ID EMC5_HUMAN Reviewed; 131 AA. AC Q8N4V1; B2R625; B4DIY3; D3DWG7; Q5JPP7; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 10-JUN-2026, entry version 166. DE RecName: Full=ER membrane protein complex subunit 5 {ECO:0000305|PubMed:29242231}; DE AltName: Full=Membrane magnesium transporter 1 {ECO:0000312|HGNC:HGNC:28100}; DE AltName: Full=Transmembrane protein 32 {ECO:0000312|HGNC:HGNC:28100}; GN Name=MMGT1 {ECO:0000312|HGNC:HGNC:28100}; GN Synonyms=EMC5 {ECO:0000303|PubMed:29242231}, TMEM32 GN {ECO:0000312|HGNC:HGNC:28100}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Blood; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP IDENTIFICATION IN THE EMC COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=22119785; DOI=10.1038/ncb2383; RA Christianson J.C., Olzmann J.A., Shaler T.A., Sowa M.E., Bennett E.J., RA Richter C.M., Tyler R.E., Greenblatt E.J., Harper J.W., Kopito R.R.; RT "Defining human ERAD networks through an integrative mapping strategy."; RL Nat. Cell Biol. 14:93-105(2012). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP FUNCTION. RX PubMed=30415835; DOI=10.1016/j.cell.2018.10.009; RA Chitwood P.J., Juszkiewicz S., Guna A., Shao S., Hegde R.S.; RT "EMC Is Required to Initiate Accurate Membrane Protein Topogenesis."; RL Cell 175:1507-1519(2018). RN [12] RP FUNCTION. RX PubMed=29809151; DOI=10.7554/elife.37018; RA Shurtleff M.J., Itzhak D.N., Hussmann J.A., Schirle Oakdale N.T., RA Costa E.A., Jonikas M., Weibezahn J., Popova K.D., Jan C.H., Sinitcyn P., RA Vembar S.S., Hernandez H., Cox J., Burlingame A.L., Brodsky J.L., Frost A., RA Borner G.H., Weissman J.S.; RT "The ER membrane protein complex interacts cotranslationally to enable RT biogenesis of multipass membrane proteins."; RL Elife 7:0-0(2018). RN [13] RP FUNCTION, AND SUBUNIT. RX PubMed=29242231; DOI=10.1126/science.aao3099; RA Guna A., Volkmar N., Christianson J.C., Hegde R.S.; RT "The ER membrane protein complex is a transmembrane domain insertase."; RL Science 359:470-473(2018). RN [14] {ECO:0007744|PDB:6Z3W} RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX, RP FUNCTION, AND TOPOLOGY. RX PubMed=32459176; DOI=10.7554/elife.57887; RA O'Donnell J.P., Phillips B.P., Yagita Y., Juszkiewicz S., Wagner A., RA Malinverni D., Keenan R.J., Miller E.A., Hegde R.S.; RT "The architecture of EMC reveals a path for membrane protein insertion."; RL Elife 9:0-0(2020). RN [15] {ECO:0007744|PDB:6WW7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF THE EMC COMPLEX, RP FUNCTION, AND TOPOLOGY. RX PubMed=32439656; DOI=10.1126/science.abb5008; RA Pleiner T., Tomaleri G.P., Januszyk K., Inglis A.J., Hazu M., RA Voorhees R.M.; RT "Structural basis for membrane insertion by the human ER membrane protein RT complex."; RL Science 369:433-436(2020). 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 (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, CC PubMed:32459176). Preferentially accommodates proteins with CC transmembrane domains that are weakly hydrophobic or contain CC destabilizing features such as charged and aromatic residues CC (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the CC cotranslational insertion of multi-pass membrane proteins in which CC stop-transfer membrane-anchor sequences become ER membrane spanning CC helices (PubMed:29809151, PubMed:30415835). It is also required for the CC post-translational insertion of tail-anchored/TA proteins in CC endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By CC mediating the proper cotranslational insertion of N-terminal CC transmembrane domains in an N-exo topology, with translocated N- CC terminus in the lumen of the ER, controls the topology of multi-pass CC membrane proteins like the G protein-coupled receptors CC (PubMed:30415835). By regulating the insertion of various proteins in CC membranes, it is indirectly involved in many cellular processes (By CC similarity). May be involved in Mg(2+) transport (By similarity). CC {ECO:0000250|UniProtKB:Q8K273, ECO:0000269|PubMed:29242231, CC ECO:0000269|PubMed:29809151, ECO:0000269|PubMed:30415835, CC ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC). CC {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231, CC ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. CC -!- INTERACTION: CC Q8N4V1; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-6163737, EBI-11277970; CC Q8N4V1; Q8TD06: AGR3; NbExp=3; IntAct=EBI-6163737, EBI-3925742; CC Q8N4V1; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-6163737, EBI-12109402; CC Q8N4V1; Q8WVX3-2: ARLN; NbExp=3; IntAct=EBI-6163737, EBI-12003442; CC Q8N4V1; P01031: C5; NbExp=3; IntAct=EBI-6163737, EBI-8558308; CC Q8N4V1; P07357: C8A; NbExp=3; IntAct=EBI-6163737, EBI-9021639; CC Q8N4V1; Q9H1M4: DEFB127; NbExp=3; IntAct=EBI-6163737, EBI-10305240; CC Q8N4V1; Q15006: EMC2; NbExp=13; IntAct=EBI-6163737, EBI-359031; CC Q8N4V1; Q9BV81: EMC6; NbExp=8; IntAct=EBI-6163737, EBI-2820492; CC Q8N4V1; P50402: EMD; NbExp=3; IntAct=EBI-6163737, EBI-489887; CC Q8N4V1; Q9Y3D6: FIS1; NbExp=3; IntAct=EBI-6163737, EBI-3385283; CC Q8N4V1; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-6163737, EBI-713304; CC Q8N4V1; O14653: GOSR2; NbExp=3; IntAct=EBI-6163737, EBI-4401517; CC Q8N4V1; O00155: GPR25; NbExp=3; IntAct=EBI-6163737, EBI-10178951; CC Q8N4V1; Q14416: GRM2; NbExp=3; IntAct=EBI-6163737, EBI-10232876; CC Q8N4V1; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-6163737, EBI-8503746; CC Q8N4V1; P11215: ITGAM; NbExp=3; IntAct=EBI-6163737, EBI-2568251; CC Q8N4V1; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-6163737, EBI-12133176; CC Q8N4V1; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-6163737, EBI-11956541; CC Q8N4V1; Q96ES6: MFSD3; NbExp=3; IntAct=EBI-6163737, EBI-745345; CC Q8N4V1; Q6N075: MFSD5; NbExp=4; IntAct=EBI-6163737, EBI-3920969; CC Q8N4V1; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-6163737, EBI-12070086; CC Q8N4V1; O95167: NDUFA3; NbExp=4; IntAct=EBI-6163737, EBI-1246131; CC Q8N4V1; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-6163737, EBI-10317425; CC Q8N4V1; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-6163737, EBI-11075081; CC Q8N4V1; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-6163737, EBI-981985; CC Q8N4V1; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-6163737, EBI-11721828; CC Q8N4V1; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-6163737, EBI-8636004; CC Q8N4V1; O75396: SEC22B; NbExp=3; IntAct=EBI-6163737, EBI-1058865; CC Q8N4V1; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-6163737, EBI-10281213; CC Q8N4V1; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-6163737, EBI-12867720; CC Q8N4V1; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-6163737, EBI-10314552; CC Q8N4V1; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-6163737, EBI-5235586; CC Q8N4V1; Q86Y82: STX12; NbExp=3; IntAct=EBI-6163737, EBI-2691717; CC Q8N4V1; Q16623: STX1A; NbExp=3; IntAct=EBI-6163737, EBI-712466; CC Q8N4V1; P61266: STX1B; NbExp=3; IntAct=EBI-6163737, EBI-9071709; CC Q8N4V1; Q13277: STX3; NbExp=3; IntAct=EBI-6163737, EBI-1394295; CC Q8N4V1; O43752: STX6; NbExp=3; IntAct=EBI-6163737, EBI-2695795; CC Q8N4V1; Q9UNK0: STX8; NbExp=3; IntAct=EBI-6163737, EBI-727240; CC Q8N4V1; P59542: TAS2R19; NbExp=3; IntAct=EBI-6163737, EBI-12847034; CC Q8N4V1; Q9NZ01: TECR; NbExp=3; IntAct=EBI-6163737, EBI-2877718; CC Q8N4V1; P07204: THBD; NbExp=3; IntAct=EBI-6163737, EBI-941422; CC Q8N4V1; P55061: TMBIM6; NbExp=3; IntAct=EBI-6163737, EBI-1045825; CC Q8N4V1; Q6PL24: TMED8; NbExp=3; IntAct=EBI-6163737, EBI-11603430; CC Q8N4V1; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-6163737, EBI-2800360; CC Q8N4V1; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-6163737, EBI-2339195; CC Q8N4V1; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-6163737, EBI-12195227; CC Q8N4V1; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-6163737, EBI-11956809; CC Q8N4V1; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-6163737, EBI-12038591; CC Q8N4V1; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-6163737, EBI-2852148; CC Q8N4V1; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-6163737, EBI-2548832; CC Q8N4V1; Q86Y07: VRK2; NbExp=3; IntAct=EBI-6163737, EBI-1207615; CC Q8N4V1; O95070: YIF1A; NbExp=3; IntAct=EBI-6163737, EBI-2799703; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:22119785}; Multi-pass membrane protein CC {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. Golgi CC apparatus membrane {ECO:0000250|UniProtKB:Q8K273}; Multi-pass membrane CC protein {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. CC Early endosome membrane {ECO:0000250|UniProtKB:Q8K273}; Multi-pass CC membrane protein {ECO:0000269|PubMed:32439656, CC ECO:0000269|PubMed:32459176}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N4V1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N4V1-2; Sequence=VSP_036488; CC -!- SIMILARITY: Belongs to the membrane magnesium transporter (TC 1.A.67) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK295829; BAG58645.1; -; mRNA. DR EMBL; AK312409; BAG35322.1; -; mRNA. DR EMBL; AL732579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL953870; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471150; EAW88483.1; -; Genomic_DNA. DR EMBL; CH471150; EAW88485.1; -; Genomic_DNA. DR EMBL; BC033588; AAH33588.1; -; mRNA. DR CCDS; CCDS14653.1; -. [Q8N4V1-1] DR RefSeq; NP_001316929.1; NM_001330000.2. [Q8N4V1-1] DR RefSeq; NP_775741.1; NM_173470.3. [Q8N4V1-1] DR PDB; 6WW7; EM; 3.40 A; E=1-131. DR PDB; 6Z3W; EM; 6.40 A; E=1-131. DR PDB; 7ADO; EM; 3.39 A; E=1-131. DR PDB; 7ADP; EM; 3.60 A; E=1-131. DR PDB; 8EOI; EM; 3.40 A; E=3-103. DR PDB; 8J0N; EM; 3.47 A; E=1-131. DR PDB; 8J0O; EM; 3.32 A; E=1-131. DR PDB; 8S9S; EM; 3.60 A; 5=1-131. DR PDB; 9C7V; EM; 6.60 A; 5=1-131. DR PDBsum; 6WW7; -. DR PDBsum; 6Z3W; -. DR PDBsum; 7ADO; -. DR PDBsum; 7ADP; -. DR PDBsum; 8EOI; -. DR PDBsum; 8J0N; -. DR PDBsum; 8J0O; -. DR PDBsum; 8S9S; -. DR PDBsum; 9C7V; -. DR AlphaFoldDB; Q8N4V1; -. DR EMDB; EMD-11732; -. DR EMDB; EMD-11733; -. DR EMDB; EMD-21929; -. DR EMDB; EMD-28376; -. DR EMDB; EMD-35906; -. DR EMDB; EMD-35907; -. DR EMDB; EMD-40245; -. DR EMDB; EMD-40246; -. DR EMDB; EMD-45295; -. DR SMR; Q8N4V1; -. DR BioGRID; 125021; 420. DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant. DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant. DR CORUM; Q8N4V1; -. DR FunCoup; Q8N4V1; 1136. DR IntAct; Q8N4V1; 206. DR MINT; Q8N4V1; -. DR STRING; 9606.ENSP00000306220; -. DR ChEMBL; CHEMBL6067286; -. DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family. DR GlyGen; Q8N4V1; 1 site, 3 N-linked glycans (1 site). DR iPTMnet; Q8N4V1; -. DR PhosphoSitePlus; Q8N4V1; -. DR SwissPalm; Q8N4V1; -. DR BioMuta; MMGT1; -. DR DMDM; 74751006; -. DR jPOST; Q8N4V1; -. DR MassIVE; Q8N4V1; -. DR PaxDb; 9606-ENSP00000306220; -. DR PeptideAtlas; Q8N4V1; -. DR ProteomicsDB; 71978; -. [Q8N4V1-1] DR ProteomicsDB; 71979; -. [Q8N4V1-2] DR Pumba; Q8N4V1; -. DR TopDownProteomics; Q8N4V1-1; -. [Q8N4V1-1] DR Antibodypedia; 51536; 125 antibodies from 16 providers. DR DNASU; 93380; -. DR Ensembl; ENST00000305963.3; ENSP00000306220.2; ENSG00000169446.7. [Q8N4V1-1] DR Ensembl; ENST00000679621.1; ENSP00000505226.1; ENSG00000169446.7. [Q8N4V1-1] DR GeneID; 93380; -. DR KEGG; hsa:93380; -. DR MANE-Select; ENST00000305963.3; ENSP00000306220.2; NM_173470.3; NP_775741.1. DR UCSC; uc004ezi.2; human. [Q8N4V1-1] DR AGR; HGNC:28100; -. DR ClinPGx; PA164723074; -. DR CTD; 93380; -. DR GeneCards; MMGT1; -. DR HGNC; HGNC:28100; MMGT1. DR HPA; ENSG00000169446; Low tissue specificity. DR MIM; 301098; gene. DR OpenTargets; ENSG00000169446; -. DR VEuPathDB; HostDB:ENSG00000169446; -. DR eggNOG; KOG3918; Eukaryota. DR GeneTree; ENSGT00510000047104; -. DR HOGENOM; CLU_122437_1_0_1; -. DR InParanoid; Q8N4V1; -. DR OMA; CYGIVHL; -. DR OrthoDB; 44756at2759; -. DR PAN-GO; Q8N4V1; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q8N4V1; -. DR PathwayCommons; Q8N4V1; -. DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events. DR SignaLink; Q8N4V1; -. DR Agora; ENSG00000169446; -. DR BioGRID-ORCS; 93380; 148 hits in 792 CRISPR screens. DR ChiTaRS; MMGT1; human. DR GenomeRNAi; 93380; -. DR Pharos; Q8N4V1; Tbio. DR PRO; PR:Q8N4V1; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8N4V1; protein. DR Bgee; ENSG00000169446; Expressed in secondary oocyte and 192 other cell types or tissues. DR ExpressionAtlas; Q8N4V1; baseline and differential. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0015693; P:magnesium ion transport; ISS:UniProtKB. DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IDA:ComplexPortal. DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:ComplexPortal. DR InterPro; IPR018937; MMgT. DR PANTHER; PTHR21181; -; 1. DR PANTHER; PTHR21181:SF7; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 5; 1. DR Pfam; PF10270; MMgT; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Endosome; KW Golgi apparatus; Magnesium; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..131 FT /note="ER membrane protein complex subunit 5" FT /id="PRO_0000286435" FT TOPO_DOM 1..3 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32439656" FT TRANSMEM 4..22 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:32439656" FT TOPO_DOM 23..43 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:32439656" FT TRANSMEM 44..63 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:32439656" FT TOPO_DOM 64..131 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32439656" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MTPLGSGPPREASIAQPSGFSTTETLCAQDFSDVIFLRRADTRRWKK FT KQLRRPSLLLLGCCSFGIM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_036488" FT HELIX 3..33 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 43..63 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 81..85 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:7ADO" FT HELIX 96..101 FT /evidence="ECO:0007829|PDB:8J0O" SQ SEQUENCE 131 AA; 14686 MW; DF6255A8172C6016 CRC64; MAPSLWKGLV GIGLFALAHA AFSAAQHRSY MRLTEKEDES LPIDIVLQTL LAFAVTCYGI VHIAGEFKDM DATSELKNKT FDTLRNHPSF YVFNHRGRVL FRPSDTANSS NQDALSSNTS LKLRKLESLR R //