EMC1_HUMAN
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 03-AUG-2022, entry version 159.
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: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}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231}.
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}.
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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_001271427.1. [Q8N766-2]
DR RefSeq; NP_001258357.1; NM_001271428.1. [Q8N766-3]
DR RefSeq; NP_001258358.1; NM_001271429.1. [Q8N766-4]
DR RefSeq; NP_055862.1; NM_015047.2. [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 PDBsum; 6WW7; -.
DR PDBsum; 6Z3W; -.
DR PDBsum; 7ADO; -.
DR PDBsum; 7ADP; -.
DR AlphaFoldDB; Q8N766; -.
DR SMR; Q8N766; -.
DR BioGRID; 116700; 426.
DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q8N766; 48.
DR MINT; Q8N766; -.
DR STRING; 9606.ENSP00000420608; -.
DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR GlyConnect; 1223; 6 N-Linked glycans (1 site).
DR GlyGen; Q8N766; 3 sites, 8 N-linked glycans (1 site).
DR iPTMnet; Q8N766; -.
DR MetOSite; Q8N766; -.
DR PhosphoSitePlus; Q8N766; -.
DR SwissPalm; Q8N766; -.
DR BioMuta; EMC1; -.
DR DMDM; 74751081; -.
DR EPD; Q8N766; -.
DR jPOST; Q8N766; -.
DR MassIVE; Q8N766; -.
DR MaxQB; Q8N766; -.
DR PaxDb; Q8N766; -.
DR PeptideAtlas; Q8N766; -.
DR PRIDE; Q8N766; -.
DR ProteomicsDB; 72266; -. [Q8N766-1]
DR ProteomicsDB; 72267; -. [Q8N766-2]
DR ProteomicsDB; 72268; -. [Q8N766-3]
DR ProteomicsDB; 72269; -. [Q8N766-4]
DR TopDownProteomics; Q8N766-3; -. [Q8N766-3]
DR Antibodypedia; 53149; 195 antibodies from 26 providers.
DR DNASU; 23065; -.
DR Ensembl; ENST00000375199.7; ENSP00000364345.3; ENSG00000127463.16. [Q8N766-2]
DR Ensembl; ENST00000375208.7; ENSP00000364354.3; ENSG00000127463.16. [Q8N766-4]
DR Ensembl; ENST00000477853.6; ENSP00000420608.1; ENSG00000127463.16. [Q8N766-1]
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 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 neXtProt; NX_Q8N766; -.
DR OpenTargets; ENSG00000127463; -.
DR Orphanet; 480898; Global developmental delay-visual anomalies-progressive cerebellar atrophy-truncal hypotonia syndrome.
DR PharmGKB; PA142671634; -.
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; 1017611at2759; -.
DR PhylomeDB; Q8N766; -.
DR TreeFam; TF313012; -.
DR PathwayCommons; Q8N766; -.
DR SignaLink; Q8N766; -.
DR BioGRID-ORCS; 23065; 427 hits in 1088 CRISPR screens.
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 196 other tissues.
DR ExpressionAtlas; Q8N766; baseline and differential.
DR Genevisible; Q8N766; HS.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
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: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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR026895; EMC1.
DR InterPro; IPR011678; EMC1_C.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR21573; PTHR21573; 1.
DR Pfam; PF07774; EMC1_C; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Neurodegeneration;
KW Reference proteome; Signal; Transmembrane; 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 unknown pathological 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; unknown pathological
FT significance; 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 HELIX 24..29
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6WW7"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6WW7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6WW7"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6WW7"
FT HELIX 481..501
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 606..609
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 656..665
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 680..685
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 693..699
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 706..712
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 731..734
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 756..766
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 769..776
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 790..797
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 798..801
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 802..815
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 819..821
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 832..842
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 845..849
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 860..864
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 870..874
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 875..877
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 888..893
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 906..908
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 910..913
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 921..926
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 928..931
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 933..941
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 943..947
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 949..954
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 962..966
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 969..981
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 984..991
FT /evidence="ECO:0007829|PDB:7ADO"
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
