EMC6_YEAST
ID EMC6_YEAST Reviewed; 108 AA.
AC Q12431; D6VXY8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ER membrane protein complex subunit 6;
GN Name=EMC6; OrderedLocusNames=YLL014W; ORFNames=L1321;
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 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046100;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT known genes, a new member of the seripauperins family and a new ABC
RT transporter homologous to the human multidrug resistance protein.";
RL Yeast 13:183-188(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
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 [6]
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 [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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BV81}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9BV81}.
CC -!- SIMILARITY: Belongs to the EMC6 family. {ECO:0000305}.
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DR EMBL; X91488; CAA62778.1; -; Genomic_DNA.
DR EMBL; X97560; CAA66163.1; -; Genomic_DNA.
DR EMBL; Z73119; CAA97459.1; -; Genomic_DNA.
DR EMBL; AY557926; AAS56252.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09304.1; -; Genomic_DNA.
DR PIR; S64756; S64756.
DR RefSeq; NP_013087.1; NM_001181834.1.
DR PDB; 6WB9; EM; 3.00 A; 6=1-108.
DR PDB; 7KRA; EM; 3.20 A; F=1-108.
DR PDB; 7KTX; EM; 4.30 A; F=1-108.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; Q12431; -.
DR SMR; Q12431; -.
DR BioGRID; 31237; 173.
DR ComplexPortal; CPX-307; Endoplasmic Reticulum Membrane Complex.
DR DIP; DIP-988N; -.
DR IntAct; Q12431; 10.
DR STRING; 4932.YLL014W; -.
DR TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR MaxQB; Q12431; -.
DR PaxDb; Q12431; -.
DR EnsemblFungi; YLL014W_mRNA; YLL014W; YLL014W.
DR GeneID; 850646; -.
DR KEGG; sce:YLL014W; -.
DR SGD; S000003937; EMC6.
DR VEuPathDB; FungiDB:YLL014W; -.
DR eggNOG; KOG4455; Eukaryota.
DR HOGENOM; CLU_110781_4_1_1; -.
DR InParanoid; Q12431; -.
DR OMA; FRELMGF; -.
DR BioCyc; YEAST:G3O-32119-MON; -.
DR PRO; PR:Q12431; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12431; protein.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
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; IPR029008; EMC6-like.
DR Pfam; PF07019; EMC6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..108
FT /note="ER membrane protein complex subunit 6"
FT /id="PRO_0000247112"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..48
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..108
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT HELIX 14..41
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 46..67
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:6WB9"
SQ SEQUENCE 108 AA; 12404 MW; 36C316F18156823E CRC64;
MSSNEEVFTQ INATANVVDN KKRLLFVQDS SALVLGLVAG FLQIESVHGF IWFLILYNLI
NVIYIVWICQ LQPGKFYQSP LHDIFFESFF REITGFVMAW TFGYALIG
