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Database: UniProt
Entry: A0A3B4V3L3_SERDU
LinkDB: A0A3B4V3L3_SERDU
Original site: A0A3B4V3L3_SERDU 
ID   A0A3B4V3L3_SERDU        Unreviewed;       714 AA.
AC   A0A3B4V3L3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Small conductance calcium-activated potassium channel protein 1-like {ECO:0000313|Ensembl:ENSSDUP00000025286.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000025286.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000025286.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3B4V3L3; -.
DR   Ensembl; ENSSDUT00000025750.1; ENSSDUP00000025286.1; ENSSDUG00000018270.1.
DR   GeneTree; ENSGT00950000182904; -.
DR   Proteomes; UP000261420; 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:SF40; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN 3; 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   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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        265..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        493..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        522..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          560..621
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000259|SMART:SM01053"
FT   REGION          110..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  80685 MW;  FEA78808A09BF266 CRC64;
     MVFKLYSVHL SNISLSLSLS LSLPSKRFGA SSPLNLLTME HSPSMNLSVV DGDEVEDQRP
     LLPLRMVPPP QACSPQCGIH HTVQTSADHT VWLDRTQAMA TSPLYNGQLY VASSPRSNRR
     GDKAKGKEKK CEKRSGGSKQ NKERNHQCKA KNTGSHRLQE KVTSFTDIPI SPCGSPFQGP
     CRSFVDVQDV EGRGRCRPGI VSLEMHDRQS LPEIIITSKD DDPQPHNETS HPKHKIDGKD
     DNYWKTHSIG WRLLRRRSLF LRRQRLSDCA LAVGIFGVVM MVMETELSWS VYSKVRDSIY
     SLALKSIISL STIILVGLII AYHCCEVQLY VHDIGAEDWR IAMTTERVAL IALELAAVAI
     HPYPVGLLAY FQHTTSRLSL SETELEIILA LPMFLRLYLL GRAMMLHSRL FTDTASRSIG
     ALNKIHFNTR FVGKTLMTNY PGTVLMIFSV SLWIVAAWGL HVCERPEKLN ISYENIFFHS
     FRHHNYRDLS SNYMEALWMV SVTFLSIGYG DVVPHTYCGR SICLLTGIMG AGCTVLVVAV
     VARKLELTRA EKHVHNFMMD SHISKRIKIA AANVLRETWL IYKHTKLSRE RDHTRVRMHQ
     RKLLLAIHHS NLIFPDAFSF SSPTWTCTHH CGQTTPPQMQ NLMCDVLSEV QGCRGELDSH
     IRCLEKHVEE LREGFKSLMP LLSSTLSTQN SSIRHLLRER EVKTEAASVS GGDR
//
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