EMC4_MOUSE
ID EMC4_MOUSE Reviewed; 183 AA.
AC Q9CZX9; A2AGJ7; Q9D1D9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ER membrane protein complex subunit 4;
DE AltName: Full=Transmembrane protein 85;
GN Name=Emc4; Synonyms=Tmem85;
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=BALB/cJ, and C57BL/6J; TISSUE=Medulla oblongata;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP 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:Q5J8M3}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q5J8M3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5J8M3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5J8M3}. Note=Could also be a single-pass
CC transmembrane protein with cytosolic N-terminus and lumenal C-terminus.
CC {ECO:0000250|UniProtKB:Q5J8M3}.
CC -!- SIMILARITY: Belongs to the EMC4 family. {ECO:0000305}.
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DR EMBL; AK003668; BAB22926.1; -; mRNA.
DR EMBL; AK012047; BAB27992.1; -; mRNA.
DR EMBL; AK078165; BAC37155.1; -; mRNA.
DR EMBL; AK167745; BAE39782.1; -; mRNA.
DR EMBL; AL683897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27839.1; -; Genomic_DNA.
DR EMBL; BC051926; AAH51926.1; -; mRNA.
DR CCDS; CCDS16553.1; -.
DR RefSeq; NP_080795.1; NM_026519.3.
DR AlphaFoldDB; Q9CZX9; -.
DR SMR; Q9CZX9; -.
DR BioGRID; 212612; 2.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q9CZX9; 2.
DR STRING; 10090.ENSMUSP00000028551; -.
DR iPTMnet; Q9CZX9; -.
DR PhosphoSitePlus; Q9CZX9; -.
DR SwissPalm; Q9CZX9; -.
DR EPD; Q9CZX9; -.
DR jPOST; Q9CZX9; -.
DR MaxQB; Q9CZX9; -.
DR PaxDb; Q9CZX9; -.
DR PeptideAtlas; Q9CZX9; -.
DR PRIDE; Q9CZX9; -.
DR ProteomicsDB; 277856; -.
DR Antibodypedia; 65253; 75 antibodies from 21 providers.
DR DNASU; 68032; -.
DR Ensembl; ENSMUST00000028551; ENSMUSP00000028551; ENSMUSG00000027131.
DR GeneID; 68032; -.
DR KEGG; mmu:68032; -.
DR UCSC; uc008loy.1; mouse.
DR CTD; 51234; -.
DR MGI; MGI:1915282; Emc4.
DR VEuPathDB; HostDB:ENSMUSG00000027131; -.
DR eggNOG; KOG3318; Eukaryota.
DR GeneTree; ENSGT00390000006970; -.
DR HOGENOM; CLU_098404_0_1_1; -.
DR InParanoid; Q9CZX9; -.
DR OMA; QQTFKVI; -.
DR OrthoDB; 1623701at2759; -.
DR PhylomeDB; Q9CZX9; -.
DR TreeFam; TF313750; -.
DR BioGRID-ORCS; 68032; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Emc4; mouse.
DR PRO; PR:Q9CZX9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CZX9; protein.
DR Bgee; ENSMUSG00000027131; Expressed in embryonic brain and 247 other tissues.
DR Genevisible; Q9CZX9; 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:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; IPR009445; TMEM85/Emc4.
DR PANTHER; PTHR19315; PTHR19315; 1.
DR Pfam; PF06417; DUF1077; 1.
DR PIRSF; PIRSF017207; UCP017207_TM-p85; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT CHAIN 2..183
FT /note="ER membrane protein complex subunit 4"
FT /id="PRO_0000251915"
FT TOPO_DOM 2..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT TOPO_DOM 88..98
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT TOPO_DOM 121..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT TOPO_DOM 149..183
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 9
FT /note="A -> R (in Ref. 1; BAB22926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20117 MW; 7FED8D53F092D161 CRC64;
MTTQGGLVAN RGRRFKWAIE LSGPGGGSRG RSDRGSGQGD SLYPVGYLDK QVPDTSVQET
DRILVEKRCW DIALGPLKQI PMNLFIMYMA GNTISIFPTM MVCMMAWRPI QALMAISATF
KMLESSSQKF LQGLVYLIGN LMGLALAVYK CQSMGLLPTH ASDWLAFIEP PERMEFSGGG
LLL
