EMC5_YEAST
ID EMC5_YEAST Reviewed; 141 AA.
AC P40540; D6VVQ3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ER membrane protein complex subunit 5;
DE AltName: Full=Killer toxin-resistance protein 27;
GN Name=EMC5; Synonyms=KRE27; OrderedLocusNames=YIL027C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [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 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 -!- INTERACTION:
CC P40540; P14359: SNA3; NbExp=3; IntAct=EBI-24977, EBI-26122;
CC P40540; P80967: TOM5; NbExp=2; IntAct=EBI-24977, EBI-12501;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the membrane magnesium transporter (TC 1.A.67)
CC family. {ECO:0000305}.
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DR EMBL; Z46881; CAA86965.1; -; Genomic_DNA.
DR EMBL; AY557848; AAS56174.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08519.1; -; Genomic_DNA.
DR PIR; S49955; S49955.
DR RefSeq; NP_012237.1; NM_001179377.1.
DR PDB; 6WB9; EM; 3.00 A; 5=1-141.
DR PDB; 7KRA; EM; 3.20 A; E=1-141.
DR PDB; 7KTX; EM; 4.30 A; E=1-141.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; P40540; -.
DR SMR; P40540; -.
DR BioGRID; 34962; 197.
DR ComplexPortal; CPX-307; Endoplasmic Reticulum Membrane Complex.
DR DIP; DIP-4937N; -.
DR IntAct; P40540; 38.
DR MINT; P40540; -.
DR STRING; 4932.YIL027C; -.
DR TCDB; 1.A.67.1.7; the membrane mg(2+) transporter (mmgt) family.
DR TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR MaxQB; P40540; -.
DR PaxDb; P40540; -.
DR PRIDE; P40540; -.
DR EnsemblFungi; YIL027C_mRNA; YIL027C; YIL027C.
DR GeneID; 854785; -.
DR KEGG; sce:YIL027C; -.
DR SGD; S000001289; EMC5.
DR VEuPathDB; FungiDB:YIL027C; -.
DR eggNOG; ENOG502S8V0; Eukaryota.
DR HOGENOM; CLU_132206_1_0_1; -.
DR InParanoid; P40540; -.
DR OMA; KISTHYH; -.
DR BioCyc; YEAST:G3O-31301-MON; -.
DR PRO; PR:P40540; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40540; 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; IDA:UniProtKB.
DR InterPro; IPR018937; MMgT.
DR Pfam; PF10270; MMgT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..141
FT /note="ER membrane protein complex subunit 5"
FT /id="PRO_0000202998"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..48
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 3..30
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 47..65
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:6WB9"
SQ SEQUENCE 141 AA; 15907 MW; 6DBEEEE7722203B0 CRC64;
MSFVSKLLYT VSALVLFHSG FSSYEFHHLL KLNSLNNAQG AISKLPKDIM YETYAGLILF
VLAVFTSFEK LQYLPIESND GKIISQGNYL KEIALNKATN VDNLIGSNPN GEIIFTPSFV
DVHMKRKICR EWASNTVKKE K
