ID   TM38A_XENLA             Reviewed;         295 AA.
AC   Q7ZY07;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Trimeric intracellular cation channel type A;
DE            Short=TRIC-A;
DE            Short=TRICA;
DE   AltName: Full=Transmembrane protein 38A;
GN   Name=tmem38a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q3TMP8}.
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   -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000305}.
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DR   EMBL; BC044031; AAH44031.1; -; mRNA.
DR   RefSeq; NP_001079534.1; NM_001086065.1.
DR   AlphaFoldDB; Q7ZY07; -.
DR   SMR; Q7ZY07; -.
DR   DNASU; 379221; -.
DR   GeneID; 379221; -.
DR   KEGG; xla:379221; -.
DR   CTD; 379221; -.
DR   Xenbase; XB-GENE-5802954; tmem38a.L.
DR   OMA; LQEAHWL; -.
DR   OrthoDB; 1319985at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 379221; Expressed in muscle tissue and 8 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR   GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007866; TRIC_channel.
DR   PANTHER; PTHR12454; PTHR12454; 1.
DR   Pfam; PF05197; TRIC; 1.
PE   2: Evidence at transcript 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..295
FT                   /note="Trimeric intracellular cation channel type A"
FT                   /id="PRO_0000291521"
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..84
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        85..105
FT                   /note="Helical;Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..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..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        202..222
FT                   /note="Helical;Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..233
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        234..254
FT                   /note="Helical;Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          258..295
FT                   /note="Disordered"
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"
SQ   SEQUENCE   295 AA;  33332 MW;  492AB4B48561D1D3 CRC64;
     MELLSALSLD DLAASFSKLP VFPLFDVAYY IISILYLKYE PGAVDLSKRS PVASWLCAML
     YCFGSYILAD VLLGESPIHY FSNNANILLA SAVWYLTFFC PLNIFYKIVS FLPVKLVLVG
     MKEVVRVRKI AMGIHHAHHH YHHGWVIMVL IGWVKGSGVA LMSNLEQLLR GVWKPETNEI
     LHMSFPTKAS LYGAILFTLQ QAHWLPISKA YLIFFFTLFM AVCKIYMTAT HSHGSPFAIF
     ESGICYVLFA AANGDHDDHG NHHHHHDDHD VSHSAGKSKE EHNEGTRKRK TKKAE