ID SYN_DROME Reviewed; 1025 AA.
AC Q24546; Q24544; Q24545; Q86BA0; Q8INM4; Q8INM6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 24-JAN-2024, entry version 159.
DE RecName: Full=Synapsin;
DE Contains:
DE RecName: Full=Synapsin-1;
DE Short=Syn1;
DE AltName: Full=Syn1-S;
DE Contains:
DE RecName: Full=Synapsin-2;
DE Short=Syn2;
GN Name=Syn; Synonyms=Syn-1, Syn-2; ORFNames=CG3985;
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 F), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 145-1025 (ISOFORM C), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Berlin, and Canton-S; TISSUE=Head;
RX PubMed=8627354; DOI=10.1523/jneurosci.16-10-03154.1996;
RA Klagges B.R.E., Heimbeck G., Godenschwege T.A., Hofbauer A.,
RA Pflugfelder G.O., Reifegerste R., Reisch D., Schaupp M., Buchner S.,
RA Buchner E.;
RT "Invertebrate synapsins: a single gene codes for several isoforms in
RT Drosophila.";
RL J. Neurosci. 16:3154-3165(1996).
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 PROTEIN SEQUENCE OF 2-10, FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Head;
RX PubMed=15255973; DOI=10.1111/j.1460-9568.2004.03527.x;
RA Godenschwege T.A., Reisch D., Diegelmann S., Eberle K., Funk N.,
RA Heisenberg M., Hoppe V., Hoppe J., Klagges B.R.E., Martin J.R.,
RA Nikitina E.A., Putz G., Reifegerste R., Reisch N., Rister J., Schaupp M.,
RA Scholz H., Schwarzel M., Werner U., Zars T.D., Buchner S., Buchner E.;
RT "Flies lacking all synapsins are unexpectedly healthy but are impaired in
RT complex behaviour.";
RL Eur. J. Neurosci. 20:611-622(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH NWK AND SYT1.
RX PubMed=29568072; DOI=10.1038/emm.2017.303;
RA Hur J.H., Lee S.H., Kim A.Y., Koh Y.H.;
RT "Regulation of synaptic architecture and synaptic vesicle pools by Nervous
RT wreck at Drosophila Type 1b glutamatergic synapses.";
RL Exp. Mol. Med. 50:E462-E462(2018).
CC -!- FUNCTION: Plays a significant role in nervous system function, which is
CC subtle at the cellular level but manifests itself in complex behavior.
CC {ECO:0000269|PubMed:15255973}.
CC -!- SUBUNIT: Identified in a complex with Syt1 and nwk.
CC {ECO:0000269|PubMed:29568072}.
CC -!- SUBCELLULAR LOCATION: Synapse.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=F; Synonyms=Syn1-RT;
CC IsoId=Q24546-1; Sequence=Displayed;
CC Name=C; Synonyms=Syn2;
CC IsoId=Q24546-3; Sequence=VSP_013200, VSP_013201;
CC -!- TISSUE SPECIFICITY: Widely expressed in the embryonic and adult nervous
CC system synaptic terminals. {ECO:0000269|PubMed:8627354}.
CC -!- DEVELOPMENTAL STAGE: Detected at all developmental stages after mid-
CC embryogenesis. {ECO:0000269|PubMed:8627354}.
CC -!- DISRUPTION PHENOTYPE: Mutants show no obvious defects in brain
CC morphology and no striking qualitative changes in behavior are
CC observed. Quantitative differenes are seen: mutants show faster
CC habituation of an olfactory jump response, enhanced ethanol tolerance,
CC and significant defects in learning and memory as measured using three
CC different paradigms. {ECO:0000269|PubMed:15255973}.
CC -!- MISCELLANEOUS: Readthrough of the terminator UGA may occur between the
CC codons for 581-Met and 583-Glu.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN13462.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAN13464.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO41538.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA64722.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA64723.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X95453; CAA64722.1; ALT_INIT; mRNA.
DR EMBL; X95453; CAA64723.1; ALT_INIT; mRNA.
DR EMBL; X95454; CAA64724.1; -; mRNA.
DR EMBL; AE014297; AAN13462.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAN13464.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAO41538.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_731457.2; NM_169332.3.
DR RefSeq; NP_788628.2; NM_176451.3.
DR BioGRID; 66396; 9.
DR IntAct; Q24546; 2.
DR STRING; 7227.FBpp0099901; -.
DR GlyGen; Q24546; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q24546; -.
DR PaxDb; 7227-FBpp0099902; -.
DR PeptideAtlas; Q24546; -.
DR GeneID; 41247; -.
DR KEGG; dme:Dmel_CG3985; -.
DR UCSC; CG3985-RA; d. melanogaster. [Q24546-1]
DR AGR; FB:FBgn0004575; -.
DR CTD; 41247; -.
DR FlyBase; FBgn0004575; Syn.
DR VEuPathDB; VectorBase:FBgn0004575; -.
DR eggNOG; KOG3895; Eukaryota.
DR HOGENOM; CLU_010582_1_0_1; -.
DR InParanoid; Q24546; -.
DR Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 41247; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Sdc; fly.
DR GenomeRNAi; 41247; -.
DR PRO; PR:Q24546; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; Q24546; baseline and differential.
DR Genevisible; Q24546; DM.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008306; P:associative learning; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0071632; P:optomotor response; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR001359; Synapsin.
DR InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR PANTHER; PTHR10841; SYNAPSIN; 1.
DR PANTHER; PTHR10841:SF17; SYNAPSIN; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Behavior; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..1025
FT /note="Synapsin"
FT /id="PRO_0000033495"
FT CHAIN 1..581
FT /note="Synapsin-1"
FT /id="PRO_0000033496"
FT CHAIN 583..1025
FT /note="Synapsin-2"
FT /id="PRO_0000033497"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 438..532
FT /note="NVCRPSMAQTGPGKLPSRSSVSSRAESPTDEGVAPTPPLPAGPRPAPMGGPP
FT PIPERTSPAVGSIGRLSSRSSISEVPEEPSSSGPSTVGGVRRD -> VERLPSQHGADG
FT SGQVALPLLGLFPSRESHGRGRGSNTTTPSWTKTRAHGWTTTDTGAYLTRRGFHWAAEQ
FT SQQHFGGAGGTLLVGTQHSGWGAS (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8627354"
FT /id="VSP_013200"
FT VAR_SEQ 533..1025
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8627354"
FT /id="VSP_013201"
FT CONFLICT 94
FT /note="S -> G (in Ref. 1; CAA64722/CAA64723)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="V -> G (in Ref. 1; CAA64722/CAA64723/CAA64724)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="D -> N (in Ref. 1; CAA64722/CAA64723/CAA64724)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="Q -> K (in Ref. 1; CAA64723)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="S -> G (in Ref. 1; CAA64723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1025 AA; 107539 MW; D18B5AE0F8EE360C CRC64;
MKRGFSSGDL SSEVDDVDPN SLPPAARPIQ DQPTKPPVAG GPPNMPPPPA PGQPAGAAPE
LSLSFGAGKT PATAAPAPPR GVSAPTSPAK SRESLLQRVQ SLTGAARDQG ASILGAAVQS
ATQRAPAFSK DKYFTLLVLD DQNTDWSKYF RGRRLHGDFD IRVEQAEFRD ITVVSSADTG
PVVTMAAYRS GTRVARSFRP DFVLIRQPPR DGSSDYRSTI LGLKYGGVPS INSLHSIYQF
QDKPWVFSHL LQLQRRLGRD GFPLIEQTFF PNPRDLFQFT KFPSVLKAGH CHGGVATARL
ENQSALQDAA GLVSGAGNDS HCYCTIEPYI DAKFSVHIQK IGNNYKAFMR KSITGNWKTN
QGSAMLEQIT LTEKYKSWVD EISELFGGME VCGLSVVVAK DGREYIISAC DSTFALIGDT
QEEDRRQIAD LVSGRMQNVC RPSMAQTGPG KLPSRSSVSS RAESPTDEGV APTPPLPAGP
RPAPMGGPPP IPERTSPAVG SIGRLSSRSS ISEVPEEPSS SGPSTVGGVR RDSQTSQSST
ISSSVSRAGQ RPPQTQNSVV EDAEDTMKNL RKTFAGIFGD MXEIANKKRG RTASETSSGS
GPGSVPSSAG PGSGFSSSFL GKQFSFAGKG EGVISTQPTQ RPSEEPPAIP TTASSAVRPE
SSVSVSDSRN TDTLTERAGA GYQPVTNYEQ QERVNPFDKE PSKSGSAASI HTSSSSSISS
SSISSRINRN GNAIQSPPPP AGPPPPPPTN VTAVGSNANS SSGYRNSFSS SLSKDKTSYG
NYGSTTSVET ITRMDTNTTN IGATATEAGE ASGVTAITNI SNSDGIVAPT TGTITTSVTT
NDWRSAIGMR SASVYSAPAA VTTVLPGDTS GYDSNSIASQ GEGLNNPSDL PSYTRPSYSR
SESNASKHSD LDVIFGDSKT TPASYGNGKY TRAAGSISDA DMIFGGPPSN YKTDRFGASK
SMSMTSGGVG SGNGSGSGLG GYKIYDSIQN AAFSDFSDSG SMSSIGSHTK RWSASKEEDD
ELDLK
//
