TAPT1_YEAST
ID TAPT1_YEAST Reviewed; 556 AA.
AC P40085; D3DM47;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Endoplasmic reticulum membrane protein 65 {ECO:0000305|PubMed:23275891};
DE AltName: Full=65 kDa endoplasmic reticulum membrane protein {ECO:0000303|PubMed:23275891};
GN Name=EMP65 {ECO:0000303|PubMed:23275891};
GN OrderedLocusNames=YER140W {ECO:0000312|SGD:S000000942};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP FUNCTION.
RX PubMed=19325107; DOI=10.1126/science.1167983;
RA Jonikas M.C., Collins S.R., Denic V., Oh E., Quan E.M., Schmid V.,
RA Weibezahn J., Schwappach B., Walter P., Weissman J.S., Schuldiner M.;
RT "Comprehensive characterization of genes required for protein folding in
RT the endoplasmic reticulum.";
RL Science 323:1693-1697(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLP1.
RX PubMed=23275891; DOI=10.1534/g3.112.004614;
RA Friederichs J.M., Gardner J.M., Smoyer C.J., Whetstine C.R., Gogol M.,
RA Slaughter B.D., Jaspersen S.L.;
RT "Genetic analysis of Mps3 SUN domain mutants in Saccharomyces cerevisiae
RT reveals an interaction with the SUN-like protein Slp1.";
RL G3 (Bethesda) 2:1703-1718(2012).
CC -!- FUNCTION: May be involved in membrane protein folding.
CC {ECO:0000269|PubMed:19325107}.
CC -!- SUBUNIT: Interacts with SLP1. {ECO:0000269|PubMed:23275891}.
CC -!- INTERACTION:
CC P40085; Q12232: SLP1; NbExp=3; IntAct=EBI-22717, EBI-35990;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23275891}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:14576278}.
CC -!- SIMILARITY: Belongs to the TAPT1 family. {ECO:0000305}.
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DR EMBL; U18917; AAB64667.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07801.1; -; Genomic_DNA.
DR PIR; S50643; S50643.
DR RefSeq; NP_011067.3; NM_001179030.3.
DR AlphaFoldDB; P40085; -.
DR BioGRID; 36889; 110.
DR DIP; DIP-5409N; -.
DR IntAct; P40085; 2.
DR MINT; P40085; -.
DR STRING; 4932.YER140W; -.
DR iPTMnet; P40085; -.
DR PaxDb; P40085; -.
DR PRIDE; P40085; -.
DR EnsemblFungi; YER140W_mRNA; YER140W; YER140W.
DR GeneID; 856883; -.
DR KEGG; sce:YER140W; -.
DR SGD; S000000942; EMP65.
DR VEuPathDB; FungiDB:YER140W; -.
DR eggNOG; KOG2490; Eukaryota.
DR GeneTree; ENSGT00390000010628; -.
DR HOGENOM; CLU_003655_1_1_1; -.
DR InParanoid; P40085; -.
DR OMA; NSWKSWN; -.
DR BioCyc; YEAST:G3O-30301-MON; -.
DR PRO; PR:P40085; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40085; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; HGI:SGD.
DR InterPro; IPR008010; Tatp1.
DR PANTHER; PTHR13317; PTHR13317; 1.
DR Pfam; PF05346; DUF747; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..556
FT /note="Endoplasmic reticulum membrane protein 65"
FT /id="PRO_0000202654"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..151
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..330
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..428
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 556 AA; 64794 MW; 16B04343A0F33AAF CRC64;
MQHKDTAVAK DTAKKRLLRR NSAPSAIHII SRLDKKWSFL WNTIDRHNIV EEQDESSAAK
SEEEHEDDYE LEQLLNMIRI PMFLEKFMLF ALLTSLDCFL YYFTVLPIRL IKGYVKQFKS
YRQHYRLQQR SGHKNKIPFR YRITSREYKE RCMIFIIVIS SILLSKLDTS KLYHRIKRQS
TMKLYMLFSV LEMADKMLAS LGQSLLTVML SRKNSERILL HKCLLVSMSL TYVTIHGYVL
VYQAISLNIA VNSYSNALLT LLLSMQFAEI KSSVLKKFDK EGFFQITIAD VVERFKLTLL
LSITGLRNLQ SWSSSLSNTS INFWSPRSTL SIVINILCGP MVSVVGSEVL VDWAKHAYIT
KFNRIRPQIY DKFYYIIYKD YSTRTHKLED RLGLPLPAFV VLFIVMVRPT LFKSSEPSYL
PSLFRILFMG ASVFLLALLA KFTLDLILIK WSKRIEQRFR DQAFNTVVTE EEYVPGLLSG
GMGKVDVSTR IALHSDYNKE NRIETESVSP MRKRKTTLTA ECTPPSLNDI RRQKDSKNPR
SLENVARYKM VSKRIW
