EMC6_MOUSE
ID EMC6_MOUSE Reviewed; 110 AA.
AC Q9CQW0; Q9CQ41;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ER membrane protein complex subunit 6;
DE AltName: Full=Transmembrane protein 93;
GN Name=Emc6; Synonyms=Tmem93;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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:Q9BV81}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q9BV81}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BV81}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9BV81}.
CC -!- SIMILARITY: Belongs to the EMC6 family. {ECO:0000305}.
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DR EMBL; AK002385; BAB22059.1; -; mRNA.
DR EMBL; AK003198; BAB22636.1; -; mRNA.
DR EMBL; AK004149; BAB23194.1; -; mRNA.
DR EMBL; AK012769; BAB28457.1; -; mRNA.
DR EMBL; AL670399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022104; AAH22104.1; -; mRNA.
DR CCDS; CCDS24999.1; -.
DR RefSeq; NP_001161942.1; NM_001168470.1.
DR RefSeq; NP_079594.1; NM_025318.3.
DR AlphaFoldDB; Q9CQW0; -.
DR SMR; Q9CQW0; -.
DR BioGRID; 211176; 18.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q9CQW0; 15.
DR STRING; 10090.ENSMUSP00000104120; -.
DR PhosphoSitePlus; Q9CQW0; -.
DR EPD; Q9CQW0; -.
DR jPOST; Q9CQW0; -.
DR MaxQB; Q9CQW0; -.
DR PaxDb; Q9CQW0; -.
DR PeptideAtlas; Q9CQW0; -.
DR PRIDE; Q9CQW0; -.
DR ProteomicsDB; 277857; -.
DR Antibodypedia; 23098; 62 antibodies from 16 providers.
DR DNASU; 66048; -.
DR Ensembl; ENSMUST00000054952; ENSMUSP00000060892; ENSMUSG00000047260.
DR Ensembl; ENSMUST00000108480; ENSMUSP00000104120; ENSMUSG00000047260.
DR GeneID; 66048; -.
DR KEGG; mmu:66048; -.
DR UCSC; uc007kab.2; mouse.
DR CTD; 83460; -.
DR MGI; MGI:1913298; Emc6.
DR VEuPathDB; HostDB:ENSMUSG00000047260; -.
DR eggNOG; KOG4455; Eukaryota.
DR GeneTree; ENSGT00390000003917; -.
DR HOGENOM; CLU_110781_3_0_1; -.
DR InParanoid; Q9CQW0; -.
DR OMA; FIYGMVH; -.
DR OrthoDB; 1547548at2759; -.
DR PhylomeDB; Q9CQW0; -.
DR TreeFam; TF332611; -.
DR BioGRID-ORCS; 66048; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Emc6; mouse.
DR PRO; PR:Q9CQW0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQW0; protein.
DR Bgee; ENSMUSG00000047260; Expressed in right kidney and 256 other tissues.
DR Genevisible; Q9CQW0; 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:0097631; C:integral component of omegasome membrane; ISO:MGI.
DR GO; GO:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; 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; IPR008504; Emc6.
DR InterPro; IPR029008; EMC6-like.
DR PANTHER; PTHR20994; PTHR20994; 1.
DR Pfam; PF07019; EMC6; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT CHAIN 2..110
FT /note="ER membrane protein complex subunit 6"
FT /id="PRO_0000254157"
FT TOPO_DOM 2..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 29..44
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TOPO_DOM 45..50
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TOPO_DOM 72..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 90..106
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TOPO_DOM 107..110
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT CONFLICT 63
FT /note="S -> P (in Ref. 1; BAB28457/BAB22059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12017 MW; 5120B6E4CC12FD48 CRC64;
MAAVVAKREG PPFISEAAVR GNAAVLDYCR TSVSALSGAT AGILGLTGLY GFIFYLLASV
LLSLLLILKA GRRWNKYFKS RRPLFTGGLI GGLFTYVLFW TFLYGMVHVY
