EMC1_YEAST
ID EMC1_YEAST Reviewed; 760 AA.
AC P25574; D6VQX1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ER membrane protein complex subunit 1;
DE Flags: Precursor;
GN Name=EMC1; OrderedLocusNames=YCL045C; ORFNames=YCL315, YCL45C;
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].
RX PubMed=1523890; DOI=10.1002/yea.320080709;
RA Scherens B., Messenguy F., Gigot D., Dubois E.;
RT "The complete sequence of a 9,543 bp segment on the left arm of chromosome
RT III reveals five open reading frames including glucokinase and the protein
RT disulfide isomerase.";
RL Yeast 8:577-586(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 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 GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [8]
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 [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:Q8N766, 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 P25574; P80967: TOM5; NbExp=2; IntAct=EBI-21744, EBI-12501;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EMC1 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42370.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07440.1; -; Genomic_DNA.
DR PIR; S19374; S19374.
DR RefSeq; NP_009884.1; NM_001178690.1.
DR PDB; 6WB9; EM; 3.00 A; 1=1-760.
DR PDB; 7KRA; EM; 3.20 A; A=1-760.
DR PDB; 7KTX; EM; 4.30 A; A=1-760.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; P25574; -.
DR SMR; P25574; -.
DR BioGRID; 30939; 152.
DR ComplexPortal; CPX-307; Endoplasmic Reticulum Membrane Complex.
DR DIP; DIP-5140N; -.
DR IntAct; P25574; 6.
DR MINT; P25574; -.
DR STRING; 4932.YCL045C; -.
DR TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR MaxQB; P25574; -.
DR PaxDb; P25574; -.
DR PRIDE; P25574; -.
DR ABCD; P25574; 1 sequenced antibody.
DR EnsemblFungi; YCL045C_mRNA; YCL045C; YCL045C.
DR GeneID; 850312; -.
DR KEGG; sce:YCL045C; -.
DR SGD; S000000550; EMC1.
DR VEuPathDB; FungiDB:YCL045C; -.
DR eggNOG; KOG2103; Eukaryota.
DR GeneTree; ENSGT00390000002461; -.
DR HOGENOM; CLU_005034_3_0_1; -.
DR InParanoid; P25574; -.
DR OMA; PIPEQKL; -.
DR BioCyc; YEAST:G3O-29301-MON; -.
DR PRO; PR:P25574; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25574; 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; IPR026895; EMC1.
DR InterPro; IPR011678; EMC1_C.
DR PANTHER; PTHR21573; PTHR21573; 2.
DR Pfam; PF07774; EMC1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..760
FT /note="ER membrane protein complex subunit 1"
FT /id="PRO_0000202547"
FT TOPO_DOM 25..723
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT TURN 27..32
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 248..269
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:7KRA"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 436..444
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 500..503
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 517..523
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 539..548
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 553..564
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:7KRA"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 592..602
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 620..625
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 645..650
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 672..676
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 698..712
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 727..757
FT /evidence="ECO:0007829|PDB:6WB9"
SQ SEQUENCE 760 AA; 87181 MW; 56F2B5A7186BDF7A CRC64;
MKITCTDLVY VFILLFLNTS CVQAVFSDDA FITDWQLANL GPWEKVIPDS RDRNRVLILS
NPTETSCLVS SFNVSSGQIL FRNVLPFTID EIQLDSNDHN AMVCVNSSSN HWQKYDLHDW
FLLEEGVDNA PSTTILPQSS YLNDQVSIKN NELHILDEQS KLAEWKLELP QGFNKVEYFH
REDPLALVLN VNDTQYMGFS ANGTELIPVW QRDEWLTNVV DYAVLDVFDS RDVELNKDMK
AELDSNSLWN AYWLRLTTNW NRLINLLKEN QFSPGRVFTK LLALDAKDTT VSDLKFGFAK
ILIVLTHDGF IGGLDMVNKG QLIWKLDLEI DQGVKMFWTD KNHDELVVFS HDGHYLTIEV
TKDQPIIKSR SPLSERKTVD SVIRLNEHDH QYLIKFEDKD HLLFKLNPGK NTDVPIVANN
HSSSHIFVTE HDTNGIYGYI IENDTVKQTW KKAVNSKEKM VAYSKRETTN LNTLGITLGD
KSVLYKYLYP NLAAYLIANE EHHTITFNLI DTITGEILIT QEHKDSPDFR FPMDIVFGEY
WVVYSYFSSE PVPEQKLVVV ELYESLTPDE RLSNSSDNFS YDPLTGHINK PQFQTKQFIF
PEIIKTMSIS KTTDDITTKA IVMELENGQI TYIPKLLLNA RGKPAEEMAK DKKKEFMATP
YTPVIPINDN FIITHFRNLL PGSDSQLISI PTNLESTSII CDLGLDVFCT RITPSGQFDL
MSPTFEKGKL LITIFVLLVI TYFIRPSVSN KKLKSQWLIK
