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Database: UniProt
Entry: A0A3Q3AFX9_KRYMA
LinkDB: A0A3Q3AFX9_KRYMA
Original site: A0A3Q3AFX9_KRYMA 
ID   A0A3Q3AFX9_KRYMA        Unreviewed;       684 AA.
AC   A0A3Q3AFX9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Small conductance calcium-activated potassium channel protein 1-like {ECO:0000313|Ensembl:ENSKMAP00000015523.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000015523.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000015523.1}
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   RefSeq; XP_017282352.1; XM_017426863.1.
DR   AlphaFoldDB; A0A3Q3AFX9; -.
DR   Ensembl; ENSKMAT00000015747.1; ENSKMAP00000015523.1; ENSKMAG00000011606.1.
DR   GeneID; 108242172; -.
DR   KEGG; kmr:108242172; -.
DR   GeneTree; ENSGT00950000182904; -.
DR   OrthoDB; 4200919at2759; -.
DR   Proteomes; UP000264800; 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   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:UP000264800};
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        261..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        437..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        498..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          536..612
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000259|SMART:SM01053"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  77488 MW;  02A174BDB6ACA92D CRC64;
     MDHSPSMTST VVDGDDLEDH RPLLPPRMVA PSQVYSPQCG IHHTVQTSID HTVWLDRTQA
     LATTPLYNGH LYVTATPRST RRREKIKSKE KKCEKRSGEC RQTPGPKERN HQSKAKGAGS
     NRLQEKVTSF TDVPISPCGS PFKGPPSRSN LDVRDVDGRG YRKSGNVSLE MHDRQSLPEI
     IITSKDENLQ QQNKASHYEQ RPGEAKGSLP GLERFSRSPG SSPQVSPKHK EDPQKDPYWR
     THNIGWRLVH RRALFLRRQR LNDSALAVGI FGVVMMVMET ELSWSIYSKS SIYSLTLKSV
     ISISTLLLLG LIMAYHCCEV QLYVHDIGAE DWRIAMTTDR IALIALELAV AAIHPYPVGL
     QAYFQKTPTR TTLSETELEI MLALPMFLRL YLLGRAMMLH SRLFTDTASR SIGALNKIHY
     NTRFVGKTLM TTYPGTVLMI FSVSLWIVAA WGLHVCERHH NYRDLSSNYM EALWMVSVTF
     LSIGYGDVVP HTYCGRSICL LTGIMGAGCT VLVVAVVARK LELTRAEKHV HNFMMDSHIS
     KRIKIAAANV LRETWLIYKH TKLSRERDHT RVRMHQRKLL LAIHQLRRVK MEKRILADQG
     NTLVDLCKMQ SLMYDTLAEV QGCRGELDSH IHSLEKHVEE LREGFRSLMP LLSSTLSTQN
     SSIRHLLRER EVKSECASAS GADK
//
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