ID   KCNN2_HUMAN             Reviewed;         579 AA.
AC   Q9H2S1; A6NF94; Q0VFZ4; Q6PJI0; Q6X2Y2;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Small conductance calcium-activated potassium channel protein 2;
DE            Short=SK2;
DE            Short=SKCa 2;
DE            Short=SKCa2;
DE   AltName: Full=KCa2.2;
GN   Name=KCNN2;
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), FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=10991935; DOI=10.1074/jbc.m001562200;
RA   Desai R., Peretz A., Idelson H., Lazarovici P., Attali B.;
RT   "Ca2+-activated K+ channels in human leukemic Jurkat T cells. Molecular
RT   cloning, biochemical and functional characterization.";
RL   J. Biol. Chem. 275:39954-39963(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=13679367; DOI=10.1074/jbc.m307508200;
RA   Xu Y., Tuteja D., Zhang Z., Xu D., Zhang Y., Rodriguez J., Nie L.,
RA   Tuxson H.R., Young J.N., Glatter K.A., Vazquez A.E., Yamoah E.N.,
RA   Chiamvimonvat N.;
RT   "Molecular identification and functional roles of a Ca(2+)-activated K+
RT   channel in human and mouse hearts.";
RL   J. Biol. Chem. 278:49085-49094(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Myometrium;
RA   Mazzone J.N., Kaiser R.A., Buxton I.L.O.;
RT   "Characterization of calcium-activated potassium channels in human
RT   myometrium.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Skin;
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   [8]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=9287325; DOI=10.1074/jbc.272.37.23195;
RA   Ishii T.M., Maylie J., Adelman J.P.;
RT   "Determinants of apamin and d-tubocurarine block in SK potassium
RT   channels.";
RL   J. Biol. Chem. 272:23195-23200(1997).
RN   [9]
RP   INVOLVEMENT IN NEDMAB, VARIANTS NEDMAB GLN-30; 160-TYR--SER-579 DEL;
RP   SER-288; LEU-321 DEL; MET-359; CYS-361; SER-362; VAL-388 AND PRO-432,
RP   CHARACTERIZATION OF VARIANTS NEDMAB GLN-30; LEU-321 DEL; MET-359; CYS-361;
RP   SER-362; VAL-388 AND PRO-432, AND FUNCTION.
RX   PubMed=33242881; DOI=10.1093/brain/awaa346;
RA   Mochel F., Rastetter A., Ceulemans B., Platzer K., Yang S., Shinde D.N.,
RA   Helbig K.L., Lopergolo D., Mari F., Renieri A., Benetti E., Canitano R.,
RA   Waisfisz Q., Plomp A.S., Huisman S.A., Wilson G.N., Cathey S.S.,
RA   Louie R.J., Gaudio D.D., Waggoner D., Kacker S., Nugent K.M., Roeder E.R.,
RA   Bruel A.L., Thevenon J., Ehmke N., Horn D., Holtgrewe M., Kaiser F.J.,
RA   Kamphausen S.B., Abou Jamra R., Weckhuysen S., Dalle C., Depienne C.;
RT   "Variants in the SK2 channel gene (KCNN2) lead to dominant
RT   neurodevelopmental movement disorders.";
RL   Brain 143:3564-3573(2020).
RN   [10]
RP   INVOLVEMENT IN DYT34, AND VARIANT DYT34 GLU-371.
RX   PubMed=32212350; DOI=10.1111/ene.14228;
RA   Balint B., Guerreiro R., Carmona S., Dehghani N., Latorre A., Cordivari C.,
RA   Bhatia K.P., Bras J.;
RT   "KCNN2 mutation in autosomal-dominant tremulous myoclonus-dystonia.";
RL   Eur. J. Neurol. 27:1471-1477(2020).
CC   -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC       intracellular calcium (PubMed:10991935, PubMed:9287325,
CC       PubMed:33242881). Activation is followed by membrane hyperpolarization.
CC       Thought to regulate neuronal excitability by contributing to the slow
CC       component of synaptic afterhyperpolarization.
CC       {ECO:0000269|PubMed:10991935, ECO:0000269|PubMed:32212350,
CC       ECO:0000269|PubMed:9287325}.
CC   -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin
CC       (PubMed:10991935, PubMed:9287325). Inhibited by UCL 1684 and
CC       tetraethylammonium (TEA) (By similarity).
CC       {ECO:0000250|UniProtKB:P70604, ECO:0000269|PubMed:10991935,
CC       ECO:0000269|PubMed:9287325}.
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).
CC       {ECO:0000250|UniProtKB:P70604}.
CC   -!- INTERACTION:
CC       Q9H2S1; P35609: ACTN2; NbExp=3; IntAct=EBI-6658875, EBI-77797;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H2S1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H2S1-2; Sequence=VSP_044584;
CC   -!- TISSUE SPECIFICITY: Expressed in atrial myocytes (at protein level).
CC       Widely expressed. {ECO:0000269|PubMed:13679367}.
CC   -!- DISEASE: Dystonia 34, myoclonic (DYT34) [MIM:619724]: A form of
CC       dystonia, a disorder defined by the presence of sustained involuntary
CC       muscle contraction, often leading to abnormal postures. DYT34 is an
CC       autosomal dominant form characterized by childhood-onset dystonia
CC       predominantly affecting hands and neck, with a fast tremor with
CC       superimposed myoclonus and, in some individuals, subtle cerebellar
CC       signs. {ECO:0000269|PubMed:32212350}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Neurodevelopmental disorder with or without variable movement
CC       or behavioral abnormalities (NEDMAB) [MIM:619725]: An autosomal
CC       dominant disorder characterized by motor and language developmental
CC       delay, intellectual disability often associated with early-onset
CC       movement disorders comprising cerebellar ataxia and/or extrapyramidal
CC       symptoms. Other variable features include autism spectrum disorder or
CC       autistic features and epilepsy. {ECO:0000269|PubMed:33242881}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.2/KCNN2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF239613; AAG16728.1; -; mRNA.
DR   EMBL; AY258141; AAP45946.1; -; mRNA.
DR   EMBL; AF397175; AAK84039.1; -; mRNA.
DR   EMBL; AK289948; BAF82637.1; -; mRNA.
DR   EMBL; AC025761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471086; EAW48975.1; -; Genomic_DNA.
DR   EMBL; CH471086; EAW48976.1; -; Genomic_DNA.
DR   EMBL; BC015371; AAH15371.1; -; mRNA.
DR   EMBL; BC117454; AAI17455.1; -; mRNA.
DR   EMBL; BC117456; AAI17457.1; -; mRNA.
DR   CCDS; CCDS43352.1; -. [Q9H2S1-2]
DR   RefSeq; NP_001265133.1; NM_001278204.1.
DR   RefSeq; NP_067627.2; NM_021614.3.
DR   RefSeq; NP_740721.1; NM_170775.2. [Q9H2S1-2]
DR   PDB; 5V02; X-ray; 1.78 A; B=395-486.
DR   PDB; 5WBX; X-ray; 1.90 A; B=395-486.
DR   PDB; 5WC5; X-ray; 2.30 A; B=395-486.
DR   PDB; 6ALE; X-ray; 2.50 A; B=394-486.
DR   PDBsum; 5V02; -.
DR   PDBsum; 5WBX; -.
DR   PDBsum; 5WC5; -.
DR   PDBsum; 6ALE; -.
DR   AlphaFoldDB; Q9H2S1; -.
DR   BMRB; Q9H2S1; -.
DR   SMR; Q9H2S1; -.
DR   BioGRID; 109982; 7.
DR   DIP; DIP-48997N; -.
DR   IntAct; Q9H2S1; 4.
DR   STRING; 9606.ENSP00000264773; -.
DR   BindingDB; Q9H2S1; -.
DR   ChEMBL; CHEMBL4469; -.
DR   DrugBank; DB02587; Colforsin.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB01054; Nitrendipine.
DR   DrugBank; DB00721; Procaine.
DR   DrugBank; DB16733; Rimtuzalcap.
DR   DrugBank; DB00867; Ritodrine.
DR   DrugBank; DB09089; Trimebutine.
DR   DrugCentral; Q9H2S1; -.
DR   GuidetoPHARMACOLOGY; 382; -.
DR   TCDB; 1.A.1.16.1; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; Q9H2S1; -.
DR   PhosphoSitePlus; Q9H2S1; -.
DR   SwissPalm; Q9H2S1; -.
DR   BioMuta; KCNN2; -.
DR   DMDM; 209572638; -.
DR   EPD; Q9H2S1; -.
DR   jPOST; Q9H2S1; -.
DR   MassIVE; Q9H2S1; -.
DR   MaxQB; Q9H2S1; -.
DR   PaxDb; 9606-ENSP00000427120; -.
DR   PeptideAtlas; Q9H2S1; -.
DR   ProteomicsDB; 67208; -.
DR   ProteomicsDB; 80583; -. [Q9H2S1-1]
DR   ABCD; Q9H2S1; 1 sequenced antibody.
DR   Antibodypedia; 13591; 153 antibodies from 30 providers.
DR   DNASU; 3781; -.
DR   Ensembl; ENST00000503706.5; ENSP00000421439.1; ENSG00000080709.17. [Q9H2S1-2]
DR   GeneID; 3781; -.
DR   KEGG; hsa:3781; -.
DR   UCSC; uc003kqo.4; human. [Q9H2S1-1]
DR   AGR; HGNC:6291; -.
DR   CTD; 3781; -.
DR   DisGeNET; 3781; -.
DR   GeneCards; KCNN2; -.
DR   HGNC; HGNC:6291; KCNN2.
DR   HPA; ENSG00000080709; Tissue enhanced (adrenal gland, liver).
DR   MalaCards; KCNN2; -.
DR   MIM; 605879; gene.
DR   MIM; 619724; phenotype.
DR   MIM; 619725; phenotype.
DR   neXtProt; NX_Q9H2S1; -.
DR   OpenTargets; ENSG00000080709; -.
DR   PharmGKB; PA30071; -.
DR   VEuPathDB; HostDB:ENSG00000080709; -.
DR   eggNOG; KOG3684; Eukaryota.
DR   GeneTree; ENSGT00950000182904; -.
DR   HOGENOM; CLU_014617_0_1_1; -.
DR   InParanoid; Q9H2S1; -.
DR   OrthoDB; 4200919at2759; -.
DR   PhylomeDB; Q9H2S1; -.
DR   TreeFam; TF315015; -.
DR   PathwayCommons; Q9H2S1; -.
DR   Reactome; R-HSA-1296052; Ca2+ activated K+ channels.
DR   Reactome; R-HSA-9667769; Acetylcholine inhibits contraction of outer hair cells.
DR   SignaLink; Q9H2S1; -.
DR   SIGNOR; Q9H2S1; -.
DR   BioGRID-ORCS; 3781; 10 hits in 1152 CRISPR screens.
DR   ChiTaRS; KCNN2; human.
DR   GeneWiki; KCNN2; -.
DR   GenomeRNAi; 3781; -.
DR   Pharos; Q9H2S1; Tchem.
DR   PRO; PR:Q9H2S1; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9H2S1; Protein.
DR   Bgee; ENSG00000080709; Expressed in secondary oocyte and 150 other cell types or tissues.
DR   ExpressionAtlas; Q9H2S1; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR   GO; GO:0051393; F:alpha-actinin binding; IPI:BHF-UCL.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISS:BHF-UCL.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; NAS:UniProtKB.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
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:SF43; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN 2; 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.
DR   Genevisible; Q9H2S1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calmodulin-binding; Disease variant;
KW   Dystonia; Intellectual disability; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..579
FT                   /note="Small conductance calcium-activated potassium
FT                   channel protein 2"
FT                   /id="PRO_0000155010"
FT   TRANSMEM        138..158
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        345..365
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..488
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          551..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         160
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P70604"
FT   VAR_SEQ         1..348
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044584"
FT   VARIANT         30
FT                   /note="E -> Q (in NEDMAB; uncertain significance; no effect
FT                   on channel function)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086742"
FT   VARIANT         160..579
FT                   /note="Missing (in NEDMAB)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086743"
FT   VARIANT         288
FT                   /note="I -> S (in NEDMAB; requires 2 nucleotide
FT                   substitutions)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086744"
FT   VARIANT         321
FT                   /note="Missing (in NEDMAB; loss of function of homomeric
FT                   channels)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086745"
FT   VARIANT         359
FT                   /note="I -> M (in NEDMAB; loss of function of homomeric
FT                   channels)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086746"
FT   VARIANT         361
FT                   /note="Y -> C (in NEDMAB)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086747"
FT   VARIANT         362
FT                   /note="G -> S (in NEDMAB; loss of function of homomeric
FT                   channels)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086748"
FT   VARIANT         371
FT                   /note="G -> E (in DYT34; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:32212350"
FT                   /id="VAR_086749"
FT   VARIANT         388
FT                   /note="L -> V (in NEDMAB; loss of function of homomeric
FT                   channels)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086750"
FT   VARIANT         432
FT                   /note="L -> P (in NEDMAB; loss of function of homomeric
FT                   channels)"
FT                   /evidence="ECO:0000269|PubMed:33242881"
FT                   /id="VAR_086751"
FT   CONFLICT        50
FT                   /note="S -> SA (in Ref. 3; AAK84039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="A -> D (in Ref. 1; AAG16728)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="A -> AA (in Ref. 2; AAP45946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="I -> T (in Ref. 3; AAK84039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        530
FT                   /note="Q -> R (in Ref. 2; AAP45946 and 3; AAK84039)"
FT                   /evidence="ECO:0000305"
FT   STRAND          405..409
FT                   /evidence="ECO:0007829|PDB:6ALE"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:5WBX"
FT   HELIX           413..438
FT                   /evidence="ECO:0007829|PDB:5V02"
FT   STRAND          439..442
FT                   /evidence="ECO:0007829|PDB:5WBX"
FT   HELIX           445..484
FT                   /evidence="ECO:0007829|PDB:5V02"
SQ   SEQUENCE   579 AA;  63760 MW;  2ED87FE13C106183 CRC64;
     MSSCRYNGGV MRPLSNLSAS RRNLHEMDSE AQPLQPPASV GGGGGASSPS AAAAAAAAVS
     SSAPEIVVSK PEHNNSNNLA LYGTGGGGST GGGGGGGGSG HGSSSGTKSS KKKNQNIGYK
     LGHRRALFEK RKRLSDYALI FGMFGIVVMV IETELSWGAY DKASLYSLAL KCLISLSTII
     LLGLIIVYHA REIQLFMVDN GADDWRIAMT YERIFFICLE ILVCAIHPIP GNYTFTWTAR
     LAFSYAPSTT TADVDIILSI PMFLRLYLIA RVMLLHSKLF TDASSRSIGA LNKINFNTRF
     VMKTLMTICP GTVLLVFSIS LWIIAAWTVR ACERYHDQQD VTSNFLGAMW LISITFLSIG
     YGDMVPNTYC GKGVCLLTGI MGAGCTALVV AVVARKLELT KAEKHVHNFM MDTQLTKRVK
     NAAANVLRET WLIYKNTKLV KKIDHAKVRK HQRKFLQAIH QLRSVKMEQR KLNDQANTLV
     DLAKTQNIMY DMISDLNERS EDFEKRIVTL ETKLETLIGS IHALPGLISQ TIRQQQRDFI
     EAQMESYDKH VTYNAERSRS SSRRRRSSST APPTSSESS
//