EMC3_MOUSE
ID EMC3_MOUSE Reviewed; 261 AA.
AC Q99KI3; Q3TIK3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ER membrane protein complex subunit 3;
DE AltName: Full=Transmembrane protein 111;
GN Name=Emc3; Synonyms=Tmem111;
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, and DBA/2J; TISSUE=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 MRNA].
RC STRAIN=FVB/N; 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 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:Q9P0I2}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q9P0I2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9P0I2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9P0I2}.
CC -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000305}.
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DR EMBL; AK075595; BAC35844.1; -; mRNA.
DR EMBL; AK167819; BAE39843.1; -; mRNA.
DR EMBL; BC004641; AAH04641.1; -; mRNA.
DR CCDS; CCDS20425.1; -.
DR RefSeq; NP_780310.1; NM_175101.3.
DR AlphaFoldDB; Q99KI3; -.
DR SMR; Q99KI3; -.
DR BioGRID; 211205; 12.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q99KI3; 10.
DR STRING; 10090.ENSMUSP00000032425; -.
DR iPTMnet; Q99KI3; -.
DR PhosphoSitePlus; Q99KI3; -.
DR EPD; Q99KI3; -.
DR jPOST; Q99KI3; -.
DR MaxQB; Q99KI3; -.
DR PaxDb; Q99KI3; -.
DR PeptideAtlas; Q99KI3; -.
DR PRIDE; Q99KI3; -.
DR ProteomicsDB; 277584; -.
DR TopDownProteomics; Q99KI3; -.
DR Antibodypedia; 49265; 63 antibodies from 15 providers.
DR DNASU; 66087; -.
DR Ensembl; ENSMUST00000032425; ENSMUSP00000032425; ENSMUSG00000030286.
DR GeneID; 66087; -.
DR KEGG; mmu:66087; -.
DR UCSC; uc009dgu.1; mouse.
DR CTD; 55831; -.
DR MGI; MGI:1913337; Emc3.
DR VEuPathDB; HostDB:ENSMUSG00000030286; -.
DR eggNOG; KOG3188; Eukaryota.
DR GeneTree; ENSGT00390000005780; -.
DR HOGENOM; CLU_060791_0_0_1; -.
DR InParanoid; Q99KI3; -.
DR OMA; WYFLTLF; -.
DR OrthoDB; 1482782at2759; -.
DR PhylomeDB; Q99KI3; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 66087; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Emc3; mouse.
DR PRO; PR:Q99KI3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99KI3; protein.
DR Bgee; ENSMUSG00000030286; Expressed in vestibular membrane of cochlear duct and 251 other tissues.
DR Genevisible; Q99KI3; 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: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; IPR008568; EMC3.
DR InterPro; IPR002809; EMC3/TMCO1.
DR PANTHER; PTHR13116; PTHR13116; 1.
DR Pfam; PF01956; EMC3_TMCO1; 1.
DR PIRSF; PIRSF010045; DUF850_TM_euk; 1.
DR SMART; SM01415; DUF106; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT CHAIN 2..261
FT /note="ER membrane protein complex subunit 3"
FT /id="PRO_0000211407"
FT TOPO_DOM 2..14
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TOPO_DOM 39..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TRANSMEM 115..130
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TOPO_DOM 131..168
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TOPO_DOM 188..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
SQ SEQUENCE 261 AA; 29980 MW; 0FA0CE154D6C1FCC CRC64;
MAGPELLLDS NIRLWVVLPI VIITFFVGMI RHYVSILLQS DKKLTQEQVS DSQVLIRSRV
LRENGKYIPK QSFLTRKYYF NNPEDGFFKK TKRKVVPPSP MTDPTMLTDM MKGNVTNVLP
MILIGGWINM TFSGFVTTKV PFPLTLRFKP MLQQGIELLT LDASWVSSAS WYFLNVFGLR
SIYSLILGQD NAADQSRMMQ EQMTGAAMAM PADTNKAFKT EWEALELTDH QWALDDVEEE
LMARDLHFEG MFKKELQTSI F
