T38BB_XENLA
ID T38BB_XENLA Reviewed; 284 AA.
AC Q6GN30;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Trimeric intracellular cation channel type B-B;
DE Short=TRIC-B-B;
DE Short=TRICB-B;
DE AltName: Full=Transmembrane protein 38B-B;
GN Name=tmem38b-b;
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;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC073691; AAH73691.1; -; mRNA.
DR RefSeq; NP_001086006.1; NM_001092537.1.
DR PDB; 6IZ3; X-ray; 3.79 A; A/B/C/D=1-284.
DR PDB; 6IZ4; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-284.
DR PDB; 6IZ5; X-ray; 3.70 A; A=1-284.
DR PDB; 6IZ6; X-ray; 3.29 A; A=1-284.
DR PDBsum; 6IZ3; -.
DR PDBsum; 6IZ4; -.
DR PDBsum; 6IZ5; -.
DR PDBsum; 6IZ6; -.
DR AlphaFoldDB; Q6GN30; -.
DR SMR; Q6GN30; -.
DR DNASU; 444435; -.
DR GeneID; 444435; -.
DR KEGG; xla:444435; -.
DR CTD; 444435; -.
DR Xenbase; XB-GENE-6255127; tmem38b.L.
DR OMA; KEIQRTH; -.
DR OrthoDB; 1319985at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 444435; Expressed in zone of skin 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 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..284
FT /note="Trimeric intracellular cation channel type B-B"
FT /id="PRO_0000291529"
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 251..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 HELIX 6..12
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 46..67
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 107..135
FT /evidence="ECO:0007829|PDB:6IZ4"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:6IZ4"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:6IZ4"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6IZ4"
FT HELIX 204..226
FT /evidence="ECO:0007829|PDB:6IZ4"
SQ SEQUENCE 284 AA; 31743 MW; A86A32F34BFA2798 CRC64;
MESLSEVSVQ FSQLSMFPFF DMAHYLASVM SAREQAGALD IASHSPMASW FSAMLHCFGG
GILSSILLAE PPVGILANTT NIMLASAIWY MVYYFPYDLF YNCFFFLPIR LIAAGMKEVT
RTWKILSGIT HAHSHYKDAW LVMITIGWAR GAGGGLISNF EQLVRGVWKP ESNEFLKMSY
PVKVTLIGAV LFTLQHGHYL PISRHNLMFI YTMFLVSIKV TMMLTHSAGS PFLPLETPLH
RILFGLRQNQ AEVRESPSSS GAKGKPSKKT LDKDSGEQSN KKDK
