EMC5_MOUSE
ID EMC5_MOUSE Reviewed; 131 AA.
AC Q8K273; A7UH87;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ER membrane protein complex subunit 5 {ECO:0000250|UniProtKB:Q8N4V1};
DE AltName: Full=Membrane magnesium transporter 1 {ECO:0000303|PubMed:18057121};
DE AltName: Full=Transmembrane protein 32 {ECO:0000312|MGI:MGI:2384305};
GN Name=Mmgt1 {ECO:0000303|PubMed:18057121, ECO:0000312|MGI:MGI:2384305};
GN Synonyms=Emc5 {ECO:0000250|UniProtKB:Q8N4V1},
GN Tmem32 {ECO:0000312|MGI:MGI:2384305};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=18057121; DOI=10.1152/ajpcell.00238.2007;
RA Goytain A., Quamme G.A.;
RT "Identification and characterization of a novel family of membrane
RT magnesium transporters, MMgT1 and MMgT2.";
RL Am. J. Physiol. 294:C495-C502(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Cerebellum, and Embryonic spinal cord;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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 similarity). By regulating the insertion
CC of various proteins in membranes, it is indirectly involved in many
CC cellular processes (Probable). May be involved Mg(2+) transport
CC (PubMed:18057121). {ECO:0000250|UniProtKB:Q8N4V1,
CC ECO:0000269|PubMed:18057121, ECO:0000305|PubMed:18057121}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q8N4V1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N4V1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N4V1}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:18057121}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N4V1}. Early endosome membrane
CC {ECO:0000269|PubMed:18057121}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N4V1}.
CC -!- TISSUE SPECIFICITY: Abundant in heart muscle and kidney with lower
CC levels in liver and brain and very little expression in intestine or
CC colon. In kidney, highest levels in distal convoluted tubule.
CC {ECO:0000269|PubMed:18057121}.
CC -!- INDUCTION: Up-regulated by low extracellular Mg(2+).
CC {ECO:0000269|PubMed:18057121}.
CC -!- SIMILARITY: Belongs to the membrane magnesium transporter (TC 1.A.67)
CC family. {ECO:0000305}.
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DR EMBL; EU069461; ABS87351.1; -; mRNA.
DR EMBL; AK036253; BAC29362.1; -; mRNA.
DR EMBL; AK043524; BAC31567.1; -; mRNA.
DR EMBL; AK049689; BAC33874.1; -; mRNA.
DR EMBL; BC032271; AAH32271.1; -; mRNA.
DR CCDS; CCDS30147.1; -.
DR RefSeq; NP_666346.1; NM_146234.3.
DR AlphaFoldDB; Q8K273; -.
DR SMR; Q8K273; -.
DR BioGRID; 231797; 2.
DR ComplexPortal; CPX-5882; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5883; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q8K273; 1.
DR MINT; Q8K273; -.
DR STRING; 10090.ENSMUSP00000051621; -.
DR TCDB; 1.A.67.1.1; the membrane mg(2+) transporter (mmgt) family.
DR iPTMnet; Q8K273; -.
DR PhosphoSitePlus; Q8K273; -.
DR EPD; Q8K273; -.
DR jPOST; Q8K273; -.
DR MaxQB; Q8K273; -.
DR PaxDb; Q8K273; -.
DR PeptideAtlas; Q8K273; -.
DR PRIDE; Q8K273; -.
DR ProteomicsDB; 291368; -.
DR Antibodypedia; 51536; 128 antibodies from 16 providers.
DR Ensembl; ENSMUST00000059899; ENSMUSP00000051621; ENSMUSG00000061273.
DR GeneID; 236792; -.
DR KEGG; mmu:236792; -.
DR UCSC; uc009tgj.1; mouse.
DR CTD; 93380; -.
DR MGI; MGI:2384305; Mmgt1.
DR VEuPathDB; HostDB:ENSMUSG00000061273; -.
DR eggNOG; KOG3918; Eukaryota.
DR GeneTree; ENSGT00510000047104; -.
DR HOGENOM; CLU_122437_1_0_1; -.
DR InParanoid; Q8K273; -.
DR OMA; CYGIVHL; -.
DR OrthoDB; 1558871at2759; -.
DR PhylomeDB; Q8K273; -.
DR TreeFam; TF323267; -.
DR BioGRID-ORCS; 236792; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Mmgt1; mouse.
DR PRO; PR:Q8K273; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8K273; protein.
DR Bgee; ENSMUSG00000061273; Expressed in manus and 235 other tissues.
DR Genevisible; Q8K273; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:MGI.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0006812; P:cation transport; IDA:MGI.
DR GO; GO:0006824; P:cobalt ion transport; IDA:MGI.
DR GO; GO:0006825; P:copper ion transport; IDA:MGI.
DR GO; GO:0006826; P:iron ion transport; IDA:MGI.
DR GO; GO:0015693; P:magnesium ion transport; IDA:UniProtKB.
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; IPR018937; MMgT.
DR Pfam; PF10270; MMgT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Magnesium; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..131
FT /note="ER membrane protein complex subunit 5"
FT /id="PRO_0000286436"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TRANSMEM 4..22
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TOPO_DOM 23..43
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TOPO_DOM 64..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 131 AA; 14677 MW; DB3841F8CCBD801E CRC64;
MAPSLWKGLV GVGLFALAHA AFSAAQHRSY MRLTEKEDES LPIDIVLQTL LAFAVTCYGI
VHIAGEFKDM DATSELKNKT FDTLRNHPSF YVFNHRGRVL FRPSDATNSS NLDALSSNTS
LKLRKFDSLR R
