SLOB_DROME
ID SLOB_DROME Reviewed; 515 AA.
AC Q8IPH9; O61564; Q5BIJ6; Q95SL3; Q9VLZ4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Slowpoke-binding protein;
GN Name=Slob; ORFNames=CG43756;
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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP SLO, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=9539129; DOI=10.1016/s0896-6273(00)80995-2;
RA Schopperle W.M., Holmqvist M.H., Zhou Y., Wang J., Wang Z., Griffith L.C.,
RA Keselman I., Kusinitz F., Dagan D., Levitan I.B.;
RT "Slob, a novel protein that interacts with the Slowpoke calcium-dependent
RT potassium channel.";
RL Neuron 20:565-573(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-515 (ISOFORM 2).
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 INTERACTION WITH SLO AND 14-3-3-ZETA, PHOSPHORYLATION AT SER-54 AND SER-79,
RP AND MUTAGENESIS OF SER-54 AND SER-79.
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 [7]
RP INDUCTION.
RX PubMed=11719206; DOI=10.1016/s0896-6273(01)00515-3;
RA Claridge-Chang A., Wijnen H., Naef F., Boothroyd C., Rajewsky N.,
RA Young M.W.;
RT "Circadian regulation of gene expression systems in the Drosophila head.";
RL Neuron 32:657-671(2001).
RN [8]
RP INTERACTION WITH SLO.
RX PubMed=14529710; DOI=10.1016/s0028-3908(03)00285-5;
RA Zhou Y., Fei H., Levitan I.B.;
RT "An interaction domain in Slob necessary for its binding to the slowpoke
RT calcium-dependent potassium channel.";
RL Neuropharmacology 45:714-719(2003).
CC -!- FUNCTION: Regulator of calcium-activated channel Slo. Increases or
CC decreases the voltage sensitivity of Slo, depending on the absence or
CC presence of 14-3-3-zeta in the complex, respectively.
CC {ECO:0000269|PubMed:9539129}.
CC -!- SUBUNIT: Interacts specifically with Slo; which activates Slo activity.
CC Interacts with 14-3-3-zeta when phosphorylated. Forms a
CC heterotetrameric complex containing phosphorylated Slob, Slo and 14-3-
CC 3-zeta, which represses Slo activity due to the indirect interaction
CC between Slo and 14-3-3-zeta. {ECO:0000269|PubMed:10230800,
CC ECO:0000269|PubMed:14529710, ECO:0000269|PubMed:9539129}.
CC -!- INTERACTION:
CC Q8IPH9; P29310: 14-3-3zeta; NbExp=4; IntAct=EBI-142379, EBI-198100;
CC Q8IPH9-1; Q03720: slo; NbExp=2; IntAct=EBI-424896, EBI-426805;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Enriched in
CC synaptic boutons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q8IPH9-1; Sequence=Displayed;
CC Name=2; Synonyms=D;
CC IsoId=Q8IPH9-2; Sequence=VSP_010097;
CC -!- TISSUE SPECIFICITY: Expressed in head. In larval brain, it is expressed
CC in the mushroom body. Also expressed in larval muscles.
CC {ECO:0000269|PubMed:9539129}.
CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak at ZT15
CC (zeitgeber 15). {ECO:0000269|PubMed:11719206}.
CC -!- PTM: Phosphorylated. Phosphorylation of Ser-54 and Ser-79 is required
CC for the interaction with 14-3-3-zeta but not with that of Slo.
CC {ECO:0000269|PubMed:10230800}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28269.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN10635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF051162; AAC06289.1; -; mRNA.
DR EMBL; AE014134; AAF52534.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10635.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014134; ABC65880.1; -; Genomic_DNA.
DR EMBL; BT021228; AAX33376.1; -; mRNA.
DR EMBL; AY060721; AAL28269.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001033881.1; NM_001038792.1. [Q8IPH9-2]
DR RefSeq; NP_001188710.1; NM_001201781.1. [Q8IPH9-2]
DR RefSeq; NP_477349.1; NM_058001.3. [Q8IPH9-1]
DR RefSeq; NP_723292.1; NM_164756.3.
DR RefSeq; NP_723293.1; NM_164757.2. [Q8IPH9-1]
DR AlphaFoldDB; Q8IPH9; -.
DR SMR; Q8IPH9; -.
DR BioGRID; 60180; 4.
DR ELM; Q8IPH9; -.
DR IntAct; Q8IPH9; 4.
DR iPTMnet; Q8IPH9; -.
DR PaxDb; Q8IPH9; -.
DR PRIDE; Q8IPH9; -.
DR DNASU; 34038; -.
DR EnsemblMetazoa; FBtr0330697; FBpp0303540; FBgn0264087. [Q8IPH9-1]
DR EnsemblMetazoa; FBtr0330699; FBpp0303542; FBgn0264087. [Q8IPH9-1]
DR EnsemblMetazoa; FBtr0330700; FBpp0303543; FBgn0264087. [Q8IPH9-2]
DR EnsemblMetazoa; FBtr0330701; FBpp0303544; FBgn0264087. [Q8IPH9-2]
DR GeneID; 34038; -.
DR KEGG; dme:Dmel_CG43756; -.
DR UCSC; CG6772-RD; d. melanogaster.
DR CTD; 34038; -.
DR FlyBase; FBgn0264087; Slob.
DR VEuPathDB; VectorBase:FBgn0264087; -.
DR eggNOG; ENOG502QVVI; Eukaryota.
DR InParanoid; Q8IPH9; -.
DR OMA; NEPWAKK; -.
DR PhylomeDB; Q8IPH9; -.
DR BioGRID-ORCS; 34038; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34038; -.
DR PRO; PR:Q8IPH9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0264087; Expressed in head capsule and 14 other tissues.
DR ExpressionAtlas; Q8IPH9; baseline and differential.
DR Genevisible; Q8IPH9; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; NAS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IBA:GO_Central.
DR GO; GO:0043271; P:negative regulation of ion transport; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..515
FT /note="Slowpoke-binding protein"
FT /id="PRO_0000071959"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..203
FT /note="Interaction with Slo"
FT REGION 483..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10230800"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10230800"
FT VAR_SEQ 410..413
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9539129, ECO:0000303|Ref.4"
FT /id="VSP_010097"
FT MUTAGEN 54
FT /note="S->A: Abolishes phosphorylation and interaction with
FT 14-3-3-zeta; when associated with A-79."
FT /evidence="ECO:0000269|PubMed:10230800"
FT MUTAGEN 79
FT /note="S->A: Abolishes phosphorylation and interaction with
FT 14-3-3-zeta; when associated with A-54."
FT /evidence="ECO:0000269|PubMed:10230800"
FT CONFLICT 12..13
FT /note="RI -> PS (in Ref. 1; AAC06289)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="N -> T (in Ref. 1; AAC06289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 57924 MW; 1B4D86959CCAFAC1 CRC64;
MFKFNKAAQQ QRIDNRNSAV TGHDPFVRPP VPEKKVRNIM KKLHKANGLK RSNSAIEFDV
SALTAANRRQ IYSSNRSASS EQDNSDLSEH SEKSPLVSAR LDNLARLFFS KSMPAETGSR
DTIDSVLTTR PNIKYQYSAL DSGNGIVERS PRERAQREKA LNATQEWIQG ANGRYEVIAH
LDEIGSRHGK NWFLVTDASV RTDRLQTLLP LPPDCVAFED LPPNECAREI LMELLGSLHH
PYIYPVLDLG FLRNSSYNYA CLVTPFNSRG SLKDLIYKAQ WNEPWARKYT RKPNGLPVSQ
VQRLGRQILE ALLFLKERGF PLHGHLHSGN VILQNGAARL SGLENGLLGL SSRINAVMWS
RSVTEIENVD IVCFGHLLYE MCTGQELTTP KPSMRVLEME LQHYPQIGQT RKQILEILGL
IFEPPSGVCP SVEDLVLCDL FRSIDLRELR GPCFSTIKPS LSRSTLNLLQ AVKKRQCASL
GHSLSEANSP CTPPSTPHDR RTGVLPAPYE VFRMY
