TM109_MOUSE
ID TM109_MOUSE Reviewed; 243 AA.
AC Q3UBX0; Q8R006;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transmembrane protein 109;
DE AltName: Full=Mitsugumin-23;
DE Short=Mg23;
DE Flags: Precursor;
GN Name=Tmem109;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Macrophage;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, Mammary tumor, and Retina;
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 [3]
RP PROTEIN SEQUENCE OF 38-46 AND 48-59, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20060811; DOI=10.1016/j.bbrc.2010.01.013;
RA Yamazaki T., Sasaki N., Nishi M., Takeshima H.;
RT "Facilitation of DNA damage-induced apoptosis by endoplasmic reticulum
RT protein mitsugumin23.";
RL Biochem. Biophys. Res. Commun. 392:196-200(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 mediate cellular response to DNA damage by protecting
CC against ultraviolet C-induced cell death (PubMed:20060811). Can form
CC voltage-gated calcium and potassium channels in vitro (By similarity).
CC {ECO:0000250|UniProtKB:O77751, ECO:0000250|UniProtKB:Q9BVC6,
CC ECO:0000269|PubMed:20060811}.
CC -!- SUBUNIT: Homooligomer. Interacts with CRYAB.
CC {ECO:0000250|UniProtKB:O77751, ECO:0000250|UniProtKB:Q9BVC6}.
CC -!- INTERACTION:
CC Q3UBX0; P02511: CRYAB; Xeno; NbExp=2; IntAct=EBI-2366300, EBI-739060;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O77751}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O77751}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O77751}.
CC -!- DISRUPTION PHENOTYPE: Viable and normal in appearance.
CC {ECO:0000269|PubMed:20060811}.
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DR EMBL; AK150779; BAE29844.1; -; mRNA.
DR EMBL; AK151850; BAE30740.1; -; mRNA.
DR EMBL; AK152419; BAE31204.1; -; mRNA.
DR EMBL; AK165990; BAE38505.1; -; mRNA.
DR EMBL; BC022997; AAH22997.1; -; mRNA.
DR EMBL; BC023901; AAH23901.1; -; mRNA.
DR EMBL; BC025033; AAH25033.1; -; mRNA.
DR EMBL; BC025815; AAH25815.1; -; mRNA.
DR CCDS; CCDS29590.1; -.
DR RefSeq; NP_598903.1; NM_134142.1.
DR RefSeq; XP_006527380.1; XM_006527317.1.
DR AlphaFoldDB; Q3UBX0; -.
DR BioGRID; 212917; 16.
DR IntAct; Q3UBX0; 16.
DR MINT; Q3UBX0; -.
DR STRING; 10090.ENSMUSP00000039529; -.
DR TCDB; 1.A.74.1.1; the mitsugumin 23 (mg23) family.
DR iPTMnet; Q3UBX0; -.
DR PhosphoSitePlus; Q3UBX0; -.
DR EPD; Q3UBX0; -.
DR jPOST; Q3UBX0; -.
DR MaxQB; Q3UBX0; -.
DR PaxDb; Q3UBX0; -.
DR PeptideAtlas; Q3UBX0; -.
DR PRIDE; Q3UBX0; -.
DR ProteomicsDB; 259520; -.
DR Antibodypedia; 2041; 77 antibodies from 17 providers.
DR Ensembl; ENSMUST00000038128; ENSMUSP00000039529; ENSMUSG00000034659.
DR GeneID; 68539; -.
DR KEGG; mmu:68539; -.
DR UCSC; uc008gre.2; mouse.
DR CTD; 79073; -.
DR MGI; MGI:1915789; Tmem109.
DR VEuPathDB; HostDB:ENSMUSG00000034659; -.
DR eggNOG; ENOG502S0EJ; Eukaryota.
DR GeneTree; ENSGT00390000015704; -.
DR HOGENOM; CLU_099892_0_0_1; -.
DR InParanoid; Q3UBX0; -.
DR OMA; VFKVILM; -.
DR OrthoDB; 1631905at2759; -.
DR PhylomeDB; Q3UBX0; -.
DR TreeFam; TF332238; -.
DR BioGRID-ORCS; 68539; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tmem109; mouse.
DR PRO; PR:Q3UBX0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3UBX0; protein.
DR Bgee; ENSMUSG00000034659; Expressed in ascending aorta and 252 other tissues.
DR ExpressionAtlas; Q3UBX0; baseline and differential.
DR Genevisible; Q3UBX0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR039492; TMEM109.
DR PANTHER; PTHR14550; PTHR14550; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Ion channel;
KW Ion transport; Membrane; Nucleus; Reference proteome;
KW Sarcoplasmic reticulum; Signal; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..243
FT /note="Transmembrane protein 109"
FT /id="PRO_0000044619"
FT TOPO_DOM 34..83
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O77751"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O77751"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..185
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O77751"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O77751"
FT CONFLICT 159
FT /note="I -> V (in Ref. 1; BAE29844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 26306 MW; 31376625A07BF587 CRC64;
MAGAHSTPLW SRHLLKAVLM VLVALFLVHS ASAQSHREFA SPGQQKKETS ADILTQIGRS
LKEMLDTWLG PETMHVISET LLQVMWAISS AISVACFALS GIAAQLLSAL GLDGEQLTQG
LKLSPSQVQT LLLWGAAALV IYWLLSLLLG LVLALLGRIL GGLKLVLFVA GFVALVRSVP
DPSTRALMLL ALLTLFALLS RLTGSRSSGS HLEAKVRGLE RQIEELRGRQ RRAAKMPRSM
EEE
