TMM43_MOUSE
ID TMM43_MOUSE Reviewed; 400 AA.
AC Q9DBS1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transmembrane protein 43;
DE AltName: Full=Protein LUMA;
GN Name=Tmem43;
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11593002; DOI=10.1073/pnas.211201898;
RA Dreger M., Bengtsson L., Schoeneberg T., Otto H., Hucho F.;
RT "Nuclear envelope proteomics: novel integral membrane proteins of the inner
RT nuclear membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11943-11948(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Lung;
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=Czech II; 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 INTERACTION WITH EMD, LMNA, LMNB2, FUNCTION, AND SUBCELLULAR LOCATION.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
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: 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 (PubMed:18230648). Plays a role in the modulation of innate immune
CC signaling through the cGAS-STING pathway by interacting with RNF26. In
CC addition, functions as a critical signaling component in mediating NF-
CC kappa-B activation by acting downstream of EGFR and upstream of CARD10
CC (By similarity). {ECO:0000250|UniProtKB:Q9BTV4,
CC ECO:0000269|PubMed:18230648}.
CC -!- SUBUNIT: Can form oligomers through the transmembrane domains.
CC Interacts with EMD; the interaction retains EMD at the inner nuclear
CC membrane (PubMed:18230648). Interacts with LMNA and LMNB2
CC (PubMed:18230648). Interacts with SUN2. Interacts with RNF26; this
CC interaction is important to modulate innate immune signaling through
CC the cGAS-STING pathway. Interacts with CARD10. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9BTV4, ECO:0000269|PubMed:16141072,
CC ECO:0000269|PubMed:18230648}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BTV4}. Nucleus inner membrane
CC {ECO:0000269|PubMed:18230648}; Multi-pass membrane protein.
CC Note=Retained in the inner nuclear membrane through interaction with
CC EMD and A- and B-lamins. The N- and C-termini are oriented towards the
CC nucleoplasm. The majority of the hydrophilic domain resides in the
CC endoplasmic reticulum lumen. {ECO:0000269|PubMed:18230648}.
CC -!- SIMILARITY: Belongs to the TMEM43 family. {ECO:0000305}.
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DR EMBL; AK004778; BAB23556.1; -; mRNA.
DR EMBL; AK151693; BAE30617.1; -; mRNA.
DR EMBL; AK151766; BAE30672.1; -; mRNA.
DR EMBL; AK152078; BAE30929.1; -; mRNA.
DR EMBL; AK168559; BAE40432.1; -; mRNA.
DR EMBL; BC024933; AAH24933.1; -; mRNA.
DR CCDS; CCDS20368.1; -.
DR RefSeq; NP_083042.1; NM_028766.2.
DR AlphaFoldDB; Q9DBS1; -.
DR BioGRID; 216508; 3.
DR IntAct; Q9DBS1; 2.
DR MINT; Q9DBS1; -.
DR STRING; 10090.ENSMUSP00000032183; -.
DR PhosphoSitePlus; Q9DBS1; -.
DR SwissPalm; Q9DBS1; -.
DR EPD; Q9DBS1; -.
DR MaxQB; Q9DBS1; -.
DR PaxDb; Q9DBS1; -.
DR PeptideAtlas; Q9DBS1; -.
DR PRIDE; Q9DBS1; -.
DR ProteomicsDB; 259258; -.
DR TopDownProteomics; Q9DBS1; -.
DR DNASU; 74122; -.
DR Ensembl; ENSMUST00000032183; ENSMUSP00000032183; ENSMUSG00000030095.
DR GeneID; 74122; -.
DR KEGG; mmu:74122; -.
DR UCSC; uc009cyc.1; mouse.
DR CTD; 79188; -.
DR MGI; MGI:1921372; Tmem43.
DR VEuPathDB; HostDB:ENSMUSG00000030095; -.
DR eggNOG; ENOG502QSR2; Eukaryota.
DR GeneTree; ENSGT00390000009671; -.
DR HOGENOM; CLU_042602_1_0_1; -.
DR InParanoid; Q9DBS1; -.
DR OMA; DWFPVVR; -.
DR OrthoDB; 866982at2759; -.
DR PhylomeDB; Q9DBS1; -.
DR TreeFam; TF324718; -.
DR BioGRID-ORCS; 74122; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem43; mouse.
DR PRO; PR:Q9DBS1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DBS1; protein.
DR Bgee; ENSMUSG00000030095; Expressed in thoracic mammary gland and 217 other tissues.
DR Genevisible; Q9DBS1; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; IDA:MGI.
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; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BTV4"
FT CHAIN 2..400
FT /note="Transmembrane protein 43"
FT /id="PRO_0000284499"
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:0000250|UniProtKB:Q9BTV4"
SQ SEQUENCE 400 AA; 44783 MW; 5A9732B4214D4316 CRC64;
MAANYSSTSS RKEHVKVTSE PQPGFLERLS ETSGGMFVGL MTFLLSFYLI FTNEGRALKT
ATSLAEGLSL VVSPDSIHSV APENEGRLVH IIGALRTSKL LSDPNYGVHL PAVKLRRHVE
MYQWVETEES SEYTEDGQVK KETKYSYNTE WRSEIVNSRN FDREIGHKNP SAMAVESFTA
TAPFVQIGRF FLSAGLIDKI DNFKALSLAK LEDPHVDIIR RGDFFYHSEN PKYPEVGDVR
VSFSYAGLSS DDPDLGPAHV VTVIARQRGD QLIPYSTKSG DTLLLLHHGD FSAEEVFRRE
QKSNSMKTWG LRAAGWMAMF MGLNLMTRIL YTLVDWFPVF RDLVNIGLKA FAFCVATSLT
LLTVAAGWLF YRPLWAALIG CLALVPIIIA RTRVPAKKLE
