EMC7_MOUSE
ID EMC7_MOUSE Reviewed; 241 AA.
AC Q9EP72;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ER membrane protein complex subunit 7;
DE Flags: Precursor;
GN Name=Emc7; Synonyms=Orf3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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 [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RA Ievolella C., Campagna D., Lanfranchi G.;
RT "Full length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Preferentially accommodates proteins with transmembrane domains that
CC are weakly hydrophobic or contain destabilizing features such as
CC charged and aromatic residues. Involved in the cotranslational
CC insertion of multi-pass membrane proteins in which stop-transfer
CC membrane-anchor sequences become ER membrane spanning helices. It is
CC also required for the post-translational insertion of tail-anchored/TA
CC proteins in endoplasmic reticulum membranes. By mediating the proper
CC cotranslational insertion of N-terminal transmembrane domains in an N-
CC exo topology, with translocated N-terminus in the lumen of the ER,
CC controls the topology of multi-pass membrane proteins like the G
CC protein-coupled receptors. By regulating the insertion of various
CC proteins in membranes, it is indirectly involved in many cellular
CC processes. {ECO:0000250|UniProtKB:Q9NPA0}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q9NPA0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NPA0}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9NPA0}.
CC -!- SIMILARITY: Belongs to the EMC7 family. {ECO:0000305}.
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DR EMBL; AJ250345; CAC16213.1; -; mRNA.
DR EMBL; AJ278128; CAC01616.1; -; mRNA.
DR EMBL; AK088738; BAC40540.1; -; mRNA.
DR CCDS; CCDS16555.1; -.
DR RefSeq; NP_598510.1; NM_133749.2.
DR AlphaFoldDB; Q9EP72; -.
DR SMR; Q9EP72; -.
DR BioGRID; 215717; 2.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR STRING; 10090.ENSMUSP00000068610; -.
DR iPTMnet; Q9EP72; -.
DR PhosphoSitePlus; Q9EP72; -.
DR EPD; Q9EP72; -.
DR jPOST; Q9EP72; -.
DR MaxQB; Q9EP72; -.
DR PaxDb; Q9EP72; -.
DR PeptideAtlas; Q9EP72; -.
DR PRIDE; Q9EP72; -.
DR ProteomicsDB; 275612; -.
DR Antibodypedia; 2446; 49 antibodies from 18 providers.
DR DNASU; 73024; -.
DR Ensembl; ENSMUST00000069747; ENSMUSP00000068610; ENSMUSG00000055943.
DR GeneID; 73024; -.
DR KEGG; mmu:73024; -.
DR UCSC; uc008lpb.1; mouse.
DR CTD; 56851; -.
DR MGI; MGI:1920274; Emc7.
DR VEuPathDB; HostDB:ENSMUSG00000055943; -.
DR eggNOG; KOG3306; Eukaryota.
DR GeneTree; ENSGT00390000017490; -.
DR HOGENOM; CLU_073620_1_1_1; -.
DR InParanoid; Q9EP72; -.
DR OMA; EMENMQM; -.
DR OrthoDB; 1348328at2759; -.
DR PhylomeDB; Q9EP72; -.
DR TreeFam; TF106158; -.
DR BioGRID-ORCS; 73024; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Asz1; mouse.
DR PRO; PR:Q9EP72; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EP72; protein.
DR Bgee; ENSMUSG00000055943; Expressed in facial nucleus and 241 other tissues.
DR ExpressionAtlas; Q9EP72; baseline and differential.
DR Genevisible; Q9EP72; MM.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; ISS:UniProtKB.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR039163; EMC7.
DR InterPro; IPR019008; EMC7_beta_sandwich.
DR PANTHER; PTHR13605; PTHR13605; 1.
DR Pfam; PF09430; DUF2012; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT CHAIN 23..241
FT /note="ER membrane protein complex subunit 7"
FT /id="PRO_0000240862"
FT TOPO_DOM 23..158
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT REGION 216..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 26310 MW; B1973DD3B3F91764 CRC64;
MAGALWGFFS VLLLLLSGDA HSSEVPGAAA EGPGGSGVGL GDRFKIEGRA VVPGVKPQDW
ISAARVLVDG EEHVGFLKTD GSFVVHDIPS GSYVVEVISP AYKFDPVRVD ITSKGKMRAR
YVNYIKTSEV VRLPYPLQMK SSGPPSYFIK RESWGWTDFL MNPMVMMMVL PLLIFVLLPK
VVNTSDPDMR REMEQSMNML NSNHELPDVS EFMTRLFSSK SSGKSSSGSS KTGKSGAGKR
R
