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   27-MAR-2024, entry version 162.
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; 112.
DR   DIP; DIP-5409N; -.
DR   IntAct; P40085; 2.
DR   MINT; P40085; -.
DR   STRING; 4932.YER140W; -.
DR   GlyCosmos; P40085; 1 site, No reported glycans.
DR   GlyGen; P40085; 1 site.
DR   iPTMnet; P40085; -.
DR   PaxDb; 4932-YER140W; -.
DR   PeptideAtlas; P40085; -.
DR   EnsemblFungi; YER140W_mRNA; YER140W; YER140W.
DR   GeneID; 856883; -.
DR   KEGG; sce:YER140W; -.
DR   AGR; SGD:S000000942; -.
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   OrthoDB; 1215898at2759; -.
DR   BioCyc; YEAST:G3O-30301-MONOMER; -.
DR   BioGRID-ORCS; 856883; 0 hits in 10 CRISPR screens.
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:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; HGI:SGD.
DR   InterPro; IPR008010; Tatp1.
DR   PANTHER; PTHR13317:SF4; TRANSMEMBRANE ANTERIOR POSTERIOR TRANSFORMATION PROTEIN 1 HOMOLOG; 1.
DR   PANTHER; PTHR13317; UNCHARACTERIZED; 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
//