ID EMC1_HUMAN Reviewed; 993 AA. AC Q8N766; A8K6F3; Q14700; Q5TG62; Q63HL0; Q63HL3; Q8NBH8; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 10-JUN-2026, entry version 177. DE RecName: Full=ER membrane protein complex subunit 1; DE Flags: Precursor; GN Name=EMC1; Synonyms=KIAA0090; ORFNames=PSEC0263; 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 4), AND VARIANTS THR-345 RP AND ASN-347. RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-345. RC TISSUE=Placenta; 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] (ISOFORMS 1 AND 3). RC TISSUE=Amygdala, and Salivary gland; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(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 1). RC TISSUE=Testis; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-993 (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. The RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [8] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-913. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] 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 [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 IDENTIFICATION BY MASS SPECTROMETRY [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 [14] 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 [15] 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 [16] 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 [17] {ECO:0007744|PDB:6Z3W} RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX, AND RP 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 [18] {ECO:0007744|PDB:6WW7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF THE EMC COMPLEX, RP SUBUNIT, TOPOLOGY, SIGNAL PEPTIDE, DISULFIDE BOND, AND GLYCOSYLATION AT RP ASN-370; ASN-818 AND ASN-913. 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). RN [19] RP INVOLVEMENT IN CAVIPMR, AND VARIANTS CAVIPMR MET-82; ARG-471 AND ARG-868. RX PubMed=26942288; DOI=10.1016/j.ajhg.2016.01.011; RG Baylor-Hopkins Center for Mendelian Genomics; RA Harel T., Yesil G., Bayram Y., Coban-Akdemir Z., Charng W.L., Karaca E., RA Al Asmari A., Eldomery M.K., Hunter J.V., Jhangiani S.N., Rosenfeld J.A., RA Pehlivan D., El-Hattab A.W., Saleh M.A., LeDuc C.A., Muzny D., RA Boerwinkle E., Gibbs R.A., Chung W.K., Yang Y., Belmont J.W., Lupski J.R.; RT "Monoallelic and biallelic variants in EMC1 identified in individuals with RT global developmental delay, hypotonia, scoliosis, and cerebellar atrophy."; RL Am. J. Hum. Genet. 98:562-570(2016). RN [20] RP VARIANT THR-144. RX PubMed=23105016; DOI=10.1101/gr.144105.112; RA Abu-Safieh L., Alrashed M., Anazi S., Alkuraya H., Khan A.O., Al-Owain M., RA Al-Zahrani J., Al-Abdi L., Hashem M., Al-Tarimi S., Sebai M.A., Shamia A., RA Ray-Zack M.D., Nassan M., Al-Hassnan Z.N., Rahbeeni Z., Waheeb S., RA Alkharashi A., Abboud E., Al-Hazzaa S.A., Alkuraya F.S.; RT "Autozygome-guided exome sequencing in retinal dystrophy patients reveals RT pathogenetic mutations and novel candidate disease genes."; RL Genome Res. 23:236-247(2013). 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 -!- INTERACTION: CC Q8N766; P0DTC8: 8; Xeno; NbExp=3; IntAct=EBI-1044442, EBI-25475900; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:22119785}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8N766-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N766-2; Sequence=VSP_020328; CC Name=3; CC IsoId=Q8N766-3; Sequence=VSP_020329; CC Name=4; CC IsoId=Q8N766-4; Sequence=VSP_020327; CC -!- DISEASE: Cerebellar atrophy, visual impairment, and psychomotor CC retardation (CAVIPMR) [MIM:616875]: An autosomal recessive, CC neurodegenerative disorder characterized by developmental delay, CC intellectual disability, hypotonia, scoliosis, cerebellar atrophy, and CC variable dysmorphic features. {ECO:0000269|PubMed:26942288}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the EMC1 family. {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; AK075563; BAC11702.1; -; mRNA. DR EMBL; AK291618; BAF84307.1; -; mRNA. DR EMBL; BX648627; CAH56140.1; -; mRNA. DR EMBL; BX648708; CAH56165.1; -; mRNA. DR EMBL; AL035413; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471134; EAW94871.1; -; Genomic_DNA. DR EMBL; BC034589; AAH34589.1; -; mRNA. DR EMBL; D42044; BAA07645.2; -; mRNA. DR CCDS; CCDS190.1; -. [Q8N766-1] DR CCDS; CCDS59190.1; -. [Q8N766-4] DR CCDS; CCDS59191.1; -. [Q8N766-2] DR RefSeq; NP_001258356.1; NM_001271427.2. [Q8N766-2] DR RefSeq; NP_001258357.1; NM_001271428.2. [Q8N766-3] DR RefSeq; NP_001258358.1; NM_001271429.2. [Q8N766-4] DR RefSeq; NP_055862.1; NM_015047.3. [Q8N766-1] DR PDB; 6WW7; EM; 3.40 A; A=1-993. DR PDB; 6Z3W; EM; 6.40 A; A=482-510, A=960-993. DR PDB; 7ADO; EM; 3.39 A; A=1-993. DR PDB; 7ADP; EM; 3.60 A; A=1-993. DR PDB; 8EOI; EM; 3.40 A; A=21-993. DR PDB; 8J0N; EM; 3.47 A; A=1-993. DR PDB; 8J0O; EM; 3.32 A; A=1-993. DR PDB; 8S9S; EM; 3.60 A; 1=1-993. DR PDB; 9C7V; EM; 6.60 A; 1=1-993. 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; Q8N766; -. 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; Q8N766; -. DR BioGRID; 116700; 493. DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant. DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant. DR CORUM; Q8N766; -. DR FunCoup; Q8N766; 2904. DR IntAct; Q8N766; 122. DR MINT; Q8N766; -. DR NDEx; IQUERY-CP-EMC1; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000420608; -. DR ChEMBL; CHEMBL6067163; -. DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family. DR GlyConnect; Q8N766; 6 N-Linked glycans (1 site). DR GlyCosmos; Q8N766; 3 sites, 6 glycans. DR GlyGen; Q8N766; 4 sites, 14 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q8N766; -. DR MetOSite; Q8N766; -. DR PhosphoSitePlus; Q8N766; -. DR SwissPalm; Q8N766; -. DR BioMuta; EMC1; -. DR DMDM; 74751081; -. DR jPOST; Q8N766; -. DR MassIVE; Q8N766; -. DR PaxDb; 9606-ENSP00000420608; -. DR PeptideAtlas; Q8N766; -. DR ProteomicsDB; 72266; -. [Q8N766-1] DR ProteomicsDB; 72267; -. [Q8N766-2] DR ProteomicsDB; 72268; -. [Q8N766-3] DR ProteomicsDB; 72269; -. [Q8N766-4] DR Pumba; Q8N766; -. DR TopDownProteomics; Q8N766-3; -. [Q8N766-3] DR Antibodypedia; 53149; 181 antibodies from 26 providers. DR DNASU; 23065; -. DR Ensembl; ENST00000375199.7; ENSP00000364345.3; ENSG00000127463.17. [Q8N766-2] DR Ensembl; ENST00000375208.7; ENSP00000364354.3; ENSG00000127463.17. [Q8N766-4] DR Ensembl; ENST00000477853.6; ENSP00000420608.1; ENSG00000127463.17. [Q8N766-1] DR Ensembl; ENST00000911103.1; ENSP00000581162.1; ENSG00000127463.17. [Q8N766-3] DR GeneID; 23065; -. DR KEGG; hsa:23065; -. DR MANE-Select; ENST00000477853.6; ENSP00000420608.1; NM_015047.3; NP_055862.1. DR UCSC; uc001bbo.5; human. [Q8N766-1] DR AGR; HGNC:28957; -. DR ClinPGx; PA142671634; -. DR CTD; 23065; -. DR DisGeNET; 23065; -. DR GeneCards; EMC1; -. DR HGNC; HGNC:28957; EMC1. DR HPA; ENSG00000127463; Low tissue specificity. DR MalaCards; EMC1; -. DR MIM; 616846; gene. DR MIM; 616875; phenotype. DR OpenTargets; ENSG00000127463; -. DR Orphanet; 480898; Global developmental delay-visual anomalies-progressive cerebellar atrophy-truncal hypotonia syndrome. DR VEuPathDB; HostDB:ENSG00000127463; -. DR eggNOG; KOG2103; Eukaryota. DR GeneTree; ENSGT00390000002461; -. DR HOGENOM; CLU_005034_2_1_1; -. DR InParanoid; Q8N766; -. DR OMA; WSIMPLN; -. DR OrthoDB; 28092at2759; -. DR PAN-GO; Q8N766; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q8N766; -. DR PathwayCommons; Q8N766; -. DR SignaLink; Q8N766; -. DR Agora; ENSG00000127463; -. DR BioGRID-ORCS; 23065; 453 hits in 1168 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; EMC1; human. DR GenomeRNAi; 23065; -. DR Pharos; Q8N766; Tbio. DR PRO; PR:Q8N766; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8N766; protein. DR Bgee; ENSG00000127463; Expressed in stromal cell of endometrium and 198 other cell types or tissues. DR ExpressionAtlas; Q8N766; 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:0032991; C:protein-containing complex; IDA:MGI. 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 FunFam; 2.130.10.10:FF:000163; ER membrane protein complex subunit 1 isoform X2; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR058545; Beta-prop_EMC1_1st. DR InterPro; IPR026895; EMC1. DR InterPro; IPR011678; EMC1_C. DR InterPro; IPR011047; Quinoprotein_ADH-like_sf. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR21573; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 1; 1. DR PANTHER; PTHR21573:SF0; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 1; 1. DR Pfam; PF25293; Beta-prop_EMC1_N; 1. DR Pfam; PF07774; EMC1_C; 1. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Membrane; Neurodegeneration; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:32439656" FT CHAIN 23..993 FT /note="ER membrane protein complex subunit 1" FT /id="PRO_0000248597" FT TOPO_DOM 23..962 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:32439656" FT TRANSMEM 963..983 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:32439656" FT TOPO_DOM 984..993 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32439656" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:32439656, FT ECO:0007744|PDB:6WW7" FT CARBOHYD 818 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:32439656, FT ECO:0007744|PDB:6WW7" FT CARBOHYD 913 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:32439656, ECO:0007744|PDB:6WW7" FT DISULFID 227..237 FT /evidence="ECO:0000269|PubMed:32439656, FT ECO:0007744|PDB:6WW7" FT DISULFID 338..368 FT /evidence="ECO:0000269|PubMed:32439656, FT ECO:0007744|PDB:6WW7" FT VAR_SEQ 74..96 FT /note="LWRHVDKGTAEGAVDAMLLHGQD -> Y (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16303743" FT /id="VSP_020327" FT VAR_SEQ 343 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7788527" FT /id="VSP_020328" FT VAR_SEQ 437 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_020329" FT VARIANT 82 FT /note="T -> M (in CAVIPMR; dbSNP:rs869320625)" FT /evidence="ECO:0000269|PubMed:26942288" FT /id="VAR_076915" FT VARIANT 144 FT /note="A -> T (found in patients with retinitis pigmentosa; FT uncertain significance; dbSNP:rs869320623)" FT /evidence="ECO:0000269|PubMed:23105016" FT /id="VAR_076916" FT VARIANT 295 FT /note="L -> S (in dbSNP:rs3850531)" FT /id="VAR_027359" FT VARIANT 345 FT /note="S -> T (in dbSNP:rs709683)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:16303743" FT /id="VAR_027360" FT VARIANT 347 FT /note="S -> N (in dbSNP:rs709682)" FT /evidence="ECO:0000269|PubMed:16303743" FT /id="VAR_027361" FT VARIANT 471 FT /note="G -> R (in CAVIPMR; uncertain significance; FT dbSNP:rs879253819)" FT /evidence="ECO:0000269|PubMed:26942288" FT /id="VAR_076917" FT VARIANT 868 FT /note="G -> R (in CAVIPMR; dbSNP:rs869320626)" FT /evidence="ECO:0000269|PubMed:26942288" FT /id="VAR_076918" FT CONFLICT 9 FT /note="F -> L (in Ref. 2; CAH56140)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="P -> L (in Ref. 2; CAH56165)" FT /evidence="ECO:0000305" FT CONFLICT 469 FT /note="L -> P (in Ref. 2; CAH56165)" FT /evidence="ECO:0000305" FT CONFLICT 570 FT /note="F -> Y (in Ref. 1; BAC11702)" FT /evidence="ECO:0000305" FT CONFLICT 724 FT /note="R -> H (in Ref. 1; BAC11702)" FT /evidence="ECO:0000305" FT CONFLICT 824 FT /note="S -> F (in Ref. 1; BAC11702)" FT /evidence="ECO:0000305" FT CONFLICT 982..983 FT /note="LA -> PV (in Ref. 2; CAH56165)" FT /evidence="ECO:0000305" FT TURN 23..25 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 26..30 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 32..35 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 61..70 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:6WW7" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 105..114 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 116..122 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 130..146 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 148..158 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:7ADO" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:7ADO" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 193..206 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 209..216 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 234..239 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 240..243 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 244..255 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 257..260 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 262..265 FT /evidence="ECO:0007829|PDB:6WW7" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 302..308 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 321..329 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 331..337 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 372..382 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 385..394 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 396..399 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 405..412 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 416..424 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 430..433 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 435..438 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 440..445 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 449..458 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 460..463 FT /evidence="ECO:0007829|PDB:6WW7" FT HELIX 464..473 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 480..509 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 521..524 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 535..552 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 555..560 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 569..576 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 581..583 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 586..592 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 599..604 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 606..608 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 610..612 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 615..619 FT /evidence="ECO:0007829|PDB:7ADO" FT STRAND 625..633 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 634..636 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 637..643 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 649..653 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 656..665 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 666..668 FT /evidence="ECO:0007829|PDB:7ADO" FT STRAND 670..673 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 676..678 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 680..685 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 688..690 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 694..699 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 702..704 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 705..711 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 723..725 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 727..729 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 731..734 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 741..749 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 752..754 FT /evidence="ECO:0007829|PDB:6WW7" FT STRAND 757..762 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 764..766 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 769..774 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 776..786 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 788..797 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 798..801 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 802..811 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 820..822 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 824..826 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 832..839 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 847..849 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 853..855 FT /evidence="ECO:0007829|PDB:8EOI" FT STRAND 860..864 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 866..868 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 870..874 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 875..878 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 888..893 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 896..898 FT /evidence="ECO:0007829|PDB:6WW7" FT STRAND 906..908 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 910..913 FT /evidence="ECO:0007829|PDB:6WW7" FT STRAND 917..926 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 928..931 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 933..947 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 949..951 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 953..955 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 962..992 FT /evidence="ECO:0007829|PDB:8J0O" SQ SEQUENCE 993 AA; 111759 MW; C61B67802052A8A7 CRC64; MAAEWASRFW LWATLLIPAA AVYEDQVGKF DWRQQYVGKV KFASLEFSPG SKKLVVATEK NVIAALNSRT GEILWRHVDK GTAEGAVDAM LLHGQDVITV SNGGRIMRSW ETNIGGLNWE ITLDSGSFQA LGLVGLQESV RYIAVLKKTT LALHHLSSGH LKWVEHLPES DSIHYQMVYS YGSGVVWALG VVPFSHVNIV KFNVEDGEIV QQVRVSTPWL QHLSGACGVV DEAVLVCPDP SSRSLQTLAL ETEWELRQIP LQSLDLEFGS GFQPRVLPTQ PNPVDASRAQ FFLHLSPSHY ALLQYHYGTL SLLKNFPQTA LVSFATTGEK TVAAVMACRN EVQKSSSSED GSMGSFSEKS SSKDSLACFN QTYTINLYLV ETGRRLLDTT ITFSLEQSGT RPERLYIQVF LKKDDSVGYR ALVQTEDHLL LFLQQLAGKV VLWSREESLA EVVCLEMVDL PLTGAQAELE GEFGKKADGL LGMFLKRLSS QLILLQAWTS HLWKMFYDAR KPRSQIKNEI NIDTLARDEF NLQKMMVMVT ASGKLFGIES SSGTILWKQY LPNVKPDSSF KLMVQRTTAH FPHPPQCTLL VKDKESGMSS LYVFNPIFGK WSQVAPPVLK RPILQSLLLP VMDQDYAKVL LLIDDEYKVT AFPATRNVLR QLHELAPSIF FYLVDAEQGR LCGYRLRKDL TTELSWELTI PPEVQRIVKV KGKRSSEHVH SQGRVMGDRS VLYKSLNPNL LAVVTESTDA HHERTFIGIF LIDGVTGRII HSSVQKKAKG PVHIVHSENW VVYQYWNTKA RRNEFTVLEL YEGTEQYNAT AFSSLDRPQL PQVLQQSYIF PSSISAMEAT ITERGITSRH LLIGLPSGAI LSLPKALLDP RRPEIPTEQS REENLIPYSP DVQIHAERFI NYNQTVSRMR GIYTAPSGLE STCLVVAYGL DIYQTRVYPS KQFDVLKDDY DYVLISSVLF GLVFATMITK RLAQVKLLNR AWR //