ID A0A0V0TXL5_9BILA Unreviewed; 800 AA.
AC A0A0V0TXL5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Small conductance calcium-activated potassium channel protein {ECO:0000313|EMBL:KRX43271.1};
GN Name=SK {ECO:0000313|EMBL:KRX43271.1};
GN ORFNames=T05_3817 {ECO:0000313|EMBL:KRX43271.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX43271.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX43271.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX43271.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX43271.1}.
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DR EMBL; JYDJ01000123; KRX43271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TXL5; -.
DR STRING; 144512.A0A0V0TXL5; -.
DR Proteomes; UP000055048; 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 Ion channel {ECO:0000313|EMBL:KRX43271.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
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 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 657..733
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000259|SMART:SM01053"
FT REGION 274..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89585 MW; 689B46C968ADDAA0 CRC64;
MHASMNSSRN KITIRCQFLL TWYASMKAIH TICLVVYKTK LIIIINVVVV VVVVVIIIII
MASHKSNLNR QQALKSCHSF GRICPVNNSS SSSKAAKTGH GCSSSTFTAT CSMDEGCGVV
GACSSGDLQA PVPAVGATTT VVDLNDVDGT VGGDSAEALD EGEGELLVKT TDNKLSALFK
GGNFSVDGHL RNRLQHAPQA LCHSADCIDG QYPDASNGLC PLCGRAATLV RRPMSPSSDA
RNAIYEVSND FIKLFGSKRQ YGLLLSGPVD LTTPDQQSHY PSRLSSDKSD QQLLQSGPAA
ATQTAPLMPR PPGNYLLPKR KSAYGVLWKD KQNWRQKLRT RKRLFYQRNK VCDLCLLFAL
AGILITVLEA ELTSHQFLLK NKQNICFLLE EYICKKINEG KWNFQFSEWE TAIFSQVLRS
IIVVTTVVLL FLILMYHATE ILVNDSDAQD WRVAVTWQRV AQATLELVVC AVCPIPGSVS
IPWSVLDKTH RKLLVTQVPL DTVLSMPMFF RFYLICRFMA LRSRQFRDAA TRSIAALNHI
SVNFTFVLKT LMHENPLRVL IIFTVFFWII MAWILRQCEQ FDTIEDQIKY MNSLWFIIIT
FMSIGYGDVT PHTYCGRTVA ISTGIVGAGV SSALIAVISR KLELSRSEKH VNNFMADSKL
ARERKHAAAA VLQHTWFIHK FRCLHFPRDE MKLRHHQKKF LAAITEFQRI KWEQRKVADE
SNALIDVAKL QSDMHEILFE MQRVQEFLVS KVDILMKQLD KLERTLTTGT GTGSNNAVLV
TAAASRREET LPGISIRLMS
//