T38BA_XENLA
ID T38BA_XENLA Reviewed; 284 AA.
AC Q3KQE5; Q68FK1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Trimeric intracellular cation channel type B-A;
DE Short=TRIC-B-A;
DE Short=TRICB-A;
DE AltName: Full=Transmembrane protein 38B-A;
GN Name=tmem38b-a;
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=Oocyte, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) 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:Q9DAV9}.
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:0000250|UniProtKB:Q9DAV9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9DAV9}.
CC -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000305}.
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DR EMBL; BC079749; AAH79749.1; -; mRNA.
DR EMBL; BC106250; AAI06251.1; -; mRNA.
DR RefSeq; NP_001121148.1; NM_001127676.1.
DR AlphaFoldDB; Q3KQE5; -.
DR SMR; Q3KQE5; -.
DR MaxQB; Q3KQE5; -.
DR DNASU; 446269; -.
DR GeneID; 446269; -.
DR KEGG; xla:446269; -.
DR CTD; 446269; -.
DR Xenbase; XB-GENE-5849720; tmem38b.S.
DR OMA; LPIAKHN; -.
DR OrthoDB; 1319985at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 446269; Expressed in kidney and 19 other tissues.
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 InterPro; IPR007866; TRIC_channel.
DR PANTHER; PTHR12454; PTHR12454; 1.
DR Pfam; PF05197; TRIC; 1.
PE 2: Evidence at transcript 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..284
FT /note="Trimeric intracellular cation channel type B-A"
FT /id="PRO_0000291528"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..33
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..68
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..79
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..99
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 103..121
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..137
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..155
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 178..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..224
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 246..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
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 121
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 7
FT /note="L -> V (in Ref. 1; AAH79749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 31802 MW; A3AB3A8F6DBEFE1C CRC64;
MESLSELSVQ FSQLSMFPFF DMAHYVVSVM SAREQAGALD IAARSPMASW FSAMLYCFGG
GILSSILLAE PPIAVLSNTT NIMLASTIWY MVYYFPYDLF YNCFFFLPIR LIIAGMKEVT
RTWKILSGVT HAHSHYKDAL LVMITIGWAR GAGGGLISNF EQLVRGVWKP ESNEFLKMSY
PVKVTLIGAV LFTLQHGHYL PISRHNLMLI YTMFLVLIKV TMMLTHSTAS PFLPLETPLQ
RILFGQRQKP SEVRQSASSS GAKGKPSKKT LDKDSGEQSK KKDS
