TM38A_DANRE
ID TM38A_DANRE Reviewed; 295 AA.
AC Q6P2T0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Trimeric intracellular cation channel type A;
DE Short=TRIC-A;
DE Short=TRICA;
DE AltName: Full=Transmembrane protein 38A;
GN Name=tmem38a; ORFNames=zgc:77831;
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].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-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:Q3TMP8}.
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: Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane
CC {ECO:0000250|UniProtKB:A5A6S6}.
CC -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000305}.
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DR EMBL; BC064309; AAH64309.1; -; mRNA.
DR RefSeq; NP_957194.1; NM_200900.1.
DR AlphaFoldDB; Q6P2T0; -.
DR SMR; Q6P2T0; -.
DR STRING; 7955.ENSDARP00000037150; -.
DR PaxDb; Q6P2T0; -.
DR Ensembl; ENSDART00000035560; ENSDARP00000037150; ENSDARG00000024047.
DR GeneID; 393874; -.
DR KEGG; dre:393874; -.
DR CTD; 79041; -.
DR ZFIN; ZDB-GENE-040426-1888; tmem38a.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_1_1; -.
DR InParanoid; Q6P2T0; -.
DR OMA; LQEAHWL; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q6P2T0; -.
DR TreeFam; TF313483; -.
DR PRO; PR:Q6P2T0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000024047; Expressed in muscle tissue and 22 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 Ion channel; Ion transport; Membrane; Nucleus; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="Trimeric intracellular cation channel type A"
FT /id="PRO_0000291520"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..37
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..75
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..86
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..106
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..162
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..182
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..199
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..227
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..236
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..255
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 259..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Basic and acidic residues"
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 295 AA; 32951 MW; 938E391A3D68EFAE CRC64;
MEVLDVLNLG EIAQYFSKMA MFPVFDVAYY IVSILYLKYE PGAVEVSRRS PVASWLCAML
YCFGSYILAD IMLGVCPIDY FHNNSHILLA SAVWYLIFFC PLNLFYKCVA FMPVKLVLVA
LKEVVRTRKI AAGVHHAHHA YHHGWLIMVI TGYVKGSGVA LMSNFEQLLR GVWKPETNEV
LNMSFPTKAS LYGAILFTLQ EAHVLPVSKS TLICLFTLFM VSSKVFMTAR HSHGSPFALI
ESWVCHVLFG SPLGTEDAHD HHHAAPAAAP APLSPAKNKE ELSEGTRKRK SKKAE
