SBKH_DROME
ID SBKH_DROME Reviewed; 456 AA.
AC Q9VM90;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Serine/threonine-protein kinase meng-po {ECO:0000305};
DE Short=meng-po {ECO:0000303|PubMed:29473541, ECO:0000312|FlyBase:FBgn0031855};
DE EC=2.7.11.1 {ECO:0000269|PubMed:29473541};
DE AltName: Full=SH3-binding kinase homolog {ECO:0000305};
GN Name=meng {ECO:0000312|FlyBase:FBgn0031855};
GN Synonyms=MP {ECO:0000303|PubMed:29473541},
GN PKN {ECO:0000312|FlyBase:FBgn0031855};
GN ORFNames=CG11221 {ECO:0000312|FlyBase:FBgn0031855};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL49219.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL49219.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL49219.1};
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 [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT
RP SER-334, AND MUTAGENESIS OF SER-334.
RX PubMed=29473541; DOI=10.7554/elife.33007;
RA Lee P.T., Lin G., Lin W.W., Diao F., White B.H., Bellen H.J.;
RT "A kinase-dependent feedforward loop affects CREBB stability and long term
RT memory formation.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in memory formation.
CC Together with the cAMP-dependent protein kinase A Pka-C1, promotes
CC long-term memory (LTM) by regulating CrebB stability and activity.
CC Involved in the maintenance of anesthesia-sensitive memory (ASM) which
CC includes short-term memory (STM) and middle-term memory (MTM).
CC {ECO:0000269|PubMed:29473541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:29473541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:29473541};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29473541};
CC -!- ACTIVITY REGULATION: Activated by Pka-C1-mediated phosphorylation of
CC Ser-334. {ECO:0000269|PubMed:29473541}.
CC -!- TISSUE SPECIFICITY: Expressed in the mushroom bodies (at protein
CC level). {ECO:0000269|PubMed:29473541}.
CC -!- DEVELOPMENTAL STAGE: Expressed broadly in the third instar larvae and
CC adult flies (at protein levels). {ECO:0000269|PubMed:29473541}.
CC -!- DISRUPTION PHENOTYPE: Results in a decreased CrebB protein translation
CC or stability in the brain. RNAi-mediated knockdown in the mushroom
CC bodies results in a reduction of memory formation, including
CC anesthesia-sensitive memory (ASM) and long-term memory (LTM)
CC performance but not anesthesia-resistant memory (ARM) or learning
CC ability. {ECO:0000269|PubMed:29473541}.
CC -!- MISCELLANEOUS: Meng-Po is the Lady of Forgetfulness, a character in
CC Chinese mythology, who ensures that people are ready for reincarnation
CC by providing the 'Tea of Forgetfulness' that makes them loose the
CC memories associated with their former life.
CC {ECO:0000303|PubMed:29473541}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AE014134; AAF52433.1; -; Genomic_DNA.
DR EMBL; AE014134; AHN54203.1; -; Genomic_DNA.
DR EMBL; AY071597; AAL49219.1; -; mRNA.
DR RefSeq; NP_001285688.1; NM_001298759.1.
DR RefSeq; NP_609070.1; NM_135226.3.
DR AlphaFoldDB; Q9VM90; -.
DR SMR; Q9VM90; -.
DR STRING; 7227.FBpp0078933; -.
DR iPTMnet; Q9VM90; -.
DR PaxDb; Q9VM90; -.
DR DNASU; 33948; -.
DR EnsemblMetazoa; FBtr0079303; FBpp0078933; FBgn0031855.
DR EnsemblMetazoa; FBtr0339237; FBpp0308344; FBgn0031855.
DR GeneID; 33948; -.
DR KEGG; dme:Dmel_CG11221; -.
DR UCSC; CG11221-RA; d. melanogaster.
DR CTD; 104192; -.
DR FlyBase; FBgn0031855; meng.
DR VEuPathDB; VectorBase:FBgn0031855; -.
DR eggNOG; KOG1345; Eukaryota.
DR GeneTree; ENSGT00940000174103; -.
DR HOGENOM; CLU_000288_10_3_1; -.
DR InParanoid; Q9VM90; -.
DR OMA; HETACKL; -.
DR OrthoDB; 1221624at2759; -.
DR PhylomeDB; Q9VM90; -.
DR BioGRID-ORCS; 33948; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pkn; fly.
DR GenomeRNAi; 33948; -.
DR PRO; PR:Q9VM90; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031855; Expressed in oviduct (Drosophila) and 11 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0072375; P:medium-term memory; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007614; P:short-term memory; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..456
FT /note="Serine/threonine-protein kinase meng-po"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444433"
FT DOMAIN 101..367
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 15..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 107..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 334
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:29473541"
FT MUTAGEN 334
FT /note="S->A: Abolishes phosphorylation. Reduces kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:29473541"
SQ SEQUENCE 456 AA; 52419 MW; 272D73C6677C375B CRC64;
MGTIEKRSFS FRLRRSFGDG GSTNSRNSNN NSSTCTNHNN QKRCSTPLTP TSTSTGRLEV
PGAASVSRRS SIYKKPDKND GGQIHLIPDV ELPLMTFADQ YNIEKTLAEG CFAKILLCRH
RPTNTLVVLK AVHAELTTIK EFQKEFHYNY ELSHHHHILS AYAVAFQTMD YYVFAMEHAP
YGDLASNIGP NGLHENACKL ISEQLSSALG FMHSKNLVHR DLKIENILVF TPDFTRVKLC
DFGATTKKGL LVHKVKHTWT SCVPPEQLEL IKNERFQCLP VSDSWQFGIL LYNILTGNPP
WQSADWVKDQ SYANFMKYEQ RKTTKVPDNF RRFSPRLMRC FRKYLSHDPE DRCKITEVAK
YMKDRWVECR ISTSKSATLI SPTNHDQDSC IYLNQREGRL SGDENKLRFK RMMSTYGLDI
PIDQAMVRRR VWDWLSTCDA NFDPDVESLH ALDLLQ
