TMM43_HUMAN
ID TMM43_HUMAN Reviewed; 400 AA.
AC Q9BTV4; Q7L4N5; Q8NC30; Q96A63; Q96F19; Q96JX0; Q9H076;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transmembrane protein 43;
DE AltName: Full=Protein LUMA;
GN Name=TMEM43; ORFNames=UNQ2564/PRO6244;
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], AND VARIANTS ASN-168 AND THR-179.
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-168 AND THR-179.
RC TISSUE=Placenta, and Thyroid;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-168 AND THR-179.
RC TISSUE=Brain, Ovary, and Uterus;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=18230648; DOI=10.1242/jcs.019281;
RA Bengtsson L., Otto H.;
RT "LUMA interacts with emerin and influences its distribution at the inner
RT nuclear membrane.";
RL J. Cell Sci. 121:536-548(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP INTERACTION WITH SUN2, VARIANTS EDMD7 LYS-85 AND VAL-91, AND
RP CHARACTERIZATION OF VARIANTS EDMD7 LYS-85 AND VAL-91.
RX PubMed=21391237; DOI=10.1002/ana.22338;
RA Liang W.C., Mitsuhashi H., Keduka E., Nonaka I., Noguchi S., Nishino I.,
RA Hayashi Y.K.;
RT "TMEM43 mutations in Emery-Dreifuss muscular dystrophy-related myopathy.";
RL Ann. Neurol. 69:1005-1013(2011).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
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 [13]
RP FUNCTION, AND INTERACTION WITH CARD10.
RX PubMed=27991920; DOI=10.1038/onc.2016.430;
RA Jiang C., Zhu Y., Zhou Z., Gumin J., Bengtsson L., Wu W., Songyang Z.,
RA Lang F.F., Lin X.;
RT "TMEM43/LUMA is a key signaling component mediating EGFR-induced NF-kappaB
RT activation and tumor progression.";
RL Oncogene 36:2813-2823(2017).
RN [14]
RP FUNCTION, INTERACTION WITH RNF26, AND SUBCELLULAR LOCATION.
RX PubMed=32614325; DOI=10.7554/elife.57306;
RA Fenech E.J., Lari F., Charles P.D., Fischer R., Laetitia-Thezenas M.,
RA Bagola K., Paton A.W., Paton J.C., Gyrd-Hansen M., Kessler B.M.,
RA Christianson J.C.;
RT "Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies
RT modulators of innate immune signalling.";
RL Elife 9:0-0(2020).
RN [15]
RP VARIANT ARVD5 LEU-358.
RX PubMed=18313022; DOI=10.1016/j.ajhg.2008.01.010;
RA Merner N.D., Hodgkinson K.A., Haywood A.F.M., Connors S., French V.M.,
RA Drenckhahn J.-D., Kupprion C., Ramadanova K., Thierfelder L., McKenna W.,
RA Gallagher B., Morris-Larkin L., Bassett A.S., Parfrey P.S., Young T.-L.;
RT "Arrhythmogenic right ventricular cardiomyopathy type 5 is a fully
RT penetrant, lethal arrhythmic disorder caused by a missense mutation in the
RT TMEM43 gene.";
RL Am. J. Hum. Genet. 82:809-821(2008).
RN [16]
RP ACETYLATION AT ALA-2.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
CC -!- FUNCTION: May have an important role in maintaining nuclear envelope
CC structure by organizing protein complexes at the inner nuclear
CC membrane. Required for retaining emerin at the inner nuclear membrane
CC (By similarity). Plays a role in the modulation of innate immune
CC signaling through the cGAS-STING pathway by interacting with RNF26
CC (PubMed:32614325). In addition, functions as a critical signaling
CC component in mediating NF-kappa-B activation by acting downstream of
CC EGFR and upstream of CARD10 (PubMed:27991920).
CC {ECO:0000250|UniProtKB:Q9DBS1, ECO:0000269|PubMed:27991920,
CC ECO:0000269|PubMed:32614325}.
CC -!- SUBUNIT: Can form oligomers through the transmembrane domains.
CC Interacts with EMD; the interaction retains EMD at the inner nuclear
CC membrane. Interacts with LMNA and LMNB2 (By similarity). Interacts with
CC SUN2. Interacts with RNF26; this interaction is important to modulate
CC innate immune signaling through the cGAS-STING pathway
CC (PubMed:32614325). Interacts with CARD10 (PubMed:27991920).
CC {ECO:0000250, ECO:0000269|PubMed:21391237, ECO:0000269|PubMed:27991920,
CC ECO:0000269|PubMed:32614325}.
CC -!- INTERACTION:
CC Q9BTV4; Q6Q788: APOA5; NbExp=3; IntAct=EBI-721293, EBI-3936819;
CC Q9BTV4; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-721293, EBI-11343438;
CC Q9BTV4; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-721293, EBI-1045797;
CC Q9BTV4; P50402: EMD; NbExp=5; IntAct=EBI-721293, EBI-489887;
CC Q9BTV4; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-721293, EBI-18304435;
CC Q9BTV4; P02671-2: FGA; NbExp=3; IntAct=EBI-721293, EBI-9640259;
CC Q9BTV4; Q14318: FKBP8; NbExp=3; IntAct=EBI-721293, EBI-724839;
CC Q9BTV4; Q96HH9: GRAMD2B; NbExp=6; IntAct=EBI-721293, EBI-2832937;
CC Q9BTV4; P42858: HTT; NbExp=3; IntAct=EBI-721293, EBI-466029;
CC Q9BTV4; Q9Y5K3-3: PCYT1B; NbExp=3; IntAct=EBI-721293, EBI-12280028;
CC Q9BTV4; P11684: SCGB1A1; NbExp=3; IntAct=EBI-721293, EBI-7797649;
CC Q9BTV4; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-721293, EBI-747107;
CC Q9BTV4; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-721293, EBI-11522811;
CC Q9BTV4; Q9H7V2: SYNDIG1; NbExp=3; IntAct=EBI-721293, EBI-726331;
CC Q9BTV4; Q9BTV4: TMEM43; NbExp=4; IntAct=EBI-721293, EBI-721293;
CC Q9BTV4; Q9UHP3: USP25; NbExp=3; IntAct=EBI-721293, EBI-2513462;
CC Q9BTV4; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-721293, EBI-748373;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32614325}. Nucleus inner membrane; Multi-pass
CC membrane protein. Note=Retained in the inner nuclear membrane through
CC interaction with EMD and A- and B-lamins. The N- and C-termini are
CC oriented towards the nucleoplasm. The majority of the hydrophilic
CC domain resides in the endoplasmic reticulum lumen (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest expression in placenta. Also found at lower
CC levels in heart, ovary, spleen, small intestine, thymus, prostate and
CC testis. {ECO:0000269|PubMed:18230648}.
CC -!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 5
CC (ARVD5) [MIM:604400]: A congenital heart disease characterized by
CC infiltration of adipose and fibrous tissue into the right ventricle and
CC loss of myocardial cells, resulting in ventricular and supraventricular
CC arrhythmias. {ECO:0000269|PubMed:18313022}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Emery-Dreifuss muscular dystrophy 7, autosomal dominant
CC (EDMD7) [MIM:614302]: A form of Emery-Dreifuss muscular dystrophy, a
CC degenerative myopathy characterized by weakness and atrophy of muscle
CC without involvement of the nervous system, early contractures of the
CC elbows, Achilles tendons and spine, and cardiomyopathy associated with
CC cardiac conduction defects. {ECO:0000269|PubMed:21391237}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TMEM43 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136916; CAB66850.1; -; mRNA.
DR EMBL; AY358625; AAQ88988.1; -; mRNA.
DR EMBL; AK027466; BAB55131.1; -; mRNA.
DR EMBL; AK027757; BAB55348.1; -; mRNA.
DR EMBL; AK027827; BAB55396.1; ALT_INIT; mRNA.
DR EMBL; AK027877; BAB55425.1; -; mRNA.
DR EMBL; AK075010; BAC11350.1; -; mRNA.
DR EMBL; BC003125; AAH03125.1; -; mRNA.
DR EMBL; BC008054; AAH08054.2; -; mRNA.
DR EMBL; BC011719; AAH11719.1; -; mRNA.
DR CCDS; CCDS2618.1; -.
DR RefSeq; NP_077310.1; NM_024334.2.
DR AlphaFoldDB; Q9BTV4; -.
DR BioGRID; 122601; 195.
DR IntAct; Q9BTV4; 63.
DR MINT; Q9BTV4; -.
DR STRING; 9606.ENSP00000303992; -.
DR GlyGen; Q9BTV4; 1 site.
DR iPTMnet; Q9BTV4; -.
DR PhosphoSitePlus; Q9BTV4; -.
DR SwissPalm; Q9BTV4; -.
DR BioMuta; TMEM43; -.
DR DMDM; 74733151; -.
DR CPTAC; CPTAC-1646; -.
DR EPD; Q9BTV4; -.
DR jPOST; Q9BTV4; -.
DR MassIVE; Q9BTV4; -.
DR MaxQB; Q9BTV4; -.
DR PaxDb; Q9BTV4; -.
DR PeptideAtlas; Q9BTV4; -.
DR PRIDE; Q9BTV4; -.
DR ProteomicsDB; 79012; -.
DR TopDownProteomics; Q9BTV4; -.
DR Antibodypedia; 10951; 130 antibodies from 22 providers.
DR DNASU; 79188; -.
DR Ensembl; ENST00000306077.5; ENSP00000303992.5; ENSG00000170876.8.
DR GeneID; 79188; -.
DR KEGG; hsa:79188; -.
DR MANE-Select; ENST00000306077.5; ENSP00000303992.5; NM_024334.3; NP_077310.1.
DR UCSC; uc003byk.3; human.
DR CTD; 79188; -.
DR DisGeNET; 79188; -.
DR GeneCards; TMEM43; -.
DR GeneReviews; TMEM43; -.
DR HGNC; HGNC:28472; TMEM43.
DR HPA; ENSG00000170876; Low tissue specificity.
DR MalaCards; TMEM43; -.
DR MIM; 604400; phenotype.
DR MIM; 612048; gene.
DR MIM; 614302; phenotype.
DR neXtProt; NX_Q9BTV4; -.
DR OpenTargets; ENSG00000170876; -.
DR Orphanet; 98853; Autosomal dominant Emery-Dreifuss muscular dystrophy.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR PharmGKB; PA134871907; -.
DR VEuPathDB; HostDB:ENSG00000170876; -.
DR eggNOG; ENOG502QSR2; Eukaryota.
DR GeneTree; ENSGT00390000009671; -.
DR HOGENOM; CLU_042602_1_0_1; -.
DR InParanoid; Q9BTV4; -.
DR OMA; DWFPVVR; -.
DR OrthoDB; 866982at2759; -.
DR PhylomeDB; Q9BTV4; -.
DR TreeFam; TF324718; -.
DR PathwayCommons; Q9BTV4; -.
DR SignaLink; Q9BTV4; -.
DR BioGRID-ORCS; 79188; 5 hits in 1076 CRISPR screens.
DR ChiTaRS; TMEM43; human.
DR GeneWiki; TMEM43; -.
DR GenomeRNAi; 79188; -.
DR Pharos; Q9BTV4; Tbio.
DR PRO; PR:Q9BTV4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BTV4; protein.
DR Bgee; ENSG00000170876; Expressed in descending thoracic aorta and 194 other tissues.
DR ExpressionAtlas; Q9BTV4; baseline and differential.
DR Genevisible; Q9BTV4; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0071763; P:nuclear membrane organization; IDA:MGI.
DR InterPro; IPR012430; TMEM43_fam.
DR PANTHER; PTHR13416; PTHR13416; 1.
DR Pfam; PF07787; TMEM43; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cardiomyopathy; Disease variant;
KW Emery-Dreifuss muscular dystrophy; Endoplasmic reticulum; Immunity;
KW Innate immunity; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..400
FT /note="Transmembrane protein 43"
FT /id="PRO_0000284498"
FT TOPO_DOM 2..31
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..313
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..345
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..368
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..400
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25732826,
FT ECO:0007744|PubMed:19413330"
FT VARIANT 85
FT /note="E -> K (in EDMD7; the mutant protein forms
FT predominantly monomers with very few dimers indicating a
FT defect in oligomerization; overexpression in HeLa cells
FT results in abnormal nuclear structures and decreased
FT nuclear localization of both EMD and SUN2 with
FT mislocalization of EMD to the endoplasmic reticulum;
FT dbSNP:rs397514044)"
FT /evidence="ECO:0000269|PubMed:21391237"
FT /id="VAR_069794"
FT VARIANT 91
FT /note="I -> V (in EDMD7; the mutant protein is able to form
FT oligomers; overexpression in HeLa cells results in abnormal
FT nuclear structures and decreased nuclear localization of
FT both EMD and SUN2 with mislocalization of EMD to the
FT endoplasmic reticulum; dbSNP:rs144811578)"
FT /evidence="ECO:0000269|PubMed:21391237"
FT /id="VAR_069795"
FT VARIANT 168
FT /note="K -> N (in dbSNP:rs4685076)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_031751"
FT VARIANT 179
FT /note="M -> T (in dbSNP:rs2340917)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_031752"
FT VARIANT 233
FT /note="Y -> C (in dbSNP:rs35924492)"
FT /id="VAR_031753"
FT VARIANT 318
FT /note="A -> V (in dbSNP:rs11924644)"
FT /id="VAR_031754"
FT VARIANT 358
FT /note="S -> L (in ARVD5; dbSNP:rs63750743)"
FT /evidence="ECO:0000269|PubMed:18313022"
FT /id="VAR_044438"
FT CONFLICT 196
FT /note="L -> P (in Ref. 4; BAC11350)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="P -> L (in Ref. 5; AAH11719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 44876 MW; 70FDDD4ED1AA11DF CRC64;
MAANYSSTST RREHVKVKTS SQPGFLERLS ETSGGMFVGL MAFLLSFYLI FTNEGRALKT
ATSLAEGLSL VVSPDSIHSV APENEGRLVH IIGALRTSKL LSDPNYGVHL PAVKLRRHVE
MYQWVETEES REYTEDGQVK KETRYSYNTE WRSEIINSKN FDREIGHKNP SAMAVESFMA
TAPFVQIGRF FLSSGLIDKV DNFKSLSLSK LEDPHVDIIR RGDFFYHSEN PKYPEVGDLR
VSFSYAGLSG DDPDLGPAHV VTVIARQRGD QLVPFSTKSG DTLLLLHHGD FSAEEVFHRE
LRSNSMKTWG LRAAGWMAMF MGLNLMTRIL YTLVDWFPVF RDLVNIGLKA FAFCVATSLT
LLTVAAGWLF YRPLWALLIA GLALVPILVA RTRVPAKKLE
