TM38A_BOVIN
ID TM38A_BOVIN Reviewed; 299 AA.
AC A4FV75;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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; BC123825; AAI23826.1; -; mRNA.
DR RefSeq; NP_001076932.1; NM_001083463.1.
DR AlphaFoldDB; A4FV75; -.
DR SMR; A4FV75; -.
DR STRING; 9913.ENSBTAP00000018099; -.
DR PaxDb; A4FV75; -.
DR Ensembl; ENSBTAT00000018099; ENSBTAP00000018099; ENSBTAG00000013614.
DR GeneID; 532775; -.
DR KEGG; bta:532775; -.
DR CTD; 79041; -.
DR VEuPathDB; HostDB:ENSBTAG00000013614; -.
DR VGNC; VGNC:36080; TMEM38A.
DR eggNOG; KOG3944; Eukaryota.
DR GeneTree; ENSGT00390000018845; -.
DR HOGENOM; CLU_076376_0_1_1; -.
DR InParanoid; A4FV75; -.
DR OMA; LQEAHWL; -.
DR OrthoDB; 1319985at2759; -.
DR TreeFam; TF313483; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000013614; Expressed in choroid plexus and 100 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:Ensembl.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0071313; P:cellular response to caffeine; IEA:Ensembl.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IEA:Ensembl.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
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..299
FT /note="Trimeric intracellular cation channel type A"
FT /id="PRO_0000291519"
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..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..73
FT /note="Helical;Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..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..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 256..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
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 299 AA; 33314 MW; 5D0F61AD1D6B0DCA CRC64;
MELLSALSLG ELALSFSRVP LFPVFDLSYF IVSILYLKYE PGAVELSRHH PMASWLCAML
HCFGSYILAD LLLGEPVIDY FSNNSSILLA SAVWYLIFFC PLDLFYKCVC FLPVKLIFVA
MKEVVRVRKI AVGIHHAHHH YHHGWFVMIA TGWVKGSGVT LMSNLEQLLR GVWKPETNEI
LHMSFPTKAS LYGAILFTLQ QTRWLPVSKA SLIFIFTMFM VSCKVFLTAT HSHSSPFDVL
EAYICPVLFG SASGGDHHHN NHGGSQGGSG PGSPHSPLPS KSKEELSEGS RKKKTKKAD
