TM38B_XENTR
ID TM38B_XENTR Reviewed; 284 AA.
AC Q28FA9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Trimeric intracellular cation channel type B;
DE Short=TRIC-B;
DE Short=TRICB;
DE AltName: Full=Transmembrane protein 38B;
GN Name=tmem38b; ORFNames=TEgg035c21.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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; CR762060; CAJ81929.1; -; mRNA.
DR EMBL; BC135582; AAI35583.1; -; mRNA.
DR RefSeq; NP_001016127.1; NM_001016127.3.
DR AlphaFoldDB; Q28FA9; -.
DR SMR; Q28FA9; -.
DR STRING; 8364.ENSXETP00000001972; -.
DR PaxDb; Q28FA9; -.
DR Ensembl; ENSXETT00000001972; ENSXETP00000001972; ENSXETG00000000907.
DR GeneID; 548881; -.
DR KEGG; xtr:548881; -.
DR CTD; 55151; -.
DR Xenbase; XB-GENE-5849692; tmem38b.
DR eggNOG; KOG3944; Eukaryota.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q28FA9; -.
DR OMA; KEIQRTH; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q28FA9; -.
DR TreeFam; TF313483; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000907; Expressed in mesonephros and 12 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"
FT /id="PRO_0000291530"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..32
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..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..139
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..157
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..196
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..204
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..225
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 250..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..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"
SQ SEQUENCE 284 AA; 31843 MW; 29F41C90D3E6DD38 CRC64;
MESFSELSLQ FSQLSMFPFF ETAHYLTSVM SAREQAGAVD VASRSPLASW FSSMLYCFGG
GILSSILLAE PPVGILSNTT SIILASAVWY MVYYFPYDLF YNCFFFLPIR LILAGMKEVT
RTWKILSGVA HAHSHYKDAM LVMITIGWAR GAGGGLISNF EQLVRGVWKP ESNEFLKMSY
PVKVTLIGAV LFTLQHGQYL PISRHNLMFI YTLFLILIKV TMMLTRSTAS PFLPLETSLQ
HILFSRQQIP AEVRESPSSS GDKGKPSKKT LDKDSGEQDN KKDN
