EMC2_YEAST
ID EMC2_YEAST Reviewed; 292 AA.
AC P47133; D6VWQ6; Q66R61;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ER membrane protein complex subunit 2 {ECO:0000305};
GN Name=EMC2; OrderedLocusNames=YJR088C; ORFNames=J1875;
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 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 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 [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 IDENTIFICATION IN EMC COMPLEX.
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 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).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=29809151; DOI=10.7554/elife.37018;
RA Shurtleff M.J., Itzhak D.N., Hussmann J.A., Schirle Oakdale N.T.,
RA Costa E.A., Jonikas M., Weibezahn J., Popova K.D., Jan C.H., Sinitcyn P.,
RA Vembar S.S., Hernandez H., Cox J., Burlingame A.L., Brodsky J.L., Frost A.,
RA Borner G.H., Weissman J.S.;
RT "The ER membrane protein complex interacts cotranslationally to enable
RT biogenesis of multipass membrane proteins.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex
CC (EMC) that enables the energy-independent insertion into endoplasmic
CC reticulum membranes of newly synthesized membrane proteins
CC (PubMed:29809151). Preferentially accommodates proteins with
CC transmembrane domains that are weakly hydrophobic or contain
CC destabilizing features such as charged and aromatic residues
CC (PubMed:29809151). Involved in the cotranslational insertion of multi-
CC pass membrane proteins in which stop-transfer membrane-anchor sequences
CC become ER membrane spanning helices (PubMed:29809151). It is also
CC required for the post-translational insertion of tail-anchored/TA
CC proteins in endoplasmic reticulum membranes. By mediating the proper
CC cotranslational insertion of N-terminal transmembrane domains in an N-
CC exo topology, with translocated N-terminus in the lumen of the ER,
CC controls the topology of multi-pass membrane proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q15006, ECO:0000269|PubMed:29809151}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC), which is
CC composed of EMC1, EMC2, EMC3, EMC4, EMC5 and EMC6.
CC {ECO:0000269|PubMed:19325107, ECO:0000269|PubMed:29809151}.
CC -!- INTERACTION:
CC P47133; P80967: TOM5; NbExp=3; IntAct=EBI-25568, EBI-12501;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15006}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15006}.
CC -!- MISCELLANEOUS: Present with 5740 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EMC2 family. {ECO:0000305}.
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DR EMBL; Z49586; CAA89615.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39311.1; -; Genomic_DNA.
DR EMBL; AY723838; AAU09755.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08872.1; -; Genomic_DNA.
DR PIR; S57107; S57107.
DR RefSeq; NP_012621.1; NM_001181745.1.
DR PDB; 6WB9; EM; 3.00 A; 2=1-292.
DR PDB; 7KRA; EM; 3.20 A; B=1-292.
DR PDB; 7KTX; EM; 4.30 A; B=1-292.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; P47133; -.
DR SMR; P47133; -.
DR BioGRID; 33842; 176.
DR ComplexPortal; CPX-307; Endoplasmic Reticulum Membrane Complex.
DR DIP; DIP-7609N; -.
DR IntAct; P47133; 9.
DR STRING; 4932.YJR088C; -.
DR TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR MaxQB; P47133; -.
DR PaxDb; P47133; -.
DR PRIDE; P47133; -.
DR EnsemblFungi; YJR088C_mRNA; YJR088C; YJR088C.
DR GeneID; 853550; -.
DR KEGG; sce:YJR088C; -.
DR SGD; S000003848; EMC2.
DR VEuPathDB; FungiDB:YJR088C; -.
DR eggNOG; KOG3060; Eukaryota.
DR GeneTree; ENSGT00390000011922; -.
DR HOGENOM; CLU_065213_1_0_1; -.
DR InParanoid; P47133; -.
DR OMA; LMEMLFY; -.
DR BioCyc; YEAST:G3O-31715-MON; -.
DR PRO; PR:P47133; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47133; protein.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:ComplexPortal.
DR GO; GO:0015914; P:phospholipid transport; IMP:ComplexPortal.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; HGI:SGD.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR039856; EMC2-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12760; PTHR12760; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW TPR repeat.
FT CHAIN 1..292
FT /note="ER membrane protein complex subunit 2"
FT /id="PRO_0000203107"
FT REPEAT 163..196
FT /note="TPR"
FT /evidence="ECO:0000255"
FT CONFLICT 20
FT /note="T -> P (in Ref. 4; AAU09755)"
FT /evidence="ECO:0000305"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 197..214
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 218..235
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:6WB9"
SQ SEQUENCE 292 AA; 33855 MW; 157A03E75FB9E72A CRC64;
MLKDLVREKL LTIMNTKAYT QFNPEQLLQL ENEMKIYMKS GDSALTEGNY FFLMEMLFYV
LVYRNQDVDA QVVYNTLRDR LGENSYKMVI MKATLLQING NDKGAIEYLE NLLNDDLEYE
TDFVTYVSIA KKLIAIKTTS KNLSQESVLK EVVALTDKFP LDAELWWYAS EIYFEMGQFE
KACYCLEQVL CITPFNYACF GRLSETLYYE ALRSKKQTKT ELLEKALKNA LRSVELSELY
LKGWALVNII SRELGRNKQN DLIKLSASKL KEISAKSNNK DKITAELILN KI
