1; -; Genomic_DNA.
DR EMBL; EF125225; ABN58623.1; -; Genomic_DNA.
DR EMBL; EF125226; ABN58632.1; -; Genomic_DNA.
DR EMBL; EF125228; ABN58650.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10433.1; -; Genomic_DNA.
DR PIR; S63056; S63056.
DR RefSeq; NP_014284.1; NM_001182953.1.
DR AlphaFoldDB; P53925; -.
DR SMR; P53925; -.
DR BioGRID; 35711; 83.
DR IntAct; P53925; 1.
DR STRING; 4932.YNL115C; -.
DR ESTHER; yeast-ynl5; 6_AlphaBeta_hydrolase.
DR iPTMnet; P53925; -.
DR MaxQB; P53925; -.
DR PaxDb; P53925; -.
DR PRIDE; P53925; -.
DR EnsemblFungi; YNL115C_mRNA; YNL115C; YNL115C.
DR GeneID; 855608; -.
DR KEGG; sce:YNL115C; -.
DR SGD; S000005059; YNL115C.
DR VEuPathDB; FungiDB:YNL115C; -.
DR eggNOG; ENOG502QQW9; Eukaryota.
DR HOGENOM; CLU_028296_0_0_1; -.
DR InParanoid; P53925; -.
DR OMA; RPGYAFS; -.
DR BioCyc; YEAST:G3O-33138-MON; -.
DR PRO; PR:P53925; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53925; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR019431; DUF2417.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF10329; DUF2417; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..644
FT /note="Uncharacterized vacuolar membrane protein YNL115C"
FT /id="PRO_0000203433"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..122
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..174
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..644
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT DOMAIN 348..619
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 644
FT /note="D -> G (in Ref. 4; AAT92646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 74039 MW; 790B010CEA469FB2 CRC64;
MKANGLDNDP ARTGMERTDI DSEHPEAQPL LNNNHRTLGA GSANGPAVNE GRDIESDGFI
KDSLFQIRKG YRIFIHNSKW ILNILILINT IWLVTTLISD FFFNINILFG FSNRYASFND
LTLIFISIIA NSFNLWFNKL GLYSALDYSL NVTLCVLTLF NLALTYLIKY TRQRIGFVGT
FTYLWTSFSF FIGAILDWYL LFYNNSINEP LEERRIDDAN ISTFNENHTN STENRDRSQY
GSGSPTPTHR SQLVQNKHTL TEWVSIGFRN TIKFLILIFF ALFTLNTLLT TLDTYRLTHK
LPITVQSPSY EAFHYVDAAK TYQLHITCYG DVFDQENNTD LSENKKQPII LFEHGGYDTG
YLSATWIEEL YHLDKIQRYC LYDRPGYGLS DSPPAPISIA MVAESLRYAL IKDAKIKGPF
TTVGYDLGGL FTRVFTAKNV DIVDSMMLVE SWHEELLLKN YIQRLLPPGR GDGDDGDDGN
GNDGDGRNHD KTWLPSEIER HNEFRLWWKG IWSSLGWRLQ TSWLLAHHGS KERIYGRDMK
YQGRFLRSKF LESVTSSILS YRDVTNNAES LQNVKTSIVS SKEMVKKSAL WGDWQRDLTK
ISHKTQEWKI VEGGHEIYKY GLGKQQTQEV LLRLIGELGK LTED
