KCNA1_ONCMY
ID KCNA1_ONCMY Reviewed; 483 AA.
AC Q9I829;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Shaker-related potassium channel tsha2;
DE AltName: Full=Trout shaker 2;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9486764;
RX DOI=10.1002/(sici)1097-4547(19980201)51:3<284::aid-jnr2>3.0.co;2-c;
RA Nguyen T.-D., Jeserich G.;
RT "Molecular structure and expression of shaker type potassium channels in
RT glial cells of trout CNS.";
RL J. Neurosci. Res. 51:284-292(1998).
CC -!- FUNCTION: Mediates the voltage-dependent potassium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a potassium-selective channel through which potassium ions may
CC pass in accordance with their electrochemical gradient (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins. Binds PDZ
CC domains of dlg1, dlg2 and dlg4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in oligodendrocytes and astrocytes.
CC {ECO:0000269|PubMed:9486764}.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments. {ECO:0000250}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. {ECO:0000305}.
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DR EMBL; AF252302; AAF70088.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9I829; -.
DR SMR; Q9I829; -.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
DR GO; GO:0033270; C:paranode region of axon; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..483
FT /note="Shaker-related potassium channel tsha2"
FT /id="PRO_0000395617"
FT TOPO_DOM 1..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 440..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 371..376
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 481..483
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 426
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT LIPID 243
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 483 AA; 54956 MW; 68A78AECA4424956 CRC64;
MTVVSCEIQD ETVVVSPLYQ DDCDEERGDQ ECSERVVINI SGLRFETQLR TLSRFPTTLL
GDPRKRMRFF DPLRNEYFFD RNRPSFDAIL YYYQSGGKLR RPVNVTMDIF MEEMTFYEIE
EEAIDMFKED EGMIIEVERA MPDNEFQRQL WLLFEYPESS GPARMIAVVS VSVIVISIVI
FCLETLPQFR EDTSANLPLS NHHTTNGTTL HKKPNLFTDP FFMVETLCIV WFSFEFLVRF
LSCPSKPAFF KNAMNSIDIL AIAPYFITLG LELAEQQEAG SEQAMSLAIL RVIRLVRVFR
IFKLSRHSKG LQILGQTLHA SISELGLLIF FLLIGVILFS SAVYFAEADD PESGFSSIPA
AFWWAVVSMT TVGYGDMCPV TIGGKIVGSM CAIAGVLTIA LPVPVIVSNF NYFYHRERND
EETAVYTHVT CGQQNASFGE FKSTSDSRQS LTKSEDTEED SCETIRLTHF NPFEHYTGKL
TDV
