KCNN3_HUMAN
ID KCNN3_HUMAN Reviewed; 731 AA.
AC Q9UGI6; B1ANX0; O43517; Q86VF9; Q8WXG7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Small conductance calcium-activated potassium channel protein 3;
DE Short=SK3;
DE Short=SKCa 3;
DE Short=SKCa3;
DE AltName: Full=KCa2.3;
GN Name=KCNN3; Synonyms=K3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND POLYMORPHISM OF POLY-GLN
RP REGION.
RX PubMed=9491810; DOI=10.1038/sj.mp.4000353;
RA Chandy K.G., Fantino E., Wittekindt O., Kalman K., Tong L.-L., Ho T.-H.,
RA Gutman G.A., Crocq M.-A., Ganguli R., Nimgaonkar V., Morris-Rosendahl D.J.,
RA Gargus J.J.;
RT "Isolation of a novel potassium channel gene hSKCa3 containing a
RT polymorphic CAG repeat: a candidate for schizophrenia and bipolar
RT disorder?";
RL Mol. Psychiatry 3:32-37(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-GLN-GLN-GLN-GLN-80
RP INS.
RA Terstappen G.C., Pula G., Chen M.X., Roncarati R.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Tomita H., Shakkottai V., Wulff H., Sun G., Potkin S.G., Bunney W.E.,
RA Chandy G.K., Gargus J.J.;
RT "Splice variants of small conductance calcium-activated potassium channel
RT gene, KCNN3/ SKCa3 cause dominant-negative suppression of SKCa currents.";
RL Am. J. Hum. Genet. 69S:569-569(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT
RP GLN-GLN-GLN-GLN-GLN-80 INS.
RX PubMed=11501944; DOI=10.1007/s100380170046;
RA Sun G., Tomita H., Shakkottai V.G., Gargus J.J.;
RT "Genomic organization and promoter analysis of human KCNN3 gene.";
RL J. Hum. Genet. 46:463-470(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=12808432; DOI=10.1038/sj.mp.4001271;
RA Tomita H., Shakkottai V.G., Gutman G.A., Sun G., Bunney W.E., Cahalan M.D.,
RA Chandy K.G., Gargus J.J.;
RT "Novel truncated isoform of SK3 potassium channel is a potent dominant-
RT negative regulator of SK currents: implications in schizophrenia.";
RL Mol. Psychiatry 8:524-535(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-485 AND HIS-516.
RX PubMed=20562108; DOI=10.1074/jbc.m110.110072;
RA Lamy C., Goodchild S.J., Weatherall K.L., Jane D.E., Liegeois J.F.,
RA Seutin V., Marrion N.V.;
RT "Allosteric block of KCa2 channels by apamin.";
RL J. Biol. Chem. 285:27067-27077(2010).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CALM1, INVOLVEMENT IN ZLS3,
RP VARIANTS ZLS3 GLU-269; ASP-350 AND CYS-436, CHARACTERIZATION OF VARIANTS
RP ZLS3 GLU-269; ASP-350 AND CYS-436, AND CHARACTERIZATION OF VARIANT LEU-450.
RX PubMed=31155282; DOI=10.1016/j.ajhg.2019.04.012;
RA Bauer C.K., Schneeberger P.E., Kortuem F., Altmueller J.,
RA Santos-Simarro F., Baker L., Keller-Ramey J., White S.M., Campeau P.M.,
RA Gripp K.W., Kutsche K.;
RT "Gain-of-function mutations in KCNN3 encoding the small-conductance Ca2+-
RT activated K+ channel SK3 cause Zimmermann-Laband syndrome.";
RL Am. J. Hum. Genet. 104:1139-1157(2019).
RN [11]
RP VARIANT LEU-450.
RX PubMed=26658685; DOI=10.1016/j.jhep.2015.11.027;
RA Koot B.G., Alders M., Verheij J., Beuers U., Cobben J.M.;
RT "A de novo mutation in KCNN3 associated with autosomal dominant idiopathic
RT non-cirrhotic portal hypertension.";
RL J. Hepatol. 64:974-977(2016).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:31155282, PubMed:20562108). Activation is
CC followed by membrane hyperpolarization (By similarity). Thought to
CC regulate neuronal excitability by contributing to the slow component of
CC synaptic afterhyperpolarization (By similarity).
CC {ECO:0000250|UniProtKB:P70605, ECO:0000269|PubMed:20562108,
CC ECO:0000269|PubMed:31155282}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin.
CC {ECO:0000269|PubMed:20562108, ECO:0000269|PubMed:31155282}.
CC -!- SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits
CC each of which binds to a calmodulin subunit which regulates the channel
CC activity through calcium-binding (By similarity). Interacts with CALM1
CC (PubMed:31155282). {ECO:0000250, ECO:0000269|PubMed:31155282}.
CC -!- INTERACTION:
CC Q9UGI6-2; P51798: CLCN7; NbExp=3; IntAct=EBI-17888181, EBI-4402346;
CC Q9UGI6-2; P50402: EMD; NbExp=3; IntAct=EBI-17888181, EBI-489887;
CC Q9UGI6-2; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-17888181, EBI-10976398;
CC Q9UGI6-2; Q9H115: NAPB; NbExp=3; IntAct=EBI-17888181, EBI-3921185;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UGI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGI6-2; Sequence=VSP_039461, VSP_039462;
CC Name=3; Synonyms=SK3-1B;
CC IsoId=Q9UGI6-3; Sequence=VSP_047641;
CC -!- POLYMORPHISM: The second poly-Gln region of KCNN3 is highly polymorphic
CC and the number of Gln varies from 12 to 28 in the population.
CC {ECO:0000269|PubMed:9491810}.
CC -!- DISEASE: Zimmermann-Laband syndrome 3 (ZLS3) [MIM:618658]: A form of
CC Zimmermann-Laband syndrome, a rare developmental disorder characterized
CC by facial dysmorphism with bulbous nose and thick floppy ears, gingival
CC enlargement, hypoplasia or aplasia of terminal phalanges and nails,
CC hypertrichosis, joint hyperextensibility, and hepatosplenomegaly. Some
CC patients manifest intellectual disability with or without epilepsy.
CC ZLS3 inheritance is autosomal dominant. {ECO:0000269|PubMed:31155282}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Do not produce functional channels, but
CC selectively suppresses endogenous SK3 currents, in a dominant-negative
CC fashion. This dominant inhibitory effect extends to other members of
CC the SK subfamily. Widely distributed in human tissues and is present at
CC 20-60% of SK3 in the brain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.3/KCNN3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF031815; AAC26099.1; -; mRNA.
DR EMBL; AJ251016; CAB61331.1; -; mRNA.
DR EMBL; AF438203; AAL40801.1; -; mRNA.
DR EMBL; AF336797; AAK15345.1; -; Genomic_DNA.
DR EMBL; AY138900; AAN46636.1; -; mRNA.
DR EMBL; AL390204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53180.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53182.1; -; Genomic_DNA.
DR EMBL; BC042147; AAH42147.1; -; mRNA.
DR CCDS; CCDS1072.1; -. [Q9UGI6-2]
DR CCDS; CCDS30880.1; -. [Q9UGI6-1]
DR RefSeq; NP_001191016.1; NM_001204087.1.
DR RefSeq; NP_002240.3; NM_002249.5. [Q9UGI6-1]
DR RefSeq; NP_740752.1; NM_170782.2. [Q9UGI6-2]
DR AlphaFoldDB; Q9UGI6; -.
DR SMR; Q9UGI6; -.
DR BioGRID; 109983; 10.
DR IntAct; Q9UGI6; 4.
DR STRING; 9606.ENSP00000481848; -.
DR BindingDB; Q9UGI6; -.
DR ChEMBL; CHEMBL3381; -.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB16733; Rimtuzalcap.
DR DrugBank; DB09089; Trimebutine.
DR DrugCentral; Q9UGI6; -.
DR GuidetoPHARMACOLOGY; 383; -.
DR TCDB; 1.A.1.16.7; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q9UGI6; -.
DR PhosphoSitePlus; Q9UGI6; -.
DR BioMuta; KCNN3; -.
DR DMDM; 17367120; -.
DR EPD; Q9UGI6; -.
DR jPOST; Q9UGI6; -.
DR MassIVE; Q9UGI6; -.
DR MaxQB; Q9UGI6; -.
DR PaxDb; Q9UGI6; -.
DR PeptideAtlas; Q9UGI6; -.
DR PRIDE; Q9UGI6; -.
DR ProteomicsDB; 70008; -.
DR ProteomicsDB; 84216; -. [Q9UGI6-1]
DR ProteomicsDB; 84217; -. [Q9UGI6-2]
DR Antibodypedia; 20402; 177 antibodies from 28 providers.
DR DNASU; 3782; -.
DR Ensembl; ENST00000271915.9; ENSP00000271915.3; ENSG00000143603.19. [Q9UGI6-1]
DR Ensembl; ENST00000358505.2; ENSP00000351295.2; ENSG00000143603.19. [Q9UGI6-3]
DR Ensembl; ENST00000361147.8; ENSP00000354764.4; ENSG00000143603.19. [Q9UGI6-2]
DR GeneID; 3782; -.
DR KEGG; hsa:3782; -.
DR MANE-Select; ENST00000271915.9; ENSP00000271915.3; NM_002249.6; NP_002240.3.
DR UCSC; uc001ffo.4; human. [Q9UGI6-1]
DR CTD; 3782; -.
DR DisGeNET; 3782; -.
DR GeneCards; KCNN3; -.
DR HGNC; HGNC:6292; KCNN3.
DR HPA; ENSG00000143603; Tissue enriched (brain).
DR MalaCards; KCNN3; -.
DR MIM; 602983; gene.
DR MIM; 618658; phenotype.
DR neXtProt; NX_Q9UGI6; -.
DR OpenTargets; ENSG00000143603; -.
DR Orphanet; 3473; Zimmermann-Laband syndrome.
DR PharmGKB; PA30072; -.
DR VEuPathDB; HostDB:ENSG00000143603; -.
DR eggNOG; KOG3684; Eukaryota.
DR GeneTree; ENSGT00950000182904; -.
DR HOGENOM; CLU_014617_5_0_1; -.
DR InParanoid; Q9UGI6; -.
DR OrthoDB; 907751at2759; -.
DR PhylomeDB; Q9UGI6; -.
DR TreeFam; TF315015; -.
DR PathwayCommons; Q9UGI6; -.
DR Reactome; R-HSA-1296052; Ca2+ activated K+ channels.
DR SignaLink; Q9UGI6; -.
DR SIGNOR; Q9UGI6; -.
DR BioGRID-ORCS; 3782; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; KCNN3; human.
DR GeneWiki; SK3; -.
DR GenomeRNAi; 3782; -.
DR Pharos; Q9UGI6; Tchem.
DR PRO; PR:Q9UGI6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UGI6; protein.
DR Bgee; ENSG00000143603; Expressed in lateral globus pallidus and 169 other tissues.
DR ExpressionAtlas; Q9UGI6; baseline and differential.
DR Genevisible; Q9UGI6; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
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; PTHR10153; 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; SSF81327; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Disease variant; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..731
FT /note="Small conductance calcium-activated potassium
FT channel protein 3"
FT /id="PRO_0000155013"
FT TRANSMEM 288..308
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 494..514
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..637
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 709..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58391"
FT VAR_SEQ 1..313
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12808432"
FT /id="VSP_047641"
FT VAR_SEQ 1..305
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_039461"
FT VAR_SEQ 306..310
FT /note="WGLYS -> MERPI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_039462"
FT VARIANT 80
FT /note="Q -> QQQQQQ"
FT /id="VAR_081088"
FT VARIANT 269
FT /note="K -> E (in ZLS3; gain-of-function variant leading to
FT increased channel sensitivity to calcium and faster channel
FT activation; does not affect interaction with CALM1;
FT dbSNP:rs1571353663)"
FT /evidence="ECO:0000269|PubMed:31155282"
FT /id="VAR_083434"
FT VARIANT 350
FT /note="G -> D (in ZLS3; gain-of-function variant leading to
FT increased channel sensitivity to calcium and faster channel
FT activation; does not affect interaction with CALM1;
FT dbSNP:rs1571260285)"
FT /evidence="ECO:0000269|PubMed:31155282"
FT /id="VAR_083435"
FT VARIANT 436
FT /note="S -> C (in ZLS3; gain-of-function variant leading to
FT increased channel sensitivity to calcium and faster channel
FT activation; does not affect interaction with CALM1;
FT dbSNP:rs1571259807)"
FT /evidence="ECO:0000269|PubMed:31155282"
FT /id="VAR_083436"
FT VARIANT 450
FT /note="V -> L (found in a family with non-cirrhotic portal
FT hypertension; unknown pathological significance; gain-of-
FT function variant leading to constitutive activity with very
FT low calcium levels; does not affect interaction with
FT CALM1)"
FT /evidence="ECO:0000269|PubMed:26658685,
FT ECO:0000269|PubMed:31155282"
FT /id="VAR_083437"
FT MUTAGEN 485
FT /note="H->N: Reduced inhibition by apamin."
FT /evidence="ECO:0000269|PubMed:20562108"
FT MUTAGEN 516
FT /note="H->N: No effect on inhibition by apamin."
FT /evidence="ECO:0000269|PubMed:20562108"
FT CONFLICT 249
FT /note="T -> A (in Ref. 1; AAC26099)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="L -> P (in Ref. 1; AAC26099)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="V -> A (in Ref. 1; AAC26099)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="V -> A (in Ref. 1; AAC26099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 81385 MW; 02E5E79D7EAAAC29 CRC64;
MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQQQQQQQ QPPPPAPPAA PQQPLGPSLQ
PQPPQLQQQQ QQQQQQQQQQ PPHPLSQLAQ LQSQPVHPGL LHSSPTAFRA PPSSNSTAIL
HPSSRQGSQL NLNDHLLGHS PSSTATSGPG GGSRHRQASP LVHRRDSNPF TEIAMSSCKY
SGGVMKPLSR LSASRRNLIE AETEGQPLQL FSPSNPPEIV ISSREDNHAH QTLLHHPNAT
HNHQHAGTTA SSTTFPKANK RKNQNIGYKL GHRRALFEKR KRLSDYALIF GMFGIVVMVI
ETELSWGLYS KDSMFSLALK CLISLSTIIL LGLIIAYHTR EVQLFVIDNG ADDWRIAMTY
ERILYISLEM LVCAIHPIPG EYKFFWTARL AFSYTPSRAE ADVDIILSIP MFLRLYLIAR
VMLLHSKLFT DASSRSIGAL NKINFNTRFV MKTLMTICPG TVLLVFSISL WIIAAWTVRV
CERYHDQQDV TSNFLGAMWL ISITFLSIGY GDMVPHTYCG KGVCLLTGIM GAGCTALVVA
VVARKLELTK AEKHVHNFMM DTQLTKRIKN AAANVLRETW LIYKHTKLLK KIDHAKVRKH
QRKFLQAIHQ LRSVKMEQRK LSDQANTLVD LSKMQNVMYD LITELNDRSE DLEKQIGSLE
SKLEHLTASF NSLPLLIADT LRQQQQQLLS AIIEARGVSV AVGTTHTPIS DSPIGVSSTS
FPTPYTSSSS C
