TM38A_RABIT
ID TM38A_RABIT Reviewed; 295 AA.
AC A5A6S6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Trimeric intracellular cation channel type A;
DE Short=TRIC-A;
DE Short=TRICA;
DE AltName: Full=Mitsugumin-33A;
DE AltName: Full=Transmembrane protein 38A;
GN Name=TMEM38A {ECO:0000250|UniProtKB:Q3TMP8};
GN Synonyms=MG33A {ECO:0000312|EMBL:BAF62543.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF62543.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17611541; DOI=10.1038/nature05928;
RA Yazawa M., Ferrante C., Feng J., Mio K., Ogura T., Zhang M., Lin P.-H.,
RA Pan Z., Komazaki S., Kato K., Nishi M., Zhao X., Weisleder N., Sato C.,
RA Ma J., Takeshima H.;
RT "TRIC channels are essential for Ca2+ handling in intracellular stores.";
RL Nature 448:78-82(2007).
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 ECO:0000269|PubMed:17611541}.
CC -!- SUBUNIT: Homotrimer (PubMed:17611541). Trimerization probably requires
CC binding to phosphatidylinositol 4,5-bisphosphate (PIP2) (By
CC similarity). {ECO:0000250|UniProtKB:Q9NA73,
CC ECO:0000269|PubMed:17611541}.
CC -!- INTERACTION:
CC A5A6S6; A5A6S6: TMEM38A; NbExp=3; IntAct=EBI-15646422, EBI-15646422;
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17611541}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17611541}. Nucleus membrane
CC {ECO:0000269|PubMed:17611541}.
CC -!- SIMILARITY: Belongs to the TMEM38 family. {ECO:0000255}.
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DR EMBL; AB261160; BAF62543.1; -; mRNA.
DR RefSeq; NP_001093439.1; NM_001099969.1.
DR AlphaFoldDB; A5A6S6; -.
DR SMR; A5A6S6; -.
DR DIP; DIP-60261N; -.
DR STRING; 9986.ENSOCUP00000010672; -.
DR GeneID; 100101583; -.
DR KEGG; ocu:100101583; -.
DR CTD; 79041; -.
DR eggNOG; KOG3944; Eukaryota.
DR InParanoid; A5A6S6; -.
DR OrthoDB; 1319985at2759; -.
DR Proteomes; UP000001811; Unplaced.
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; IPI:IntAct.
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 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_0000309465"
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..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..178
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 210..230
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..234
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 256..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; 32881 MW; C6898995BC411475 CRC64;
MELLSALSLG ELALSFSRVP LFPVFDLSYF IVSILYLKYE PGAVELSRRH PVASWLCAML
HCFGSYILAD LLLGEPLIDY FSNNSSILLA SAVWYLIFFC PLDLFYKCVC FLPVKLIFVA
MKEVVRVRKI AVGIHHAHHH YHHGWFIMIA TGWVKGSGVA LLSNVEQLLR GVWKPETNEI
LHMSFPTKAS LYGAILFTLQ QTRWLPVSKA SLIFIFTMFM VSCKVFLTAT HSHSSPFDVL
EAYVCPVLFG TGSGGDHPQD NHGAWPGGPP SGALATKSKE ELSEGSRKKK TKKAD
