ID   TM38B_DANRE             Reviewed;         289 AA.
AC   Q7ZVP8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=zgc:55815;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) 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: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; BC045460; AAH45460.1; -; mRNA.
DR   RefSeq; NP_956470.1; NM_200176.1.
DR   AlphaFoldDB; Q7ZVP8; -.
DR   SMR; Q7ZVP8; -.
DR   GeneID; 393145; -.
DR   KEGG; dre:393145; -.
DR   CTD; 55151; -.
DR   ZFIN; ZDB-GENE-040426-807; tmem38b.
DR   InParanoid; Q7ZVP8; -.
DR   OrthoDB; 1319985at2759; -.
DR   PhylomeDB; Q7ZVP8; -.
DR   PRO; PR:Q7ZVP8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..289
FT                   /note="Trimeric intracellular cation channel type B"
FT                   /id="PRO_0000291527"
FT   TOPO_DOM        1..18
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        19..36
FT                   /note="Helical;Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        50..73
FT                   /note="Helical;Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..85
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        86..103
FT                   /note="Helical;Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        108..125
FT                   /note="Helical;Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..144
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        145..162
FT                   /note="Helical;Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        184..201
FT                   /note="Helical;Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..210
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        211..230
FT                   /note="Helical;Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          260..289
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   289 AA;  32029 MW;  EA0CB9B8A1DE4BD8 CRC64;
     MDVFAFFNLN ELAFGLSKLP MFPYFDMAHY IISVMSLREQ PGALCVSQRS PLACWFSSML
     YCFGGAVLSA LMLADAPVAP LSNTTNLLLA TLMWYLVFYC PLDVVYSLAS LLPLRLVLTA
     MKEVTRTWKV LSGVSQAGSK YSDALFVMVA VGWAKGAGGG LISNFEQLVR GVWKPETNEL
     LKMSYPTKVT LLGAVVFSLQ QCRYLPIQTH HLTFIYTLFT VTNKTRMMLL GSSSHPLSSL
     ESFLYKTLFV RPLTDLSAEH THSKHNGSVP EPTTAQTHTK EAEASKKTN