TM38B_RAT
ID TM38B_RAT Reviewed; 291 AA.
AC Q68FV1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC079336; AAH79336.1; -; mRNA.
DR RefSeq; NP_001014213.1; NM_001014191.1.
DR AlphaFoldDB; Q68FV1; -.
DR SMR; Q68FV1; -.
DR STRING; 10116.ENSRNOP00000033050; -.
DR PaxDb; Q68FV1; -.
DR PRIDE; Q68FV1; -.
DR Ensembl; ENSRNOT00000034570; ENSRNOP00000033050; ENSRNOG00000028063.
DR GeneID; 362521; -.
DR KEGG; rno:362521; -.
DR UCSC; RGD:1305703; rat.
DR CTD; 55151; -.
DR RGD; 1305703; Tmem38b.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q68FV1; -.
DR OMA; LPIAKHN; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q68FV1; -.
DR TreeFam; TF313483; -.
DR PRO; PR:Q68FV1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000028063; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q68FV1; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0071313; P:cellular response to caffeine; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0060487; P:lung epithelial cell differentiation; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:RGD.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:1903514; P:release of sequestered calcium ion into cytosol by endoplasmic reticulum; ISO:RGD.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0061033; P:secretion by lung epithelial cell involved in lung growth; ISO:RGD.
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..291
FT /note="Trimeric intracellular cation channel type B"
FT /id="PRO_0000291526"
FT TOPO_DOM 1..16
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..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..99
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..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..197
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..206
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..225
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 254..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..278
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"
SQ SEQUENCE 291 AA; 32445 MW; A2A821E0058EEE96 CRC64;
MEYPWDDLTL AFSRTSMFPF FDIAHYLVSV MALKQRPGAV AAAWSNPLSS WLSAMLHCFG
GGILSCILLA EPPLKFLTNH TNILLASSIW YIVFFCPRDL VSQGYSYQPI QLLAAGMKEV
TRTWKIVGGV AHANGYYRNG WIVMIAVGWA RGAGGAIITA CEQLLKGDWK PEGDEWLKMS
FPCKVTLLGS IMFTFQHTRH LAISKHDLMF LYTIFLVTIK VTMMMTKDAA VTLTPFEDTL
TRMLFGRQQQ QFSLSEKKAE VKPSSNGSAS SASKRGTEPP SSAKRHAKKE D
