TM38A_RAT
ID TM38A_RAT Reviewed; 297 AA.
AC A6ZIQ8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Trimeric intracellular cation channel type A;
DE Short=TRIC-A;
DE Short=TRICA;
DE AltName: Full=27 kDa sarcoplasmic reticulum protein;
DE AltName: Full=SPR-27;
DE AltName: Full=Transmembrane protein 38A;
GN Name=Tmem38a {ECO:0000250|UniProtKB:Q3TMP8};
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] {ECO:0000312|EMBL:ABR68564.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bleunven C., Treves S., Leo E., Ronjat M., De Waard M., Kern G.,
RA Flucher B.E., Zorzato F.;
RT "SPR-27 is a novel component of the supramolecular signaling complex
RT involved in skeletal muscle excitation-contraction coupling.";
RL Submitted (JUN-2007) 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:0000255}.
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DR EMBL; EF690436; ABR68564.1; -; mRNA.
DR RefSeq; NP_001093645.1; NM_001100175.1.
DR AlphaFoldDB; A6ZIQ8; -.
DR SMR; A6ZIQ8; -.
DR BioGRID; 258417; 2.
DR IntAct; A6ZIQ8; 1.
DR STRING; 10116.ENSRNOP00000059284; -.
DR PaxDb; A6ZIQ8; -.
DR PRIDE; A6ZIQ8; -.
DR GeneID; 306327; -.
DR KEGG; rno:306327; -.
DR UCSC; RGD:1307901; rat.
DR CTD; 79041; -.
DR RGD; 1307901; Tmem38a.
DR eggNOG; KOG3944; Eukaryota.
DR InParanoid; A6ZIQ8; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; A6ZIQ8; -.
DR PRO; PR:A6ZIQ8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005267; F:potassium channel activity; 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:0098662; P:inorganic cation transmembrane transport; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; 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:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
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..297
FT /note="Trimeric intracellular cation channel type A"
FT /id="PRO_0000309466"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical;Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..85
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..177
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 178..198
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..233
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 234..254
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 259..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..297
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 297 AA; 33276 MW; AEC3C1ED6542A12D CRC64;
MDLISSLSLG ELALSFSRVP LFPVFDLSYF IVSIIYLKYE PGSVELSRRH PVASWLCAML
HCFGSYILAD LLLGEPIIDY FSNSSSILLA SGVWYLIFFC PLDLFYKCVC FLPVKLIFVA
MKEVVRVRKI AVGIHHAHHY HHGWFIMIAT GWVKGSGVAL LSNLEQLLRG VWKPETNEIL
HMSFPTKASL YGAILFTLQQ TRWLPVSKAS LIFVFTMFMV SCKVFLTATH SHSSPFDVLE
GYICPVLFGA TWGGDHHHDN HGAPHGMGLG TQHSGLPAKA KEELSEGFRK KKTKKAD
