TM38A_MOUSE
ID TM38A_MOUSE Reviewed; 298 AA.
AC Q3TMP8; A5A6S4; A7LBB7; Q3TZB9; Q91WL2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Trimeric intracellular cation channel type A;
DE Short=TRIC-A;
DE Short=TRICA;
DE AltName: Full=27 kDa sarcoplasmic reticulum protein;
DE AltName: Full=Mitsugumin-33A;
DE AltName: Full=SPR-27;
DE AltName: Full=Transmembrane protein 38A;
GN Name=Tmem38a;
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, TOPOLOGY, TISSUE SPECIFICITY, AND
RP 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 [MRNA].
RC STRAIN=C57BL/6J;
RA Bleunven C., Treves S., Leo E., Ronjat M., De Waard M., Kern G.,
RA Flucher B.E., Zorzato F.;
RT "SPR-27 is a novel component of the supramolecular signaling complex
RT involved in skeletal muscle excitation-contraction coupling.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Inner ear;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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=Brain, and Heart;
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: Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane
CC {ECO:0000250|UniProtKB:A5A6S6}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart and striated
CC muscle. Also detected in brain, lung and kidney.
CC {ECO:0000269|PubMed:17611541}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable. Mice lacking Tmem38a and Tmem38b
CC show a weak heartbeat at E9.5 followed by loss of cardiomyocyte
CC viability and embryonic lethality around 10.5 dpc.
CC {ECO:0000269|PubMed:17611541}.
CC -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000305}.
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DR EMBL; AB261158; BAF62541.1; -; mRNA.
DR EMBL; EF988666; ABS17665.1; -; mRNA.
DR EMBL; AK157969; BAE34290.1; -; mRNA.
DR EMBL; AK165818; BAE38393.1; -; mRNA.
DR EMBL; BC014728; AAH14728.1; -; mRNA.
DR EMBL; BC024788; AAH24788.1; -; mRNA.
DR CCDS; CCDS22417.1; -.
DR RefSeq; NP_653117.1; NM_144534.1.
DR AlphaFoldDB; Q3TMP8; -.
DR SMR; Q3TMP8; -.
DR STRING; 10090.ENSMUSP00000034244; -.
DR TCDB; 1.A.62.1.1; the homotrimeric cation channel (tric) family.
DR iPTMnet; Q3TMP8; -.
DR PhosphoSitePlus; Q3TMP8; -.
DR EPD; Q3TMP8; -.
DR MaxQB; Q3TMP8; -.
DR PaxDb; Q3TMP8; -.
DR PeptideAtlas; Q3TMP8; -.
DR PRIDE; Q3TMP8; -.
DR ProteomicsDB; 259227; -.
DR Antibodypedia; 27435; 131 antibodies from 27 providers.
DR DNASU; 74166; -.
DR Ensembl; ENSMUST00000034244; ENSMUSP00000034244; ENSMUSG00000031791.
DR GeneID; 74166; -.
DR KEGG; mmu:74166; -.
DR UCSC; uc009mgi.2; mouse.
DR CTD; 79041; -.
DR MGI; MGI:1921416; Tmem38a.
DR VEuPathDB; HostDB:ENSMUSG00000031791; -.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_1_1; -.
DR InParanoid; Q3TMP8; -.
DR OMA; LQEAHWL; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q3TMP8; -.
DR TreeFam; TF313483; -.
DR BioGRID-ORCS; 74166; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q3TMP8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TMP8; protein.
DR Bgee; ENSMUSG00000031791; Expressed in interventricular septum and 234 other tissues.
DR ExpressionAtlas; Q3TMP8; baseline and differential.
DR Genevisible; Q3TMP8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; TAS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR GO; GO:0071313; P:cellular response to caffeine; IGI:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IGI:MGI.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA: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:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IGI:MGI.
DR InterPro; IPR007866; TRIC_channel.
DR PANTHER; PTHR12454; PTHR12454; 1.
DR Pfam; PF05197; TRIC; 1.
PE 1: Evidence at protein level;
KW Ion channel; Ion transport; Membrane; Nucleus; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Trimeric intracellular cation channel type A"
FT /id="PRO_0000271069"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..85
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..178
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 210..230
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..234
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 260..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 126
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 73
FT /note="L -> P (in Ref. 3; BAE38393)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="G -> S (in Ref. 2; ABS17665 and 3; BAE34290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33309 MW; F35559581DA80BD7 CRC64;
MDLMSALSLG ELALSFSRVP LFPVFDLSYF IVSIIYLKYE PGAVELSRRH PVASWLCAML
HCFGSYILAD LLLGEPIIDY FSNSSSILLA SGVWYLIFFC PLDLFYKCVC FLPVKLIFVA
MKEVVRVRKI AVGIHHAHHH YHHGWFIMIA TGWVKGSGVA LLSNVEQLLR GVWKPETNEI
LHMSFPTKAS LYGAILFTLQ QTRWLPVSKA SLIFVFTMFM VSCKVFLTAT HSHSSPFDIL
EGYICPVLFG ATWGGDHHHD NHGAPHGMGL GTQHSGLPAK AKEELGEGSR KKKTKKAD
