ID   F4X2R1_ACREC            Unreviewed;       454 AA.
AC   F4X2R1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Small conductance calcium-activated potassium channel protein {ECO:0000313|EMBL:EGI59257.1};
GN   ORFNames=G5I_12592 {ECO:0000313|EMBL:EGI59257.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI59257.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; GL888591; EGI59257.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4X2R1; -.
DR   STRING; 103372.F4X2R1; -.
DR   eggNOG; KOG3684; Eukaryota.
DR   InParanoid; F4X2R1; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 2.
DR   InterPro; IPR004178; CaM-bd_dom.
DR   InterPro; IPR036122; CaM-bd_dom_sf.
DR   InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR10153; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL; 1.
DR   PANTHER; PTHR10153:SF33; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN; 1.
DR   Pfam; PF02888; CaMBD; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   Pfam; PF03530; SK_channel; 1.
DR   SMART; SM01053; CaMBD; 1.
DR   SUPFAM; SSF81327; Small-conductance potassium channel; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion channel {ECO:0000313|EMBL:EGI59257.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        67..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..291
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000259|SMART:SM01053"
FT   REGION          356..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          303..330
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        363..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50923 MW;  E45D9BA111A46756 CRC64;
     MIDNCADDWR IAMTWQRIAQ ISVELAICAI HPIPGEYYFL WTTKLANKNG DIGSKWVPYD
     VTLSLPMFLR LYLICRVMLL HSKLFTDASS RSIGALNRIN FNTRFVLKTL MTICPGTVLL
     VFMVSLWIIA SWTLRQCERF HDEEHANLLN AMWLIAITFL SVGFGDIVPN TYCGRGIAVS
     TGMMGAGCTA LLVAVVSRKL ELTRAEKHVH NFMMDTQLTK RLKNAAANVL RETWLIYKHT
     RLVKRVNPGR VRTHQRKFLL AIYALRKVKM DQRKLMDNAN TITDMAKTQN TVYEIVSDMS
     TRQDAVEERL VGLEDRLVGL EEKLTSLQGQ LELLPEELTR CLAQHAERME QRRNFLHPDT
     PHPLASLSNS PLLPHSRSVP SAPSTMSLHP WPVSPVLPPV SSRTPHLVPE TGRHHGLSHS
     ATVTTTSQSA TRLTSQAGMG GLGNSQGSDT SAHS
//