ID   EMC7_HUMAN              Reviewed;         242 AA.
AC   Q9NPA0; B2RC00; Q96ED5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Endoplasmic reticulum membrane protein complex subunit 7;
DE   AltName: Full=ER membrane protein complex subunit 7;
DE   Flags: Precursor;
GN   Name=EMC7; Synonyms=C11orf3, C15orf24; ORFNames=HT022, UNQ905/PRO1926;
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 [MRNA].
RX   PubMed=10873569; DOI=10.1006/bbrc.2000.2910;
RA   O'Brien K.P., Tapia-Paez I., Staahle-Baeckdahl M., Kedra D., Dumanski J.P.;
RT   "Characterization of five novel human genes in the 11q13-q22 region.";
RL   Biochem. Biophys. Res. Commun. 273:90-94(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RA   Ievolella C., Lanfranchi G.;
RT   "Full-length of some new muscular transcript.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hypothalamus;
RA   Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Lung;
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].
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   CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-23, AND
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-12.
RX   PubMed=17825839; DOI=10.1016/j.jmb.2007.07.028;
RA   Miller P.J., Pazy Y., Conti B., Riddle D., Appella E., Collins E.J.;
RT   "Single MHC mutation eliminates enthalpy associated with T cell receptor
RT   binding.";
RL   J. Mol. Biol. 373:315-327(2007).
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.
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   TOPOLOGY, AND SIGNAL PEPTIDE.
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}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231,
CC       ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}.
CC   -!- INTERACTION:
CC       Q9NPA0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-6309137, EBI-3867333;
CC       Q9NPA0; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-6309137, EBI-11959885;
CC       Q9NPA0; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-6309137, EBI-11958178;
CC       Q9NPA0; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-6309137, EBI-3958099;
CC       Q9NPA0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6309137, EBI-16439278;
CC       Q9NPA0; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-6309137, EBI-22310682;
CC       Q9NPA0; Q5T9L3-1: WLS; NbExp=3; IntAct=EBI-6309137, EBI-22114623;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22119785}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:32439656}.
CC   -!- SIMILARITY: Belongs to the EMC7 family. {ECO:0000305}.
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DR   EMBL; AJ250344; CAB96539.1; -; mRNA.
DR   EMBL; AJ245874; CAC01611.1; -; mRNA.
DR   EMBL; AF242729; AAG44477.1; -; mRNA.
DR   EMBL; AY358445; AAQ88810.1; -; mRNA.
DR   EMBL; AK314883; BAG37397.1; -; mRNA.
DR   EMBL; BC012456; AAH12456.1; -; mRNA.
DR   EMBL; BC104934; AAI04935.1; -; mRNA.
DR   EMBL; BC104936; AAI04937.1; -; mRNA.
DR   CCDS; CCDS10032.1; -.
DR   RefSeq; NP_064539.1; NM_020154.2.
DR   PDB; 1B0G; X-ray; 2.50 A; C/F=4-12.
DR   PDB; 1LP9; X-ray; 2.00 A; C/J=4-12.
DR   PDB; 2J8U; X-ray; 2.88 A; C/J=4-12.
DR   PDB; 2JCC; X-ray; 2.50 A; C/J=4-12.
DR   PDB; 2UWE; X-ray; 2.40 A; C/J=4-12.
DR   PDB; 6WW7; EM; 3.40 A; G=1-242.
DR   PDB; 6Z3W; EM; 6.40 A; G=1-242.
DR   PDB; 7ADO; EM; 3.39 A; G=1-242.
DR   PDB; 8EOI; EM; 3.40 A; G=43-158.
DR   PDB; 8S9S; EM; 3.60 A; 7=1-242.
DR   PDBsum; 1B0G; -.
DR   PDBsum; 1LP9; -.
DR   PDBsum; 2J8U; -.
DR   PDBsum; 2JCC; -.
DR   PDBsum; 2UWE; -.
DR   PDBsum; 6WW7; -.
DR   PDBsum; 6Z3W; -.
DR   PDBsum; 7ADO; -.
DR   PDBsum; 8EOI; -.
DR   PDBsum; 8S9S; -.
DR   AlphaFoldDB; Q9NPA0; -.
DR   EMDB; EMD-11732; -.
DR   EMDB; EMD-21929; -.
DR   EMDB; EMD-28376; -.
DR   EMDB; EMD-40245; -.
DR   EMDB; EMD-40246; -.
DR   SMR; Q9NPA0; -.
DR   BioGRID; 121211; 203.
DR   ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR   ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR   IntAct; Q9NPA0; 50.
DR   MINT; Q9NPA0; -.
DR   STRING; 9606.ENSP00000256545; -.
DR   TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR   GlyGen; Q9NPA0; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9NPA0; -.
DR   PhosphoSitePlus; Q9NPA0; -.
DR   BioMuta; EMC7; -.
DR   DMDM; 74752878; -.
DR   EPD; Q9NPA0; -.
DR   jPOST; Q9NPA0; -.
DR   MassIVE; Q9NPA0; -.
DR   MaxQB; Q9NPA0; -.
DR   PaxDb; 9606-ENSP00000256545; -.
DR   PeptideAtlas; Q9NPA0; -.
DR   ProteomicsDB; 81944; -.
DR   Pumba; Q9NPA0; -.
DR   Antibodypedia; 2446; 59 antibodies from 18 providers.
DR   DNASU; 56851; -.
DR   Ensembl; ENST00000256545.9; ENSP00000256545.4; ENSG00000134153.10.
DR   GeneID; 56851; -.
DR   KEGG; hsa:56851; -.
DR   MANE-Select; ENST00000256545.9; ENSP00000256545.4; NM_020154.3; NP_064539.1.
DR   UCSC; uc001zhm.4; human.
DR   AGR; HGNC:24301; -.
DR   CTD; 56851; -.
DR   DisGeNET; 56851; -.
DR   GeneCards; EMC7; -.
DR   HGNC; HGNC:24301; EMC7.
DR   HPA; ENSG00000134153; Low tissue specificity.
DR   MIM; 620631; gene.
DR   neXtProt; NX_Q9NPA0; -.
DR   OpenTargets; ENSG00000134153; -.
DR   PharmGKB; PA134900493; -.
DR   VEuPathDB; HostDB:ENSG00000134153; -.
DR   eggNOG; KOG3306; Eukaryota.
DR   GeneTree; ENSGT00390000017490; -.
DR   InParanoid; Q9NPA0; -.
DR   OMA; EMENMQM; -.
DR   OrthoDB; 4215044at2759; -.
DR   PhylomeDB; Q9NPA0; -.
DR   TreeFam; TF106158; -.
DR   PathwayCommons; Q9NPA0; -.
DR   SignaLink; Q9NPA0; -.
DR   BioGRID-ORCS; 56851; 537 hits in 1165 CRISPR screens.
DR   ChiTaRS; EMC7; human.
DR   EvolutionaryTrace; Q9NPA0; -.
DR   GenomeRNAi; 56851; -.
DR   Pharos; Q9NPA0; Tdark.
DR   PRO; PR:Q9NPA0; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NPA0; Protein.
DR   Bgee; ENSG00000134153; Expressed in decidua and 207 other cell types or tissues.
DR   ExpressionAtlas; Q9NPA0; 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:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR039163; EMC7.
DR   InterPro; IPR019008; EMC7_beta_sandwich.
DR   PANTHER; PTHR13605:SF4; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 7; 1.
DR   PANTHER; PTHR13605; UNCHARACTERIZED; 1.
DR   Pfam; PF09430; EMC7_beta-sandw; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   Genevisible; Q9NPA0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:32439656,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           24..242
FT                   /note="Endoplasmic reticulum membrane protein complex
FT                   subunit 7"
FT                   /id="PRO_0000240860"
FT   TOPO_DOM        24..159
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   HELIX           58..64
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   TURN            70..73
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:8EOI"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:7ADO"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:8EOI"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:6WW7"
SQ   SEQUENCE   242 AA;  26471 MW;  A71930B89A4C2458 CRC64;
     MAAALWGFFP VLLLLLLSGD VQSSEVPGAA AEGSGGSGVG IGDRFKIEGR AVVPGVKPQD
     WISAARVLVD GEEHVGFLKT DGSFVVHDIP SGSYVVEVVS PAYRFDPVRV DITSKGKMRA
     RYVNYIKTSE VVRLPYPLQM KSSGPPSYFI KRESWGWTDF LMNPMVMMMV LPLLIFVLLP
     KVVNTSDPDM RREMEQSMNM LNSNHELPDV SEFMTRLFSS KSSGKSSSGS SKTGKSGAGK
     RR
//