EMC4_HUMAN
ID EMC4_HUMAN Reviewed; 183 AA.
AC Q5J8M3; A8K3A9; B4DJQ4; Q96KX9; Q9BUI5; Q9P0T9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ER membrane protein complex subunit 4;
DE AltName: Full=Cell proliferation-inducing gene 17 protein;
DE AltName: Full=Transmembrane protein 85;
GN Name=EMC4; Synonyms=TMEM85; ORFNames=HSPC184, PIG17;
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).
RA Kim J.W.;
RT "Identification of a proliferation-inducing gene.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Placenta, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=18586032; DOI=10.1016/j.febslet.2008.06.042;
RA Ring G., Khoury C.M., Solar A.J., Yang Z., Mandato C.A., Greenwood M.T.;
RT "Transmembrane protein 85 from both human (TMEM85) and yeast (YGL231c)
RT inhibit hydrogen peroxide mediated cell death in yeast.";
RL FEBS Lett. 582:2637-2642(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP 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 [16]
RP ACETYLATION AT THR-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
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 [19]
RP FUNCTION.
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 [20]
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 [21] {ECO:0007744|PDB:6Z3W}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX,
RP FUNCTION, AND TOPOLOGY.
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 [22]
RP FUNCTION, AND TOPOLOGY.
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:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176,
CC PubMed:32439656). Preferentially accommodates proteins with
CC transmembrane domains that are weakly hydrophobic or contain
CC destabilizing features such as charged and aromatic residues
CC (PubMed:30415835, PubMed:29809151, PubMed:29242231). 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:30415835, PubMed:29809151). It is also required for the
CC post-translational insertion of tail-anchored/TA proteins in
CC endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). 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|PubMed:18586032}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231,
CC ECO:0000269|PubMed:32459176}.
CC -!- INTERACTION:
CC Q5J8M3; Q9NRM0-1: SLC2A9; NbExp=3; IntAct=EBI-2814031, EBI-25396304;
CC Q5J8M3; Q9NRM0-2: SLC2A9; NbExp=2; IntAct=EBI-2814031, EBI-25396386;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22119785}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:32439656, ECO:0000305|PubMed:32459176}. Note=Could
CC also be a single-pass transmembrane protein with cytosolic N-terminus
CC and lumenal C-terminus. {ECO:0000305|PubMed:32439656,
CC ECO:0000305|PubMed:32459176}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TMEM85v1;
CC IsoId=Q5J8M3-1; Sequence=Displayed;
CC Name=2; Synonyms=TMEM85v2;
CC IsoId=Q5J8M3-2; Sequence=VSP_020798, VSP_020799;
CC Name=3;
CC IsoId=Q5J8M3-3; Sequence=VSP_037374, VSP_037375;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain and heart. Isoform
CC 2 is expressed in heart. {ECO:0000269|PubMed:18586032}.
CC -!- SIMILARITY: Belongs to the EMC4 family. {ECO:0000305}.
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DR EMBL; AY336092; AAR24622.1; -; mRNA.
DR EMBL; AF151018; AAF36104.1; -; mRNA.
DR EMBL; AK075227; BAC11486.1; -; mRNA.
DR EMBL; AK290524; BAF83213.1; -; mRNA.
DR EMBL; AK296184; BAG58916.1; -; mRNA.
DR EMBL; AC079203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92292.1; -; Genomic_DNA.
DR EMBL; BC002583; AAH02583.1; -; mRNA.
DR CCDS; CCDS10035.1; -. [Q5J8M3-1]
DR CCDS; CCDS66732.1; -. [Q5J8M3-2]
DR RefSeq; NP_001273349.1; NM_001286420.1. [Q5J8M3-2]
DR RefSeq; NP_057538.1; NM_016454.3. [Q5J8M3-1]
DR PDB; 6Z3W; EM; 6.40 A; D=1-183.
DR PDB; 7ADO; EM; 3.39 A; D=1-183.
DR PDB; 7ADP; EM; 3.60 A; D=1-183.
DR PDBsum; 6Z3W; -.
DR PDBsum; 7ADO; -.
DR PDBsum; 7ADP; -.
DR AlphaFoldDB; Q5J8M3; -.
DR SMR; Q5J8M3; -.
DR BioGRID; 119397; 265.
DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q5J8M3; 29.
DR STRING; 9606.ENSP00000267750; -.
DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR iPTMnet; Q5J8M3; -.
DR PhosphoSitePlus; Q5J8M3; -.
DR SwissPalm; Q5J8M3; -.
DR BioMuta; EMC4; -.
DR DMDM; 115502869; -.
DR EPD; Q5J8M3; -.
DR jPOST; Q5J8M3; -.
DR MassIVE; Q5J8M3; -.
DR MaxQB; Q5J8M3; -.
DR PaxDb; Q5J8M3; -.
DR PeptideAtlas; Q5J8M3; -.
DR PRIDE; Q5J8M3; -.
DR ProteomicsDB; 62980; -. [Q5J8M3-1]
DR ProteomicsDB; 62981; -. [Q5J8M3-2]
DR ProteomicsDB; 62982; -. [Q5J8M3-3]
DR TopDownProteomics; Q5J8M3-1; -. [Q5J8M3-1]
DR TopDownProteomics; Q5J8M3-2; -. [Q5J8M3-2]
DR Antibodypedia; 65253; 75 antibodies from 21 providers.
DR DNASU; 51234; -.
DR Ensembl; ENST00000249209.8; ENSP00000249209.4; ENSG00000128463.13. [Q5J8M3-2]
DR Ensembl; ENST00000267750.9; ENSP00000267750.4; ENSG00000128463.13. [Q5J8M3-1]
DR GeneID; 51234; -.
DR KEGG; hsa:51234; -.
DR MANE-Select; ENST00000267750.9; ENSP00000267750.4; NM_016454.4; NP_057538.1.
DR UCSC; uc001zhq.5; human. [Q5J8M3-1]
DR CTD; 51234; -.
DR GeneCards; EMC4; -.
DR HGNC; HGNC:28032; EMC4.
DR HPA; ENSG00000128463; Low tissue specificity.
DR MIM; 616245; gene.
DR neXtProt; NX_Q5J8M3; -.
DR OpenTargets; ENSG00000128463; -.
DR PharmGKB; PA143485634; -.
DR VEuPathDB; HostDB:ENSG00000128463; -.
DR eggNOG; KOG3318; Eukaryota.
DR GeneTree; ENSGT00390000006970; -.
DR HOGENOM; CLU_098404_0_1_1; -.
DR InParanoid; Q5J8M3; -.
DR OMA; QQTFKVI; -.
DR PhylomeDB; Q5J8M3; -.
DR TreeFam; TF313750; -.
DR PathwayCommons; Q5J8M3; -.
DR SignaLink; Q5J8M3; -.
DR BioGRID-ORCS; 51234; 294 hits in 1081 CRISPR screens.
DR ChiTaRS; EMC4; human.
DR GenomeRNAi; 51234; -.
DR Pharos; Q5J8M3; Tbio.
DR PRO; PR:Q5J8M3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q5J8M3; protein.
DR Bgee; ENSG00000128463; Expressed in left ventricle myocardium and 184 other tissues.
DR ExpressionAtlas; Q5J8M3; baseline and differential.
DR Genevisible; Q5J8M3; HS.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; IPR009445; TMEM85/Emc4.
DR PANTHER; PTHR19315; PTHR19315; 1.
DR Pfam; PF06417; DUF1077; 1.
DR PIRSF; PIRSF017207; UCP017207_TM-p85; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..183
FT /note="ER membrane protein complex subunit 4"
FT /id="PRO_0000251914"
FT TOPO_DOM 2..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32459176"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32459176"
FT TOPO_DOM 88..98
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32459176"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32459176"
FT TOPO_DOM 121..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32459176"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32459176"
FT TOPO_DOM 149..183
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32459176"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 68..136
FT /note="RCWDIALGPLKQIPMNLFIMYMAGNTISIFPTMMVCMMAWRPIQALMAISAT
FT FKMLESSSQKFLQGLVY -> VQRYRCYRSPWASPELHTHPLLLGGVNVDSSYPEDLET
FT KLLEAGISVFYISATKVLNNLKNRRCLEHKV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037374"
FT VAR_SEQ 119..149
FT /note="TFKMLESSSQKFLQGLVYLIGNLMGLALAVY -> KNGVQWWRTAFVNMRKQ
FT RLVPMYLGLIYILL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020798"
FT VAR_SEQ 137..183
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037375"
FT VAR_SEQ 150..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020799"
FT VARIANT 98
FT /note="P -> T (in dbSNP:rs11544437)"
FT /id="VAR_053775"
FT CONFLICT 47
FT /note="Y -> H (in Ref. 1; AAR24622)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="K -> R (in Ref. 1; AAR24622)"
FT /evidence="ECO:0000305"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:7ADO"
SQ SEQUENCE 183 AA; 20087 MW; 96888D46FF22DEDE CRC64;
MTAQGGLVAN RGRRFKWAIE LSGPGGGSRG RSDRGSGQGD SLYPVGYLDK QVPDTSVQET
DRILVEKRCW DIALGPLKQI PMNLFIMYMA GNTISIFPTM MVCMMAWRPI QALMAISATF
KMLESSSQKF LQGLVYLIGN LMGLALAVYK CQSMGLLPTH ASDWLAFIEP PERMEFSGGG
LLL
