EMC8_MOUSE
ID EMC8_MOUSE Reviewed; 207 AA.
AC O70378;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ER membrane protein complex subunit 8;
DE AltName: Full=Neighbor of COX4;
GN Name=Emc8; Synonyms=Cox4al, Cox4nb, Noc4;
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].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=10337626; DOI=10.1007/s003359901031;
RA Bachman N.J., Wu W., Schmidt T.R., Grossman L.I., Lomax M.I.;
RT "The 5-prime region of the COX4 gene contains a novel overlapping gene,
RT NOC4.";
RL Mamm. Genome 10:506-512(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
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:O43402}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC). EMC8 and
CC EMC9 are mutually exclusive subunits of the EMC complex.
CC {ECO:0000250|UniProtKB:O43402}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43402}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43402}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O43402}.
CC -!- SIMILARITY: Belongs to the EMC8/EMC9 family. {ECO:0000305}.
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DR EMBL; AF052621; AAC12933.1; -; mRNA.
DR EMBL; BC009103; AAH09103.1; -; mRNA.
DR CCDS; CCDS22719.1; -.
DR RefSeq; NP_035056.1; NM_010926.5.
DR AlphaFoldDB; O70378; -.
DR SMR; O70378; -.
DR BioGRID; 201800; 3.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR STRING; 10090.ENSMUSP00000034277; -.
DR iPTMnet; O70378; -.
DR PhosphoSitePlus; O70378; -.
DR SwissPalm; O70378; -.
DR EPD; O70378; -.
DR jPOST; O70378; -.
DR PaxDb; O70378; -.
DR PeptideAtlas; O70378; -.
DR PRIDE; O70378; -.
DR ProteomicsDB; 277832; -.
DR Antibodypedia; 30647; 276 antibodies from 22 providers.
DR DNASU; 18117; -.
DR Ensembl; ENSMUST00000034277; ENSMUSP00000034277; ENSMUSG00000031819.
DR GeneID; 18117; -.
DR KEGG; mmu:18117; -.
DR UCSC; uc009nrf.1; mouse.
DR CTD; 10328; -.
DR MGI; MGI:1343095; Emc8.
DR VEuPathDB; HostDB:ENSMUSG00000031819; -.
DR eggNOG; KOG3289; Eukaryota.
DR GeneTree; ENSGT00390000006738; -.
DR HOGENOM; CLU_087337_0_1_1; -.
DR InParanoid; O70378; -.
DR OMA; HVTPMAE; -.
DR OrthoDB; 1284861at2759; -.
DR PhylomeDB; O70378; -.
DR TreeFam; TF313860; -.
DR BioGRID-ORCS; 18117; 16 hits in 71 CRISPR screens.
DR ChiTaRS; Emc8; mouse.
DR PRO; PR:O70378; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O70378; protein.
DR Bgee; ENSMUSG00000031819; Expressed in epiblast (generic) and 267 other tissues.
DR ExpressionAtlas; O70378; baseline and differential.
DR Genevisible; O70378; 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; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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 CDD; cd08060; MPN_UPF0172; 1.
DR InterPro; IPR005366; EMC8/9.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR12941; PTHR12941; 1.
DR Pfam; PF03665; UPF0172; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome.
FT CHAIN 1..207
FT /note="ER membrane protein complex subunit 8"
FT /id="PRO_0000221188"
FT DOMAIN 4..147
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 207 AA; 23348 MW; 8F3CEF1BF2498958 CRC64;
MPGVKLTTQA YCKMVLHGAK YPHCAVNGLL VAERQRPRKE HPPGAGSHTL FVDCIPLFHG
TLALTPMLEV ALTLIDSWCK DNSYVIAGYY QANERVKDAS PNQVAEKVAS RIAEGFGDAA
LIMVDNAKFT MDCAAPTIHV YEQHENRWRC RDPHHDYCED WPEAQRISAS LLDSRSYETL
VDFDNHLDDI RSDWTNPEIN KAVLHLC