EMC5_HUMAN
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 03-AUG-2022, entry version 148.
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},
GN TMEM32 {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:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176,
CC PubMed:32439656). Preferentially accommodates proteins with
CC transmembrane domains that are weakly hydrophobic or contain
CC destabilizing features such as charged and aromatic residues
CC (PubMed:30415835, PubMed:29809151, PubMed:29242231). 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:30415835, PubMed:29809151). It is also required for the
CC post-translational insertion of tail-anchored/TA proteins in
CC endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). 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: C4orf3; 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=9; IntAct=EBI-6163737, EBI-359031;
CC Q8N4V1; Q9BV81: EMC6; NbExp=6; 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=3; IntAct=EBI-6163737, EBI-3920969;
CC Q8N4V1; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-6163737, EBI-12070086;
CC Q8N4V1; O95167: NDUFA3; NbExp=3; 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_001330000.1. [Q8N4V1-1]
DR RefSeq; NP_775741.1; NM_173470.2. [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 PDBsum; 6WW7; -.
DR PDBsum; 6Z3W; -.
DR PDBsum; 7ADO; -.
DR PDBsum; 7ADP; -.
DR AlphaFoldDB; Q8N4V1; -.
DR SMR; Q8N4V1; -.
DR BioGRID; 125021; 377.
DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q8N4V1; 167.
DR MINT; Q8N4V1; -.
DR STRING; 9606.ENSP00000306220; -.
DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR iPTMnet; Q8N4V1; -.
DR PhosphoSitePlus; Q8N4V1; -.
DR SwissPalm; Q8N4V1; -.
DR BioMuta; MMGT1; -.
DR DMDM; 74751006; -.
DR EPD; Q8N4V1; -.
DR jPOST; Q8N4V1; -.
DR MassIVE; Q8N4V1; -.
DR MaxQB; Q8N4V1; -.
DR PaxDb; Q8N4V1; -.
DR PeptideAtlas; Q8N4V1; -.
DR PRIDE; Q8N4V1; -.
DR ProteomicsDB; 71978; -. [Q8N4V1-1]
DR ProteomicsDB; 71979; -. [Q8N4V1-2]
DR TopDownProteomics; Q8N4V1-1; -. [Q8N4V1-1]
DR Antibodypedia; 51536; 128 antibodies from 16 providers.
DR DNASU; 93380; -.
DR Ensembl; ENST00000305963.3; ENSP00000306220.2; ENSG00000169446.6. [Q8N4V1-1]
DR Ensembl; ENST00000679621.1; ENSP00000505226.1; ENSG00000169446.6. [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 CTD; 93380; -.
DR GeneCards; MMGT1; -.
DR HGNC; HGNC:28100; MMGT1.
DR HPA; ENSG00000169446; Low tissue specificity.
DR neXtProt; NX_Q8N4V1; -.
DR OpenTargets; ENSG00000169446; -.
DR PharmGKB; PA164723074; -.
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; 1558871at2759; -.
DR PhylomeDB; Q8N4V1; -.
DR TreeFam; TF323267; -.
DR PathwayCommons; Q8N4V1; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; Q8N4V1; -.
DR BioGRID-ORCS; 93380; 137 hits in 713 CRISPR screens.
DR ChiTaRS; MMGT1; human.
DR GenomeRNAi; 93380; -.
DR Pharos; Q8N4V1; Tdark.
DR PRO; PR:Q8N4V1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N4V1; protein.
DR Bgee; ENSG00000169446; Expressed in secondary oocyte and 190 other tissues.
DR Genevisible; Q8N4V1; HS.
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; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA: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:0022890; F:inorganic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0006825; P:copper ion transport; IEA:Ensembl.
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 Pfam; PF10270; MMgT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Magnesium; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; 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 5..34
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 43..63
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:7ADO"
SQ SEQUENCE 131 AA; 14686 MW; DF6255A8172C6016 CRC64;
MAPSLWKGLV GIGLFALAHA AFSAAQHRSY MRLTEKEDES LPIDIVLQTL LAFAVTCYGI
VHIAGEFKDM DATSELKNKT FDTLRNHPSF YVFNHRGRVL FRPSDTANSS NQDALSSNTS
LKLRKLESLR R
