EMC3_YEAST
ID EMC3_YEAST Reviewed; 253 AA.
AC P36039; D6VWZ6; Q86ZT1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ER membrane protein complex subunit 3;
DE AltName: Full=Altered inheritance rate of mitochondria protein 27;
GN Name=EMC3; Synonyms=AIM27; OrderedLocusNames=YKL207W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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] OF 194-253.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(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, SUBUNIT, AND SUBCELLULAR LOCATION.
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:Q9P0I2, 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:0000305|PubMed:29809151}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9P0I2}.
CC -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82052.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA82052.1; Type=Frameshift; Evidence={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; Z28207; CAA82052.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY260882; AAP21750.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08962.1; -; Genomic_DNA.
DR PIR; S38045; S38045.
DR RefSeq; NP_012715.3; NM_001179772.1.
DR PDB; 6WB9; EM; 3.00 A; 3=1-253.
DR PDB; 7KRA; EM; 3.20 A; C=1-253.
DR PDB; 7KTX; EM; 4.30 A; C=1-253.
DR PDBsum; 6WB9; -.
DR PDBsum; 7KRA; -.
DR PDBsum; 7KTX; -.
DR AlphaFoldDB; P36039; -.
DR SMR; P36039; -.
DR BioGRID; 33916; 126.
DR ComplexPortal; CPX-307; Endoplasmic Reticulum Membrane Complex.
DR DIP; DIP-8136N; -.
DR IntAct; P36039; 7.
DR STRING; 4932.YKL207W; -.
DR TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR MaxQB; P36039; -.
DR PaxDb; P36039; -.
DR PRIDE; P36039; -.
DR EnsemblFungi; YKL207W_mRNA; YKL207W; YKL207W.
DR GeneID; 853628; -.
DR KEGG; sce:YKL207W; -.
DR SGD; S000001690; EMC3.
DR VEuPathDB; FungiDB:YKL207W; -.
DR eggNOG; KOG3188; Eukaryota.
DR GeneTree; ENSGT00390000005780; -.
DR HOGENOM; CLU_060791_0_0_1; -.
DR InParanoid; P36039; -.
DR OMA; WYFLTLF; -.
DR BioCyc; YEAST:G3O-31966-MON; -.
DR PRO; PR:P36039; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36039; protein.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
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; IPR008568; EMC3.
DR InterPro; IPR002809; EMC3/TMCO1.
DR PANTHER; PTHR13116; PTHR13116; 1.
DR Pfam; PF01956; EMC3_TMCO1; 1.
DR PIRSF; PIRSF010045; DUF850_TM_euk; 1.
DR SMART; SM01415; DUF106; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..253
FT /note="ER membrane protein complex subunit 3"
FT /id="PRO_0000211411"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 5..33
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 44..62
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:6WB9"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:7KRA"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:7KRA"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:6WB9"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:6WB9"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7KRA"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:6WB9"
SQ SEQUENCE 253 AA; 28352 MW; 499475DA44B93B3E CRC64;
MLLDDQLKYW VLLPISIVMV LTGVLKQYIM TLITGSSANE AQPRVKLTEW QYLQWAQLLI
GNGGNLSSDA FAAKKEFLVK DLTEERHLAK AKQQDGSQAG EVPNPFNDPS MSNAMMNMAK
GNMASFIPQT IIMWWVNHFF AGFILMQLPF PLTAKFKEML QTGIICQDLD VRWVSSISWY
FISVLGLNPV YNLIGLNDQD MGIQAGIGGP QGPQGPPQSQ VDKAMHAMAN DLTIIQHETC
LDNVEQRVLK QYM
