TM109_RABIT
ID TM109_RABIT Reviewed; 243 AA.
AC O77751;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Transmembrane protein 109;
DE AltName: Full=Mitsugumin-23;
DE Short=Mg23;
DE Flags: Precursor;
GN Name=TMEM109;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=9720923; DOI=10.1016/s0014-5793(98)00864-3;
RA Nishi M., Komazaki S., Iino M., Kanagawa K., Takeshima H.;
RT "Mitsugumin23, a novel transmembrane protein on endoplasmic reticulum and
RT nuclear membranes.";
RL FEBS Lett. 432:191-196(1998).
RN [2]
RP FUNCTION, SUBUNIT, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=21381722; DOI=10.1021/bi1019447;
RA Venturi E., Mio K., Nishi M., Ogura T., Moriya T., Pitt S.J., Okuda K.,
RA Kakizawa S., Sitsapesan R., Sato C., Takeshima H.;
RT "Mitsugumin 23 forms a massive bowl-shaped assembly and cation-conducting
RT channel.";
RL Biochemistry 50:2623-2632(2011).
CC -!- FUNCTION: May mediate cellular response to DNA damage by protecting
CC against ultraviolet C-induced cell death (By similarity). Can form
CC voltage-gated calcium and potassium channels in vitro
CC (PubMed:21381722). {ECO:0000250|UniProtKB:Q3UBX0,
CC ECO:0000250|UniProtKB:Q9BVC6, ECO:0000269|PubMed:21381722}.
CC -!- SUBUNIT: Homooligomer (PubMed:21381722). Interacts with CRYAB (By
CC similarity). {ECO:0000250|UniProtKB:Q9BVC6,
CC ECO:0000269|PubMed:21381722}.
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:9720923}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21381722}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:21381722}. Sarcoplasmic reticulum
CC membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21381722}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in skeletal, cardiac
CC and smooth muscle cells, in brain, including neuroglial cells, cerebral
CC cortex neurons and cerebellum, but not Purkinje cells. Also detected in
CC Paneth and Goblet cells of the small intestine (but not in the
CC epithelium), duodenal gland, pancreas, parotid gland, testis, thyroid
CC gland and adrenal gland, as well as in epidermis, choroid plexus,
CC ductus epididymidis, lymphocytes, fibroblasts, endothelial cells and
CC seminiferous epithelial cells (at protein level). Not detected in
CC mucous cells of the duodenal gland, in hepatocytes nor in uriniferous
CC tubules. {ECO:0000269|PubMed:9720923}.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; AB013721; BAA33366.1; -; mRNA.
DR RefSeq; NP_001075462.1; NM_001081993.1.
DR AlphaFoldDB; O77751; -.
DR STRING; 9986.ENSOCUP00000013488; -.
DR PRIDE; O77751; -.
DR GeneID; 100008604; -.
DR KEGG; ocu:100008604; -.
DR CTD; 79073; -.
DR eggNOG; ENOG502S0EJ; Eukaryota.
DR InParanoid; O77751; -.
DR OrthoDB; 1631905at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA: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; IEA:InterPro.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:InterPro.
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_0000044620"
FT TOPO_DOM 34..83
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21381722"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21381722"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..185
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21381722"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21381722"
SQ SEQUENCE 243 AA; 26146 MW; 89A0AB316F657D36 CRC64;
MAGSGSSAPW GKHLLHAVLM VLVALVLLHS ALAQSHRDFA PPGQQRREAP VDLLTQIGRS
VRETLDTWIG PETMHLISET LSQVMWAISS AISVAFFALS GIAAQLLTAL GLDGDHLTQG
LKLSPSQVQT FLLWGAGALV VYWLLSLLLG LVLAVLGRIL GGLKLVIFLA GFVALVRSVP
DPSTRALLLL ALLTLYALLS RLTGSRASGA QLEAKVRGLE RQVDELRWRQ RRAAKGARSV
EEE
