EMC2_MOUSE
ID EMC2_MOUSE Reviewed; 297 AA.
AC Q9CRD2; Q925K1;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ER membrane protein complex subunit 2 {ECO:0000305};
DE AltName: Full=Tetratricopeptide repeat protein 35 {ECO:0000312|MGI:MGI:1913986};
DE Short=TPR repeat protein 35 {ECO:0000312|MGI:MGI:1913986};
GN Name=Emc2 {ECO:0000312|MGI:MGI:1913986};
GN Synonyms=Kiaa0103, Ttc35 {ECO:0000312|MGI:MGI:1913986};
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=Testis;
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 MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-297.
RC STRAIN=ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=11593002; DOI=10.1073/pnas.211201898;
RA Dreger M., Bengtsson L., Schoeneberg T., Otto H., Hucho F.;
RT "Nuclear envelope proteomics: novel integral membrane proteins of the inner
RT nuclear membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11943-11948(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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:Q15006}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q15006}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15006}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15006}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15006}. Note=May also localize to the nuclear
CC envelope. {ECO:0000269|PubMed:11593002}.
CC -!- SIMILARITY: Belongs to the EMC2 family. {ECO:0000305}.
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DR EMBL; AK015968; BAB30057.1; -; mRNA.
DR EMBL; AK014989; BAB29657.1; -; mRNA.
DR EMBL; BC004716; AAH04716.1; -; mRNA.
DR EMBL; AF332065; AAK56094.1; -; mRNA.
DR CCDS; CCDS27453.1; -.
DR RefSeq; NP_080012.1; NM_025736.2.
DR AlphaFoldDB; Q9CRD2; -.
DR SMR; Q9CRD2; -.
DR BioGRID; 211681; 3.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR STRING; 10090.ENSMUSP00000022962; -.
DR iPTMnet; Q9CRD2; -.
DR PhosphoSitePlus; Q9CRD2; -.
DR EPD; Q9CRD2; -.
DR jPOST; Q9CRD2; -.
DR MaxQB; Q9CRD2; -.
DR PaxDb; Q9CRD2; -.
DR PRIDE; Q9CRD2; -.
DR ProteomicsDB; 277583; -.
DR Antibodypedia; 26545; 107 antibodies from 23 providers.
DR DNASU; 66736; -.
DR Ensembl; ENSMUST00000022962; ENSMUSP00000022962; ENSMUSG00000022337.
DR GeneID; 66736; -.
DR KEGG; mmu:66736; -.
DR UCSC; uc007vpm.1; mouse.
DR CTD; 9694; -.
DR MGI; MGI:1913986; Emc2.
DR VEuPathDB; HostDB:ENSMUSG00000022337; -.
DR eggNOG; KOG3060; Eukaryota.
DR GeneTree; ENSGT00390000011922; -.
DR HOGENOM; CLU_052388_1_0_1; -.
DR InParanoid; Q9CRD2; -.
DR OMA; YILTCAE; -.
DR OrthoDB; 956854at2759; -.
DR PhylomeDB; Q9CRD2; -.
DR TreeFam; TF312997; -.
DR BioGRID-ORCS; 66736; 16 hits in 72 CRISPR screens.
DR ChiTaRS; Emc2; mouse.
DR PRO; PR:Q9CRD2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9CRD2; protein.
DR Bgee; ENSMUSG00000022337; Expressed in intercostal muscle and 249 other tissues.
DR ExpressionAtlas; Q9CRD2; baseline and differential.
DR Genevisible; Q9CRD2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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 Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR039856; EMC2-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12760; PTHR12760; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Reference proteome; Repeat;
KW TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15006"
FT CHAIN 2..297
FT /note="ER membrane protein complex subunit 2"
FT /id="PRO_0000106354"
FT REPEAT 87..120
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 155..188
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 192..225
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15006"
FT MOD_RES 255
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15006"
SQ SEQUENCE 297 AA; 34935 MW; 009366B7A3B5BCEA CRC64;
MAKVTERYDV TWEEMRDKMR KWREENSRNS EQIMEVGEEL INDYASKLGD DIWIIYEQVM
IAALDYGRDD LALFCLQELR RQFPGSHRVK RLTGMRFEAM ERYDDAIQLY DRILQEDPTN
TAARKRKIAI RKAQGKTVEA IRELNEYLEQ FVGDQEAWHE LAELYINEHD YAKAAFCLEE
LMMTNPHNHL YCQQYAEVKY TQGGLENLEL SRKYFAQALK LNNRNMRALF GLYMSASHIA
SNPKASAKMK KDNIKYASWA ANQINRAYQF AGRSKKETKY SLKAVEDMLE TLQITQS
