TM38A_CHICK
ID TM38A_CHICK Reviewed; 296 AA.
AC Q5ZK43;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=RCJMB04_13f15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720241; CAG31900.1; -; mRNA.
DR RefSeq; NP_001073226.1; NM_001079758.1.
DR PDB; 6IYU; X-ray; 2.20 A; A=1-296.
DR PDB; 6IYX; X-ray; 1.80 A; A=1-296.
DR PDB; 6IYZ; X-ray; 2.20 A; A=1-296.
DR PDB; 6IZ0; X-ray; 2.30 A; A=1-296.
DR PDB; 6IZ1; X-ray; 2.40 A; A=1-296.
DR PDB; 6IZF; X-ray; 2.00 A; A=1-296.
DR PDBsum; 6IYU; -.
DR PDBsum; 6IYX; -.
DR PDBsum; 6IYZ; -.
DR PDBsum; 6IZ0; -.
DR PDBsum; 6IZ1; -.
DR PDBsum; 6IZF; -.
DR AlphaFoldDB; Q5ZK43; -.
DR SMR; Q5ZK43; -.
DR STRING; 9031.ENSGALP00000005984; -.
DR GeneID; 771253; -.
DR KEGG; gga:771253; -.
DR CTD; 79041; -.
DR VEuPathDB; HostDB:geneid_771253; -.
DR eggNOG; KOG3944; Eukaryota.
DR InParanoid; Q5ZK43; -.
DR OrthoDB; 1319985at2759; -.
DR PhylomeDB; Q5ZK43; -.
DR PRO; PR:Q5ZK43; -.
DR Proteomes; UP000000539; 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; 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; Ion channel; Ion transport; Membrane; Nucleus; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..296
FT /note="Trimeric intracellular cation channel type A"
FT /id="PRO_0000271070"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..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..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..103
FT /note="Helical;Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..126
FT /note="Helical;Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..144
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..162
FT /note="Helical;Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..201
FT /note="Helical;Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..209
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 210..230
FT /note="Helical;Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 256..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..296
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"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 51..73
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 84..99
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 112..140
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:6IYX"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:6IYX"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:6IYX"
SQ SEQUENCE 296 AA; 33248 MW; 2DCB3D2A87525565 CRC64;
MELPGALQLG ELAAAFASVP VFPLFDAAYF IVSVLYLKYE PGAVEMSRKS PFASWLCAML
HCFGSYILAD LLLGESPIHY FSNNSSVILA TAVWYLIFFC PMNLFYKCVS FLPVKLIFVA
MKEVVRVRKI AAGVHHAHHQ YHHGWFIMMA TGWVKGSGVA LMSNFEQLLR GVWRPETNEI
LHMSFPTKAS LYGTVLFTLQ QTHWLPVSEA NLVFFFTMFM IVCKVFMTAT HSHASPFAPV
EGFICPVFFG SVSSGHTSHH NQHGHSHEAS YQPPPPVKSK EELNEGTRKR KAKKAE
