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Database: UniProt
Entry: A0A383ZTZ1_BALAS
LinkDB: A0A383ZTZ1_BALAS
Original site: A0A383ZTZ1_BALAS 
ID   A0A383ZTZ1_BALAS        Unreviewed;       726 AA.
AC   A0A383ZTZ1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Small conductance calcium-activated potassium channel protein 3 isoform X1 {ECO:0000313|RefSeq:XP_007178541.1};
GN   Name=KCNN3 {ECO:0000313|RefSeq:XP_007178541.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007178541.1};
RN   [1] {ECO:0000313|RefSeq:XP_007178541.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007178541.1};
RG   RefSeq;
RL   Submitted (JAN-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   RefSeq; XP_007178541.1; XM_007178479.1.
DR   AlphaFoldDB; A0A383ZTZ1; -.
DR   STRING; 310752.A0A383ZTZ1; -.
DR   GeneID; 103017927; -.
DR   KEGG; bacu:103017927; -.
DR   CTD; 3782; -.
DR   InParanoid; A0A383ZTZ1; -.
DR   OrthoDB; 4200919at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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: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   PRINTS; PR01451; SKCHANNEL.
DR   SMART; SM01053; CaMBD; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion channel {ECO:0000313|RefSeq:XP_007178541.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
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        278..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        489..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          556..632
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000259|SMART:SM01053"
FT   REGION          1..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          637..664
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..65
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   726 AA;  80351 MW;  6A2A2796160C97D3 CRC64;
     MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQPPPPPP PPPPAPAPPA APQQPPGPPL
     QPQPPQLQQQ QQQQQPPHPL SQLAQLQSQP IHPGLLHSSP TAFRGPPSSN STAILHPSSR
     QGSQLNLNDH LLGHSPTSTA TSGPGGGGRH RQASPLVHRR DSNPFTEIAM SSCKYSGGVL
     HALSRLSASR RNLIEAEPEG QPLQLFSPSN PPEIVISSRE DNHAHQTLLH HPNAAHNHQH
     AGATASSTTF PKANKRKNQN IGYKLGHRRA LFEKRKRLSD YALIFGMFGI VVMVIETELS
     WGLYSKDSMF SLALKCLISL STIILLGLII AYHTREVQLF VIDNGADDWR IAMTYERILY
     ISLEMLVCAI HPIPGEYKFF WTARLAFSYT PSRAEADVDI ILSIPMFLRL YLIARVMLLH
     SKLFTDASSR SIGALNKINF NTRFVMKTLM TICPGTVLLV FSISLWIIAA WTVRVCERYH
     DQQDVTSNFL GAMWLISITF LSIGYGDMVP HTYCGKGVCL LTGIMGAGCT ALVVAVVARK
     LELTKAEKHV HNFMMDTQLT KRIKNAAANV LRETWLIYKH TKLLKKIDHA KVRKHQRKFL
     QAIHQLRSVK MEQRKLSDQA NTLVDLSKMQ NVMYDLITEL NDRSEDLEKQ IGSLESKLEH
     LTASVNSLPL LIADTLRQQQ RQFLSALTEA RGVSVAVGTT HTPLSDSPIG VSSTSFPTPY
     TSSSSC
//
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