TM38B_BOVIN
ID TM38B_BOVIN Reviewed; 291 AA.
AC Q0VC58;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC120345; AAI20346.1; -; mRNA.
DR RefSeq; NP_001069855.1; NM_001076387.1.
DR AlphaFoldDB; Q0VC58; -.
DR SMR; Q0VC58; -.
DR STRING; 9913.ENSBTAP00000005404; -.
DR PaxDb; Q0VC58; -.
DR PRIDE; Q0VC58; -.
DR Ensembl; ENSBTAT00000005404; ENSBTAP00000005404; ENSBTAG00000034867.
DR GeneID; 615646; -.
DR KEGG; bta:615646; -.
DR CTD; 55151; -.
DR VEuPathDB; HostDB:ENSBTAG00000034867; -.
DR VGNC; VGNC:36081; TMEM38B.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q0VC58; -.
DR OMA; LPIAKHN; -.
DR OrthoDB; 1319985at2759; -.
DR TreeFam; TF313483; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000034867; Expressed in biceps femoris and 108 other tissues.
DR ExpressionAtlas; Q0VC58; baseline and differential.
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 GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0071313; P:cellular response to caffeine; IEA:Ensembl.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IEA:Ensembl.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0061033; P:secretion by lung epithelial cell involved in lung growth; IEA:Ensembl.
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;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Trimeric intracellular cation channel type B"
FT /id="PRO_0000291523"
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..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..69
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..80
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..100
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..122
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..138
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..156
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..196
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..225
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 257..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
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 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 MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV0"
SQ SEQUENCE 291 AA; 32451 MW; 715BFC189236A749 CRC64;
MESPWNELTL AFSRTSMFPF FDIAHYLVSV MALKHQPGAA ALAWKNPLSS WFTAMLHCFG
GGILSCVLLA EPPLRFLANN TNILLASSIW YIAFFCPCDL ISQAYSFLPV QLLAAGMKEV
TRTWKIVGGV THANSYYKNG WIVMIAVGWA RGAGGSIITN FEQLVKGCWK PEAEEWLKMS
YPAKVTLLGS VIFTFQQTKY LAISKHNLMF LFTVFLVATK ITMMITKTAL VPFACFEDTL
SRMLFGWQQQ FSPCEKKSET KSSFNGTGSS TSKPVANASD KVKKKHSKKT E
