T38B2_CAEEL
ID T38B2_CAEEL Reviewed; 313 AA.
AC Q9NA73;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Trimeric intracellular cation channel type 1B.2 {ECO:0000305};
DE Short=TRIC-1B.2 {ECO:0000305};
DE AltName: Full=TRIC-B2;
GN Name=tric-1B.2 {ECO:0000312|WormBase:Y57A10A.28};
GN ORFNames=Y57A10A.28 {ECO:0000312|WormBase:Y57A10A.28};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0007744|PDB:5EIK}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-252 IN COMPLEX WITH PIP2,
RP FUNCTION, SUBUNIT, AND TOPOLOGY.
RX PubMed=27698420; DOI=10.1038/nature19767;
RA Yang H., Hu M., Guo J., Ou X., Cai T., Liu Z.;
RT "Pore architecture of TRIC channels and insights into their gating
RT mechanism.";
RL Nature 538:537-541(2016).
CC -!- FUNCTION: Potassium channel that mediates transmembrane potassium
CC transport (By similarity). Might be required for maintenance of rapid
CC intracellular calcium release (By similarity). May act as a potassium
CC counter-ion channel that functions in synchronization with calcium
CC release from intracellular stores (By similarity). Binds
CC phosphatidylinositol 4,5-bisphosphate (PIP2) (PubMed:27698420).
CC {ECO:0000250|UniProtKB:Q9DAV9, ECO:0000250|UniProtKB:Q9NA75,
CC ECO:0000269|PubMed:27698420}.
CC -!- SUBUNIT: Homotrimer; trimerization probably requires binding to
CC phosphatidylinositol 4,5-bisphosphate (PIP2).
CC {ECO:0000269|PubMed:27698420}.
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; BX284602; CAB55033.2; -; Genomic_DNA.
DR PIR; T31650; T31650.
DR RefSeq; NP_496606.2; NM_064205.2.
DR PDB; 5EIK; X-ray; 2.30 A; A=1-252.
DR PDBsum; 5EIK; -.
DR AlphaFoldDB; Q9NA73; -.
DR SMR; Q9NA73; -.
DR STRING; 6239.Y57A10A.28; -.
DR TCDB; 1.A.62.1.4; the homotrimeric cation channel (tric) family.
DR EPD; Q9NA73; -.
DR PaxDb; Q9NA73; -.
DR PeptideAtlas; Q9NA73; -.
DR EnsemblMetazoa; Y57A10A.28.1; Y57A10A.28.1; WBGene00013268.
DR GeneID; 190342; -.
DR KEGG; cel:CELE_Y57A10A.28; -.
DR UCSC; Y57A10A.28; c. elegans.
DR CTD; 190342; -.
DR WormBase; Y57A10A.28; CE35686; WBGene00013268; tric-1B.2.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q9NA73; -.
DR OMA; LQEAHWL; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q9NA73; -.
DR PRO; PR:Q9NA73; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013268; Expressed in embryo and 3 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..313
FT /note="Trimeric intracellular cation channel type 1B.2"
FT /id="PRO_0000440242"
FT TOPO_DOM 1..28
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 29..48
FT /note="Helical;Name=1"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 49..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 58..82
FT /note="Discontinuously helical;Name=2"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 83..90
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 91..108
FT /note="Helical;Name=3"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 109..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 119..149
FT /note="Helical;Name=4"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 150..151
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 152..178
FT /note="Discontinuously helical;Name=5"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 179..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 193..210
FT /note="Helical;Name=6"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 211..216
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 217..239
FT /note="Helical;Name=7"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 240..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT BINDING 130
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:0007744|PDB:5EIK"
FT BINDING 134
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:0007744|PDB:5EIK"
FT BINDING 168
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:0007744|PDB:5EIK"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 120..148
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 194..209
FT /evidence="ECO:0007829|PDB:5EIK"
FT HELIX 218..238
FT /evidence="ECO:0007829|PDB:5EIK"
SQ SEQUENCE 313 AA; 35019 MW; 6133A84C0469798A CRC64;
MGWVPDEWSI DHDTLIDAGG YVQKLKLYPY FDAAHYVLTC LSVRHDLGPD AISFSRKHPF
SCWLSCMLMS FAGSFLSCFL LGEPIISPLK QHADILLGSI VWYLVFYSPF DVVFRLATWF
PVKLGLSVLK EVQRTHKIAA GVKHAVRIYP ESYLVQILVG VAKGAGSGVV KIVEQLARGT
WHPTNHEILR PSFTTKACVI ASIVFTLERH SMYVTAPHDL VYLCVVGFFI YFKLASLCLS
VHDVLMPIEN VLCAVFMGGI IDAFAKAVDA TKKAIHSNRV LSEEEILSKE REKVLKKKKL
LAQMSNGTDK KNN
