ID   EMC3_HUMAN              Reviewed;         261 AA.
AC   Q9P0I2; B2R4Z9; Q53GH8; Q6ZMC2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   10-JUN-2026, entry version 168.
DE   RecName: Full=ER membrane protein complex subunit 3;
DE   AltName: Full=Transmembrane protein 111;
GN   Name=EMC3; Synonyms=TMEM111;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Adrenal gland;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Stomach cancer;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Small intestine;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-13; 140-147 AND 181-197, CLEAVAGE OF INITIATOR
RP   METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   IDENTIFICATION IN THE EMC COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=22119785; DOI=10.1038/ncb2383;
RA   Christianson J.C., Olzmann J.A., Shaler T.A., Sowa M.E., Bennett E.J.,
RA   Richter C.M., Tyler R.E., Greenblatt E.J., Harper J.W., Kopito R.R.;
RT   "Defining human ERAD networks through an integrative mapping strategy.";
RL   Nat. Cell Biol. 14:93-105(2012).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   FUNCTION.
RX   PubMed=30415835; DOI=10.1016/j.cell.2018.10.009;
RA   Chitwood P.J., Juszkiewicz S., Guna A., Shao S., Hegde R.S.;
RT   "EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.";
RL   Cell 175:1507-1519(2018).
RN   [12]
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).
RN   [13]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=29242231; DOI=10.1126/science.aao3099;
RA   Guna A., Volkmar N., Christianson J.C., Hegde R.S.;
RT   "The ER membrane protein complex is a transmembrane domain insertase.";
RL   Science 359:470-473(2018).
RN   [14] {ECO:0007744|PDB:6Z3W}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX, AND
RP   FUNCTION.
RX   PubMed=32459176; DOI=10.7554/elife.57887;
RA   O'Donnell J.P., Phillips B.P., Yagita Y., Juszkiewicz S., Wagner A.,
RA   Malinverni D., Keenan R.J., Miller E.A., Hegde R.S.;
RT   "The architecture of EMC reveals a path for membrane protein insertion.";
RL   Elife 9:0-0(2020).
RN   [15] {ECO:0007744|PDB:6WW7}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF THE EMC COMPLEX,
RP   FUNCTION, TOPOLOGY, AND MUTAGENESIS OF ARG-31; MET-101; MET-106; MET-110;
RP   MET-111; PHE-173 AND ARG-180.
RX   PubMed=32439656; DOI=10.1126/science.abb5008;
RA   Pleiner T., Tomaleri G.P., Januszyk K., Inglis A.J., Hazu M.,
RA   Voorhees R.M.;
RT   "Structural basis for membrane insertion by the human ER membrane protein
RT   complex.";
RL   Science 369:433-436(2020).
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:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656,
CC       PubMed:32459176). Preferentially accommodates proteins with
CC       transmembrane domains that are weakly hydrophobic or contain
CC       destabilizing features such as charged and aromatic residues
CC       (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the
CC       cotranslational insertion of multi-pass membrane proteins in which
CC       stop-transfer membrane-anchor sequences become ER membrane spanning
CC       helices (PubMed:29809151, PubMed:30415835). It is also required for the
CC       post-translational insertion of tail-anchored/TA proteins in
CC       endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By
CC       mediating the proper cotranslational insertion of N-terminal
CC       transmembrane domains in an N-exo topology, with translocated N-
CC       terminus in the lumen of the ER, controls the topology of multi-pass
CC       membrane proteins like the G protein-coupled receptors
CC       (PubMed:30415835). By regulating the insertion of various proteins in
CC       membranes, it is indirectly involved in many cellular processes
CC       (Probable). {ECO:0000269|PubMed:29242231, ECO:0000269|PubMed:29809151,
CC       ECO:0000269|PubMed:30415835, ECO:0000269|PubMed:32439656,
CC       ECO:0000269|PubMed:32459176, ECO:0000305}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231,
CC       ECO:0000269|PubMed:29809151, ECO:0000269|PubMed:32439656,
CC       ECO:0000269|PubMed:32459176}.
CC   -!- INTERACTION:
CC       Q9P0I2; Q15006: EMC2; NbExp=12; IntAct=EBI-1054670, EBI-359031;
CC       Q9P0I2; Q13126: MTAP; NbExp=3; IntAct=EBI-1054670, EBI-2547776;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22119785}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:32439656}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9P0I2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P0I2-2; Sequence=VSP_014886;
CC   -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD18807.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF157321; AAF67487.1; -; mRNA.
DR   EMBL; AK172843; BAD18807.1; ALT_SEQ; mRNA.
DR   EMBL; AK222953; BAD96673.1; -; mRNA.
DR   EMBL; AK312008; BAG34946.1; -; mRNA.
DR   EMBL; CH471055; EAW64047.1; -; Genomic_DNA.
DR   EMBL; BC022807; AAH22807.1; -; mRNA.
DR   CCDS; CCDS2594.1; -. [Q9P0I2-1]
DR   RefSeq; NP_001381603.1; NM_001394674.1. [Q9P0I2-1]
DR   RefSeq; NP_060917.1; NM_018447.4. [Q9P0I2-1]
DR   PDB; 6WW7; EM; 3.40 A; C=1-261.
DR   PDB; 6Z3W; EM; 6.40 A; C=1-261.
DR   PDB; 7ADO; EM; 3.39 A; C=1-261.
DR   PDB; 7ADP; EM; 3.60 A; C=1-261.
DR   PDB; 8EOI; EM; 3.40 A; C=4-261.
DR   PDB; 8J0N; EM; 3.47 A; C=1-261.
DR   PDB; 8J0O; EM; 3.32 A; C=1-261.
DR   PDB; 8S9S; EM; 3.60 A; 3=1-261.
DR   PDB; 9C7V; EM; 6.60 A; 3=1-261.
DR   PDBsum; 6WW7; -.
DR   PDBsum; 6Z3W; -.
DR   PDBsum; 7ADO; -.
DR   PDBsum; 7ADP; -.
DR   PDBsum; 8EOI; -.
DR   PDBsum; 8J0N; -.
DR   PDBsum; 8J0O; -.
DR   PDBsum; 8S9S; -.
DR   PDBsum; 9C7V; -.
DR   AlphaFoldDB; Q9P0I2; -.
DR   EMDB; EMD-11732; -.
DR   EMDB; EMD-11733; -.
DR   EMDB; EMD-21929; -.
DR   EMDB; EMD-28376; -.
DR   EMDB; EMD-35906; -.
DR   EMDB; EMD-35907; -.
DR   EMDB; EMD-40245; -.
DR   EMDB; EMD-40246; -.
DR   EMDB; EMD-45295; -.
DR   SMR; Q9P0I2; -.
DR   BioGRID; 120936; 143.
DR   ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR   ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR   CORUM; Q9P0I2; -.
DR   FunCoup; Q9P0I2; 1854.
DR   IntAct; Q9P0I2; 86.
DR   MINT; Q9P0I2; -.
DR   STRING; 9606.ENSP00000245046; -.
DR   ChEMBL; CHEMBL6067207; -.
DR   TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR   iPTMnet; Q9P0I2; -.
DR   MetOSite; Q9P0I2; -.
DR   PhosphoSitePlus; Q9P0I2; -.
DR   BioMuta; EMC3; -.
DR   DMDM; 71153383; -.
DR   jPOST; Q9P0I2; -.
DR   MassIVE; Q9P0I2; -.
DR   PaxDb; 9606-ENSP00000245046; -.
DR   PeptideAtlas; Q9P0I2; -.
DR   ProteomicsDB; 83550; -. [Q9P0I2-1]
DR   ProteomicsDB; 83551; -. [Q9P0I2-2]
DR   Pumba; Q9P0I2; -.
DR   TopDownProteomics; Q9P0I2-1; -. [Q9P0I2-1]
DR   TopDownProteomics; Q9P0I2-2; -. [Q9P0I2-2]
DR   Antibodypedia; 49265; 60 antibodies from 15 providers.
DR   DNASU; 55831; -.
DR   Ensembl; ENST00000245046.7; ENSP00000245046.2; ENSG00000125037.14. [Q9P0I2-1]
DR   Ensembl; ENST00000470827.3; ENSP00000474771.2; ENSG00000125037.14. [Q9P0I2-1]
DR   GeneID; 55831; -.
DR   KEGG; hsa:55831; -.
DR   MANE-Select; ENST00000245046.7; ENSP00000245046.2; NM_001394674.1; NP_001381603.1.
DR   UCSC; uc003bun.4; human. [Q9P0I2-1]
DR   AGR; HGNC:23999; -.
DR   ClinPGx; PA142670762; -.
DR   CTD; 55831; -.
DR   DisGeNET; 55831; -.
DR   GeneCards; EMC3; -.
DR   HGNC; HGNC:23999; EMC3.
DR   HPA; ENSG00000125037; Low tissue specificity.
DR   MIM; 620273; gene.
DR   OpenTargets; ENSG00000125037; -.
DR   VEuPathDB; HostDB:ENSG00000125037; -.
DR   eggNOG; KOG3188; Eukaryota.
DR   GeneTree; ENSGT00390000005780; -.
DR   HOGENOM; CLU_060791_0_0_1; -.
DR   InParanoid; Q9P0I2; -.
DR   OMA; DSINMID; -.
DR   OrthoDB; 6745403at2759; -.
DR   PAN-GO; Q9P0I2; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9P0I2; -.
DR   PathwayCommons; Q9P0I2; -.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   SignaLink; Q9P0I2; -.
DR   Agora; ENSG00000125037; -.
DR   BioGRID-ORCS; 55831; 510 hits in 1170 CRISPR screens.
DR   ChiTaRS; EMC3; human.
DR   GenomeRNAi; 55831; -.
DR   Pharos; Q9P0I2; Tbio.
DR   PRO; PR:Q9P0I2; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9P0I2; protein.
DR   Bgee; ENSG00000125037; Expressed in triceps brachii and 207 other cell types or tissues.
DR   ExpressionAtlas; Q9P0I2; baseline and differential.
DR   GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IDA:ComplexPortal.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR   InterPro; IPR008568; EMC3.
DR   InterPro; IPR002809; EMC3/TMCO1.
DR   PANTHER; PTHR13116; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 3; 1.
DR   PANTHER; PTHR13116:SF10; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 3; 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; Alternative splicing; Direct protein sequencing;
KW   Endoplasmic reticulum; Membrane; Proteomics identification;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.6"
FT   CHAIN           2..261
FT                   /note="ER membrane protein complex subunit 3"
FT                   /id="PRO_0000211406"
FT   TOPO_DOM        2..14
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TOPO_DOM        39..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TRANSMEM        115..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TOPO_DOM        131..168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TRANSMEM        169..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TOPO_DOM        188..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   VAR_SEQ         220..261
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_014886"
FT   MUTAGEN         31
FT                   /note="R->A,E: No effect on EMC assembly but decreased
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         31
FT                   /note="R->K: No effect on EMC assembly and no effect on
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         101
FT                   /note="M->S: No effect on EMC assembly but decreased
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC; when associated
FT                   S-106, S-110 and S-111."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         106
FT                   /note="M->S: No effect on EMC assembly but decreased
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC; when associated
FT                   S-101, S-110 and S-111."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         110
FT                   /note="M->S: No effect on EMC assembly but decreased
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC; when associated
FT                   S-101, S-106 and S-111."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         111
FT                   /note="M->S: No effect on EMC assembly but decreased
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC; when associated
FT                   S-101, S-106 and S-110."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         173
FT                   /note="F->A: No effect on EMC assembly and no effect on
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         180
FT                   /note="R->A,E: No effect on EMC assembly but decreased
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         180
FT                   /note="R->K: No effect on EMC assembly and no effect on
FT                   membrane insertion of hydrophobic transmembrane
FT                   helices-containing proteins by the EMC."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   CONFLICT        29
FT                   /note="M -> T (in Ref. 2; BAD18807)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="V -> I (in Ref. 3; BAD96673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="Y -> H (in Ref. 2; BAD18807)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        250
FT                   /note="G -> D (in Ref. 2; BAD18807)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           11..14
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           17..38
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           46..63
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           87..90
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           102..112
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           119..131
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   STRAND          163..166
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   HELIX           168..178
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           180..187
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           214..227
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           250..256
FT                   /evidence="ECO:0007829|PDB:8J0O"
SQ   SEQUENCE   261 AA;  29952 MW;  0FB279E54D6C1FCC CRC64;
     MAGPELLLDS NIRLWVVLPI VIITFFVGMI RHYVSILLQS DKKLTQEQVS DSQVLIRSRV
     LRENGKYIPK QSFLTRKYYF NNPEDGFFKK TKRKVVPPSP MTDPTMLTDM MKGNVTNVLP
     MILIGGWINM TFSGFVTTKV PFPLTLRFKP MLQQGIELLT LDASWVSSAS WYFLNVFGLR
     SIYSLILGQD NAADQSRMMQ EQMTGAAMAM PADTNKAFKT EWEALELTDH QWALDDVEEE
     LMAKDLHFEG MFKKELQTSI F
//