EMC4_YEAST
ID EMC4_YEAST Reviewed; 190 AA.
AC P53073; D6VVA3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ER membrane protein complex subunit 4;
GN Name=EMC4; OrderedLocusNames=YGL231C;
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=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 [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 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 [4]
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 [5]
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 [6]
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 [7]
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:Q5J8M3, 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1320 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EMC4 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z72753; CAA96949.1; -; Genomic_DNA.
DR EMBL; AY558267; AAS56593.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07887.1; -; Genomic_DNA.
DR PIR; S64253; S64253.
DR RefSeq; NP_011283.1; NM_001181097.1.
DR PDB; 6WB9; EM; 3.00 A; 4=1-190.
DR PDB; 7KRA; EM; 3.20 A; D=1-190.
DR PDB; 7KTX; EM; 4.30 A; D=1-190.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; P53073; -.
DR SMR; P53073; -.
DR BioGRID; 33008; 112.
DR ComplexPortal; CPX-307; Endoplasmic Reticulum Membrane Complex.
DR DIP; DIP-7920N; -.
DR IntAct; P53073; 6.
DR STRING; 4932.YGL231C; -.
DR TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR iPTMnet; P53073; -.
DR MaxQB; P53073; -.
DR PaxDb; P53073; -.
DR PRIDE; P53073; -.
DR EnsemblFungi; YGL231C_mRNA; YGL231C; YGL231C.
DR GeneID; 852620; -.
DR KEGG; sce:YGL231C; -.
DR SGD; S000003200; EMC4.
DR VEuPathDB; FungiDB:YGL231C; -.
DR eggNOG; KOG3318; Eukaryota.
DR GeneTree; ENSGT00390000006970; -.
DR HOGENOM; CLU_098404_1_3_1; -.
DR InParanoid; P53073; -.
DR OMA; QQTFKVI; -.
DR BioCyc; YEAST:G3O-30705-MON; -.
DR PRO; PR:P53073; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53073; protein.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; 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 InterPro; IPR009445; TMEM85/Emc4.
DR PANTHER; PTHR19315; PTHR19315; 1.
DR Pfam; PF06417; DUF1077; 1.
DR PIRSF; PIRSF017207; UCP017207_TM-p85; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..190
FT /note="ER membrane protein complex subunit 4"
FT /id="PRO_0000202711"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 25..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 76..83
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 137..162
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:7KRA"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6WB9"
SQ SEQUENCE 190 AA; 21460 MW; 062AE1EAB05360EE CRC64;
MSEQEPYEWA KHLLDTKYIE KYNIQNSNTL PSPPGFEGNS SKGNVTRKQQ DATSQTTSLA
QKNQITVLQV QKAWQIALQP AKSIPMNIFM SYMSGTSLQI IPIMTALMLL SGPIKAIFST
RSAFKPVLGN KATQSQVQTA MFMYIVFQGV LMYIGYRKLN SMGLIPNAKG DWLPWERIAH
YNNGLQWFSD
