T38B1_CAEEL
ID T38B1_CAEEL Reviewed; 295 AA.
AC Q9NA75;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Trimeric intracellular cation channel type 1B.1 {ECO:0000305};
DE Short=TRIC-1B.1 {ECO:0000305};
DE AltName: Full=TRIC-B1;
GN Name=tric-1B.1 {ECO:0000312|WormBase:Y57A10A.10};
GN ORFNames=Y57A10A.10 {ECO:0000312|WormBase:Y57A10A.10};
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:5EGI}
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 1-251 IN COMPLEX WITH PIP2,
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF
RP LYS-129; ARG-133 AND TRP-180.
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 (PubMed:27698420). Might be required for maintenance of rapid
CC intracellular calcium release (By similarity). May act as a counter-ion
CC channel that functions in synchronization with calcium release from
CC intracellular stores (By similarity). Binds phosphatidylinositol 4,5-
CC bisphosphate (PIP2) (PubMed:27698420). {ECO:0000250|UniProtKB:Q9DAV9,
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; CAB55030.2; -; Genomic_DNA.
DR RefSeq; NP_496603.2; NM_064202.2.
DR PDB; 5EGI; X-ray; 3.30 A; A/B/C=1-251.
DR PDBsum; 5EGI; -.
DR AlphaFoldDB; Q9NA75; -.
DR SMR; Q9NA75; -.
DR STRING; 6239.Y57A10A.10; -.
DR EPD; Q9NA75; -.
DR PaxDb; Q9NA75; -.
DR PeptideAtlas; Q9NA75; -.
DR EnsemblMetazoa; Y57A10A.10.1; Y57A10A.10.1; WBGene00013255.
DR GeneID; 174867; -.
DR KEGG; cel:CELE_Y57A10A.10; -.
DR UCSC; Y57A10A.10; c. elegans.
DR CTD; 174867; -.
DR WormBase; Y57A10A.10; CE44590; WBGene00013255; tric-1B.1.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_0_1; -.
DR InParanoid; Q9NA75; -.
DR OMA; WDAMSRA; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q9NA75; -.
DR PRO; PR:Q9NA75; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013255; Expressed in larva 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..295
FT /note="Trimeric intracellular cation channel type 1B.1"
FT /id="PRO_0000440241"
FT TOPO_DOM 1..27
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 28..45
FT /note="Helical;Name=1"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 46..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 57..80
FT /note="Discontinuously helical;Name=2"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 81..89
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 90..107
FT /note="Helical;Name=3"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 108..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 120..148
FT /note="Helical;Name=4"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 149..150
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 151..177
FT /note="Discontinuously helical;Name=5"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 178..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 189..210
FT /note="Helical;Name=6"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 211..215
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27698420"
FT TRANSMEM 216..239
FT /note="Helical;Name=7"
FT /evidence="ECO:0000269|PubMed:27698420"
FT TOPO_DOM 240..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27698420"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
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:0000269|PubMed:27698420,
FT ECO:0007744|PDB:5EGI"
FT BINDING 133
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:0000269|PubMed:27698420,
FT ECO:0007744|PDB:5EGI"
FT BINDING 166
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:5EGI"
FT MUTAGEN 129
FT /note="K->A: Abolishes PIP2 binding, impairs trimerization,
FT reduces potassium current and calcium-sensitivity; when
FT associated with L-133."
FT /evidence="ECO:0000269|PubMed:27698420"
FT MUTAGEN 133
FT /note="R->L: Abolishes PIP2 binding, impairs trimerization,
FT reduces potassium current and calcium-sensitivity; when
FT associated with A-129."
FT /evidence="ECO:0000269|PubMed:27698420"
FT MUTAGEN 180
FT /note="W->A: Abolishes calcium-sensitivity."
FT /evidence="ECO:0000269|PubMed:27698420"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 121..147
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:5EGI"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 190..209
FT /evidence="ECO:0007829|PDB:5EGI"
FT HELIX 217..238
FT /evidence="ECO:0007829|PDB:5EGI"
SQ SEQUENCE 295 AA; 32593 MW; 06355987AB7662AA CRC64;
MVVPESFQLD QEILLDAGAQ LHRLKMYPYF DVAHYLLMII EVRDDLGSAA SIFSRKHPLS
CWLSSMLMCF ADAFLANFLL GEPVIAPFKR HDDIILATII WYLVFYAPFD GIYKIAKITP
VKCVLAVMKE VKRAYKVSHG VSHAAKLYPN SYIVQVLVGT AKGAGSGIVR TLEQLVRGVW
LPTHNELLRP SFATKACVVA ASVLALEKSG TYLTAPHDLV YLVIVGFFVY FKLSAVILHV
TDPFAPIENL FCAIFMGGIW DAVSRALAAS RDRRAAGAHS NENGSSISTP EKKDQ
