1433Z_DROME
ID 1433Z_DROME Reviewed; 248 AA.
AC P29310; A4UZB2; A4UZB3; C1C593; C9QP27; O01665; Q0E9D5; Q0E9D6; Q0E9D7;
AC Q8IGB9; Q8MKV5; Q9V5G6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=14-3-3 protein zeta;
DE AltName: Full=14-3-3-like protein;
DE AltName: Full=Protein Leonardo;
GN Name=14-3-3zeta; Synonyms=14-3-3, 14-3-3EZ, leo, THAP; ORFNames=CG17870;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VI).
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=1349290; DOI=10.1016/0378-1119(92)90394-5;
RA Swanson K.D., Ganguly R.;
RT "Characterization of a Drosophila melanogaster gene similar to the
RT mammalian genes encoding the tyrosine/tryptophan hydroxylase activator and
RT protein kinase C inhibitor proteins.";
RL Gene 113:183-190(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ALTERNATIVE SPLICING
RP (ISOFORMS VI AND VI').
RC STRAIN=Oregon-R;
RX PubMed=9159395; DOI=10.1101/gad.11.9.1140;
RA Kockel L., Vorbrueggen G., Jaeckle H., Mlodzik M., Bohmann D.;
RT "Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor
RT development.";
RL Genes Dev. 11:1140-1147(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS VI AND VI').
RC STRAIN=Berkeley; TISSUE=Ovary;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH SLOB.
RX PubMed=10230800; DOI=10.1016/s0896-6273(00)80739-4;
RA Zhou Y., Schopperle W.M., Murrey H., Jaramillo A., Dagan D., Griffith L.C.,
RA Levitan I.B.;
RT "A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel
RT complex in Drosophila presynaptic nerve terminals.";
RL Neuron 22:809-818(1999).
RN [8]
RP HOMODIMERIZATION, AND MUTAGENESIS OF ARG-59 AND ARG-63.
RX PubMed=12529354; DOI=10.1074/jbc.m211907200;
RA Zhou Y., Reddy S., Murrey H., Fei H., Levitan I.B.;
RT "Monomeric 14-3-3 protein is sufficient to modulate the activity of the
RT Drosophila slowpoke calcium-dependent potassium channel.";
RL J. Biol. Chem. 278:10073-10080(2003).
RN [9]
RP INTERACTION WITH YKI.
RX PubMed=18256197; DOI=10.1242/dev.015255;
RA Oh H., Irvine K.D.;
RT "In vivo regulation of Yorkie phosphorylation and localization.";
RL Development 135:1081-1088(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH YKI.
RX PubMed=19900439; DOI=10.1016/j.ydbio.2009.10.046;
RA Ren F., Zhang L., Jiang J.;
RT "Hippo signaling regulates Yorkie nuclear localization and activity through
RT 14-3-3 dependent and independent mechanisms.";
RL Dev. Biol. 337:303-312(2010).
RN [11]
RP FUNCTION, INTERACTION WITH HEMO, AND SUBCELLULAR LOCATION.
RX PubMed=27015288; DOI=10.1371/journal.pbio.1002395;
RA Pueyo J.I., Magny E.G., Sampson C.J., Amin U., Evans I.R., Bishop S.A.,
RA Couso J.P.;
RT "Hemotin, a regulator of phagocytosis encoded by a small ORF and conserved
RT across metazoans.";
RL PLoS Biol. 14:E1002395-E1002395(2016).
RN [12]
RP INTERACTION WITH REPTOR.
RX PubMed=25920570; DOI=10.1016/j.devcel.2015.03.013;
RA Tiebe M., Lutz M., De La Garza A., Buechling T., Boutros M., Teleman A.A.;
RT "REPTOR and REPTOR-BP regulate organismal metabolism and transcription
RT downstream of TORC1.";
RL Dev. Cell 33:272-284(2015).
CC -!- FUNCTION: Required in Raf-dependent cell proliferation and
CC photoreceptor differentiation during eye development (PubMed:9159395).
CC Acts upstream of Raf and downstream of Ras, and is essential for
CC viability (PubMed:9159395). Acts as a negative regulator of the slo
CC calcium channel via its interaction with slo-binding protein slob
CC (PubMed:10230800). Inhibits yki activity by restricting its nuclear
CC localization (PubMed:19900439). Binds to and promotes the activity of
CC phosphoinositide 3-kinase Pi3K68D which converts phosphatidylinositol
CC to phosphatidylinositol-3-phosphate and promotes maturation of early
CC endosomes (PubMed:27015288). {ECO:0000269|PubMed:10230800,
CC ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:27015288,
CC ECO:0000269|PubMed:9159395}.
CC -!- SUBUNIT: Homodimer; homodimerization is not essential for modulating
CC the activity of Slo (PubMed:12529354). Interacts with phosphorylated
CC Slob; the interaction with Slob mediates an indirect interaction with
CC Slo (PubMed:10230800). Interacts with phosphorylated yki
CC (PubMed:18256197, PubMed:19900439). Interacts with hemo; this represses
CC 14-3-3zeta activity which prevents the 14-3-3zeta-mediated activation
CC of phosphoinositide 3-kinase Pi3K68D. This, in turn, inhibits the
CC Pi3K68D-mediated conversion of phosphatidylinositol to
CC phosphatidylinositol-3-phosphate and prevents progression of early
CC endosomes through the maturation process which regulates subsequent
CC steps of phagocytic processing (PubMed:27015288). Interacts with REPTOR
CC (when phosphorylated), this interaction may assist the cytoplasmic
CC retention of REPTOR (PubMed:25920570). {ECO:0000269|PubMed:10230800,
CC ECO:0000269|PubMed:12529354, ECO:0000269|PubMed:18256197,
CC ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:25920570,
CC ECO:0000269|PubMed:27015288}.
CC -!- INTERACTION:
CC P29310; Q8IPH9: Slob; NbExp=4; IntAct=EBI-198100, EBI-142379;
CC P29310-2; Q9VS36: mei-P22; NbExp=3; IntAct=EBI-198120, EBI-102811;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC {ECO:0000269|PubMed:27015288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=VI; Synonyms=D, J;
CC IsoId=P29310-1; Sequence=Displayed;
CC Name=VI'; Synonyms=A, G, H, I;
CC IsoId=P29310-2; Sequence=VSP_000001;
CC Name=C; Synonyms=F;
CC IsoId=P29310-3; Sequence=VSP_010303, VSP_010304;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the ventral nerve cord
CC of the embryo, and in the neural tissues of the head. Also found in the
CC region posterior to the morphogenetic furrow of the eye imaginal disk
CC where cells differentiate as photoreceptors.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of embryonic and
CC larval development.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77518; AAA28324.1; -; mRNA.
DR EMBL; Y12573; CAA73152.1; -; Genomic_DNA.
DR EMBL; Y12573; CAA73153.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58842.4; -; Genomic_DNA.
DR EMBL; AE013599; AAF58843.3; -; Genomic_DNA.
DR EMBL; AE013599; AAM71060.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71063.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM71064.2; -; Genomic_DNA.
DR EMBL; AE013599; AAS64884.1; -; Genomic_DNA.
DR EMBL; AE013599; AAX52715.1; -; Genomic_DNA.
DR EMBL; AE013599; AAX52716.1; -; Genomic_DNA.
DR EMBL; BT001855; AAN71617.1; -; mRNA.
DR EMBL; BT082022; ACO72859.1; -; mRNA.
DR EMBL; BT088441; ACR44245.1; -; mRNA.
DR EMBL; BT099909; ACX32980.1; -; mRNA.
DR PIR; JC1122; JC1122.
DR RefSeq; NP_001014515.1; NM_001014515.2. [P29310-1]
DR RefSeq; NP_001014516.1; NM_001014516.2. [P29310-2]
DR RefSeq; NP_001260845.1; NM_001273916.1. [P29310-1]
DR RefSeq; NP_001260846.1; NM_001273917.1. [P29310-1]
DR RefSeq; NP_476885.2; NM_057537.4. [P29310-1]
DR RefSeq; NP_724884.1; NM_165740.3. [P29310-1]
DR RefSeq; NP_724885.1; NM_165741.3. [P29310-2]
DR RefSeq; NP_724886.1; NM_165742.2. [P29310-2]
DR RefSeq; NP_724887.2; NM_165743.3. [P29310-3]
DR RefSeq; NP_724888.2; NM_165744.3. [P29310-3]
DR RefSeq; NP_724889.2; NM_165745.3. [P29310-2]
DR RefSeq; NP_995792.1; NM_206070.2. [P29310-2]
DR AlphaFoldDB; P29310; -.
DR SMR; P29310; -.
DR BioGRID; 61887; 90.
DR DIP; DIP-17371N; -.
DR IntAct; P29310; 19.
DR STRING; 7227.FBpp0087500; -.
DR TCDB; 8.A.98.1.1; the 14-3-3 protein (14-3-3) family.
DR PaxDb; P29310; -.
DR PRIDE; P29310; -.
DR DNASU; 36059; -.
DR EnsemblMetazoa; FBtr0088412; FBpp0087500; FBgn0004907. [P29310-2]
DR EnsemblMetazoa; FBtr0088413; FBpp0087501; FBgn0004907. [P29310-2]
DR EnsemblMetazoa; FBtr0088414; FBpp0087502; FBgn0004907. [P29310-1]
DR EnsemblMetazoa; FBtr0088415; FBpp0087503; FBgn0004907. [P29310-1]
DR EnsemblMetazoa; FBtr0088416; FBpp0087504; FBgn0004907. [P29310-3]
DR EnsemblMetazoa; FBtr0088417; FBpp0087505; FBgn0004907. [P29310-2]
DR EnsemblMetazoa; FBtr0088418; FBpp0089337; FBgn0004907. [P29310-2]
DR EnsemblMetazoa; FBtr0088419; FBpp0089338; FBgn0004907. [P29310-3]
DR EnsemblMetazoa; FBtr0100182; FBpp0099539; FBgn0004907. [P29310-2]
DR EnsemblMetazoa; FBtr0100183; FBpp0099540; FBgn0004907. [P29310-1]
DR EnsemblMetazoa; FBtr0332916; FBpp0305136; FBgn0004907. [P29310-1]
DR EnsemblMetazoa; FBtr0332917; FBpp0305137; FBgn0004907. [P29310-1]
DR GeneID; 36059; -.
DR KEGG; dme:Dmel_CG17870; -.
DR CTD; 36059; -.
DR FlyBase; FBgn0004907; 14-3-3zeta.
DR VEuPathDB; VectorBase:FBgn0004907; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P29310; -.
DR OMA; KGCQLAR; -.
DR PhylomeDB; P29310; -.
DR Reactome; R-DME-165159; MTOR signalling.
DR Reactome; R-DME-166208; mTORC1-mediated signalling.
DR Reactome; R-DME-170968; Frs2-mediated activation.
DR Reactome; R-DME-2028269; Signaling by Hippo.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
DR Reactome; R-DME-392517; Rap1 signalling.
DR Reactome; R-DME-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DME-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-DME-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-DME-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DME-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-DME-9614399; Regulation of localization of FOXO transcription factors.
DR SignaLink; P29310; -.
DR BioGRID-ORCS; 36059; 1 hit in 3 CRISPR screens.
DR ChiTaRS; 14-3-3zeta; fly.
DR GenomeRNAi; 36059; -.
DR PRO; PR:P29310; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004907; Expressed in brain and 36 other tissues.
DR ExpressionAtlas; P29310; baseline and differential.
DR Genevisible; P29310; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0031965; C:nuclear membrane; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IGI:FlyBase.
DR GO; GO:0007611; P:learning or memory; IMP:FlyBase.
DR GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IGI:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; HGI:FlyBase.
DR GO; GO:0120176; P:positive regulation of torso signaling pathway; IGI:FlyBase.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IDA:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Endosome; Neurogenesis; Reference proteome.
FT CHAIN 1..248
FT /note="14-3-3 protein zeta"
FT /id="PRO_0000058651"
FT VAR_SEQ 146..161
FT /note="DDSQTAYQDAFDISKG -> EDSKKAYQEAFDIAKT (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_010303"
FT VAR_SEQ 149..161
FT /note="QTAYQDAFDISKG -> KNAYQEAFDIAKT (in isoform VI')"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_000001"
FT VAR_SEQ 185..193
FT /note="LNSPDKACQ -> INSPARACH (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_010304"
FT MUTAGEN 59
FT /note="R->A: Abolishes homodimerization but not regulatory
FT function on Slo; when associated with A-63."
FT /evidence="ECO:0000269|PubMed:12529354"
FT MUTAGEN 63
FT /note="R->A: Abolishes homodimerization but not regulatory
FT function on Slo; when associated with A-59."
FT /evidence="ECO:0000269|PubMed:12529354"
FT CONFLICT P29310-3:149
FT /note="K -> E (in Ref. 5; AAN71617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28228 MW; C645CF3B10C6701A CRC64;
MSTVDKEELV QKAKLAEQSE RYDDMAQAMK SVTETGVELS NEERNLLSVA YKNVVGARRS
SWRVISSIEQ KTEASARKQQ LAREYRERVE KELREICYEV LGLLDKYLIP KASNPESKVF
YLKMKGDYYR YLAEVATGDA RNTVVDDSQT AYQDAFDISK GKMQPTHPIR LGLALNFSVF
YYEILNSPDK ACQLAKQAFD DAIAELDTLN EDSYKDSTLI MQLLRDNLTL WTSDTQGDEA
EPQEGGDN
