ID A0A3Q1AUI9_AMPOC Unreviewed; 553 AA.
AC A0A3Q1AUI9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Small conductance calcium-activated potassium channel protein 2-like {ECO:0000313|Ensembl:ENSAOCP00000004908.1};
GN Name=KCNN1 {ECO:0000313|Ensembl:ENSAOCP00000004908.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000004908.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000004908.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A3Q1AUI9; -.
DR STRING; 80972.ENSAOCP00000004908; -.
DR Ensembl; ENSAOCT00000007238.1; ENSAOCP00000004908.1; ENSAOCG00000008431.1.
DR GeneTree; ENSGT00950000182904; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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:SF38; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN 1; 1.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF03530; SK_channel; 1.
DR PRINTS; PR01451; SKCHANNEL.
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 Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
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 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 387..463
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000259|SMART:SM01053"
SQ SEQUENCE 553 AA; 62231 MW; DFF2B14F1CBDADF7 CRC64;
SNTLSLPKHS PLLFDTLETG DILNGDVVRP LSSHGTLRSS IADLHSSQQP LQLLHSTILE
DAFSKVIRED SSKTNSENMT REEGAVPQKK DFSYRLGQRR ALFGKRKQLS DYALVCGMFG
IVVMVIEIEL SREFYSKQSI YSYVLKGLIS LSTVILLGLI VMYHAREVQL FLVDNGAEDW
RIAMTFERIL FVGLELLICA IHPIPGQYVF TWTARLAFSY TASVADADVD IILSVPMFLR
LYLIGRVMLL HSKLFTDASS RSIGALNKIN FDTRFVMKTL MTICPGTVLL VFSVSCWIIA
AWTVRICERY HDAQEVTSTF LGAMWLISIT FLSIGYGDMV PHTYCGKGVC LLTGIMGAGC
TALVVAVVAR KSELTRAEKH VHNFMMDTQI YKKIKNTAAN VLRETWLIYK NTKLVKKIDR
ARVRHHQRKF LQAIHELRRV KLEQRKLTDQ ANTIADLAKT QNMMYDLVSE LQHRSGELDH
RIAALEEKLD SILLSVHSLP VALSQAITKL QKDFLDDLAC RVHFLSSSLS SECCSVPARQ
LCPGSTTPET PYS
//
