TM38B_MOUSE
ID TM38B_MOUSE Reviewed; 292 AA.
AC Q9DAV9; A2AQG4; Q3U6M4; Q3UBM6; Q3UWS8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Trimeric intracellular cation channel type B;
DE Short=TRIC-B;
DE Short=TRICB;
DE AltName: Full=Mitsugumin-33B;
DE AltName: Full=Transmembrane protein 38B;
GN Name=Tmem38b; Synonyms=D4Ertd89e, Mg33b;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17611541; DOI=10.1038/nature05928;
RA Yazawa M., Ferrante C., Feng J., Mio K., Ogura T., Zhang M., Lin P.-H.,
RA Pan Z., Komazaki S., Kato K., Nishi M., Zhao X., Weisleder N., Sato C.,
RA Ma J., Takeshima H.;
RT "TRIC channels are essential for Ca2+ handling in intracellular stores.";
RL Nature 448:78-82(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, and Placenta;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, 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: Monovalent cation channel required for maintenance of rapid
CC intracellular calcium release. May act as a potassium counter-ion
CC channel that functions in synchronization with calcium release from
CC intracellular stores. {ECO:0000269|PubMed:17611541}.
CC -!- SUBUNIT: Homotrimer; trimerization probably requires binding to
CC phosphatidylinositol 4,5-bisphosphate (PIP2).
CC {ECO:0000250|UniProtKB:A5A6S6, ECO:0000250|UniProtKB:Q9NA73}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17611541}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17611541}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17611541}.
CC -!- DISRUPTION PHENOTYPE: Mice are neonatal lethal. Mice lacking Tmem38a
CC and Tmem38b show a weak heartbeat at E9.5 followed by loss of
CC cardiomyocyte viability and embryonic lethality around 10.5 dpc.
CC {ECO:0000269|PubMed:17611541}.
CC -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM21468.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB261159; BAF62542.1; -; mRNA.
DR EMBL; AK005479; BAB24068.1; -; mRNA.
DR EMBL; AK136131; BAE22836.1; -; mRNA.
DR EMBL; AK150377; BAE29509.1; -; mRNA.
DR EMBL; AK150892; BAE29938.1; -; mRNA.
DR EMBL; AK153075; BAE31700.1; -; mRNA.
DR EMBL; AL844585; CAM21467.1; -; Genomic_DNA.
DR EMBL; AL844585; CAM21468.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC011072; AAH11072.1; -; mRNA.
DR CCDS; CCDS18193.1; -.
DR RefSeq; NP_082329.1; NM_028053.2.
DR AlphaFoldDB; Q9DAV9; -.
DR SMR; Q9DAV9; -.
DR BioGRID; 206367; 5.
DR IntAct; Q9DAV9; 1.
DR MINT; Q9DAV9; -.
DR STRING; 10090.ENSMUSP00000030127; -.
DR TCDB; 1.A.62.1.2; the homotrimeric cation channel (tric) family.
DR PhosphoSitePlus; Q9DAV9; -.
DR SwissPalm; Q9DAV9; -.
DR EPD; Q9DAV9; -.
DR jPOST; Q9DAV9; -.
DR MaxQB; Q9DAV9; -.
DR PaxDb; Q9DAV9; -.
DR PeptideAtlas; Q9DAV9; -.
DR PRIDE; Q9DAV9; -.
DR ProteomicsDB; 259114; -.
DR Antibodypedia; 14850; 103 antibodies from 26 providers.
DR DNASU; 52076; -.
DR Ensembl; ENSMUST00000030127; ENSMUSP00000030127; ENSMUSG00000028420.
DR GeneID; 52076; -.
DR KEGG; mmu:52076; -.
DR UCSC; uc008sxh.2; mouse.
DR CTD; 55151; -.
DR MGI; MGI:1098718; Tmem38b.
DR VEuPathDB; HostDB:ENSMUSG00000028420; -.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q9DAV9; -.
DR OMA; LPIAKHN; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q9DAV9; -.
DR TreeFam; TF313483; -.
DR BioGRID-ORCS; 52076; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tmem38b; mouse.
DR PRO; PR:Q9DAV9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DAV9; protein.
DR Bgee; ENSMUSG00000028420; Expressed in gastrula and 214 other tissues.
DR ExpressionAtlas; Q9DAV9; baseline and differential.
DR Genevisible; Q9DAV9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0071313; P:cellular response to caffeine; IGI:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:MGI.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IGI:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:1903514; P:release of sequestered calcium ion into cytosol by endoplasmic reticulum; IMP:MGI.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IGI:MGI.
DR GO; GO:0061033; P:secretion by lung epithelial cell involved in lung growth; IMP:MGI.
DR InterPro; IPR007866; TRIC_channel.
DR PANTHER; PTHR12454; PTHR12454; 1.
DR Pfam; PF05197; TRIC; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..292
FT /note="Trimeric intracellular cation channel type B"
FT /id="PRO_0000291525"
FT TOPO_DOM 1..16
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..34
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..69
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..82
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..100
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..122
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..140
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..158
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..195
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..206
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..225
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 248..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9NA73"
FT BINDING 122
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9NA73"
FT CONFLICT 192
FT /note="M -> I (in Ref. 2; BAE22836)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="M -> I (in Ref. 2; BAE31700)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="E -> G (in Ref. 2; BAE29509/BAE29938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 32640 MW; DD958501F8CDE083 CRC64;
MEYPWDDLTL AFSRTSMFPF FDIAHYLVSV MALKQRPGAV AAAWNNPLAS WLSAMLHCFG
GGILSCMLLA ESPLKFLTNH TNILLASSIW YIVFFCPRDL VSQGYSYQPI QFLAAGMKEV
TRTWKIVGGV SDANSYYRNA WIVMIVVGWA RGAGGAVVTA CEQLLKGDWK PEGDEWLKMS
FPCKITLLGS IMFTFQHTRH LAISKHDLMF LYTIFLVTIK VTMMMTKDTA VTLTPFEDTL
TRMLFGRRQQ QQFSSSEKKT EVKPSSNGSA SSASKRGAEP SGGAKRHAKK ED
