ID   SYN3_MOUSE              Reviewed;         579 AA.
AC   Q8JZP2; E9QNQ6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Synapsin-3;
DE   AltName: Full=Synapsin III;
GN   Name=Syn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants within
RT   alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-454; SER-461; SER-469;
RP   SER-474 AND SER-540, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in the regulation of neurotransmitter release
CC       and synaptogenesis. Binds ATP with high affinity and ADP with a lower
CC       affinity. This is consistent with a catalytic role of the C-domain in
CC       which ADP would be dissociated by cellular ATP after bound ATP was
CC       hydrolyzed (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CAPON. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Peripheral membrane
CC       protein localized to the cytoplasmic surface of synaptic vesicles.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The A region binds phospholipids with a preference for
CC       negatively charged species. {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic
CC       vesicles. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Regulated by calcium. Calcium inhibits ATP binding to
CC       the C-domain (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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DR   EMBL; AF498252; AAM22969.1; -; mRNA.
DR   EMBL; AF498253; AAM22970.1; -; mRNA.
DR   EMBL; AC122919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC125060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC145076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC150899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24096.1; -.
DR   RefSeq; NP_038750.2; NM_013722.3.
DR   RefSeq; XP_006513761.1; XM_006513698.2.
DR   RefSeq; XP_006513762.1; XM_006513699.3.
DR   RefSeq; XP_006513763.1; XM_006513700.3.
DR   AlphaFoldDB; Q8JZP2; -.
DR   SMR; Q8JZP2; -.
DR   BioGRID; 205126; 5.
DR   IntAct; Q8JZP2; 3.
DR   MINT; Q8JZP2; -.
DR   STRING; 10090.ENSMUSP00000113720; -.
DR   iPTMnet; Q8JZP2; -.
DR   PhosphoSitePlus; Q8JZP2; -.
DR   SwissPalm; Q8JZP2; -.
DR   MaxQB; Q8JZP2; -.
DR   PaxDb; 10090-ENSMUSP00000113720; -.
DR   ProteomicsDB; 263177; -.
DR   ABCD; Q8JZP2; 2 sequenced antibodies.
DR   Antibodypedia; 25287; 140 antibodies from 22 providers.
DR   DNASU; 27204; -.
DR   Ensembl; ENSMUST00000120638.8; ENSMUSP00000113720.2; ENSMUSG00000059602.15.
DR   GeneID; 27204; -.
DR   KEGG; mmu:27204; -.
DR   UCSC; uc007gnn.2; mouse.
DR   AGR; MGI:1351334; -.
DR   CTD; 8224; -.
DR   MGI; MGI:1351334; Syn3.
DR   VEuPathDB; HostDB:ENSMUSG00000059602; -.
DR   eggNOG; KOG3895; Eukaryota.
DR   GeneTree; ENSGT00940000155415; -.
DR   HOGENOM; CLU_010582_3_0_1; -.
DR   InParanoid; Q8JZP2; -.
DR   OMA; GPHKCIL; -.
DR   OrthoDB; 5487039at2759; -.
DR   PhylomeDB; Q8JZP2; -.
DR   TreeFam; TF319919; -.
DR   Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR   BioGRID-ORCS; 27204; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Syn3; mouse.
DR   PRO; PR:Q8JZP2; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8JZP2; Protein.
DR   Bgee; ENSMUSG00000059602; Expressed in embryonic brain and 55 other cell types or tissues.
DR   ExpressionAtlas; Q8JZP2; baseline and differential.
DR   GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0097091; P:synaptic vesicle clustering; IDA:SynGO.
DR   GO; GO:0099504; P:synaptic vesicle cycle; IDA:SynGO.
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; IPR019735; Synapsin_CS.
DR   InterPro; IPR019736; Synapsin_P_site.
DR   InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR   PANTHER; PTHR10841; SYNAPSIN; 1.
DR   PANTHER; PTHR10841:SF27; SYNAPSIN-3; 1.
DR   Pfam; PF02078; Synapsin; 1.
DR   Pfam; PF02750; Synapsin_C; 1.
DR   Pfam; PF10581; Synapsin_N; 1.
DR   PRINTS; PR01368; SYNAPSIN.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS00415; SYNAPSIN_1; 1.
DR   PROSITE; PS00416; SYNAPSIN_2; 1.
DR   Genevisible; Q8JZP2; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cytoplasmic vesicle; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Synapse.
FT   CHAIN           1..579
FT                   /note="Synapsin-3"
FT                   /id="PRO_0000183025"
FT   REGION          1..28
FT                   /note="A"
FT   REGION          15..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..90
FT                   /note="B; linker"
FT   REGION          91..398
FT                   /note="C; actin-binding and synaptic-vesicle binding"
FT   REGION          399..530
FT                   /note="J; Pro-rich linker"
FT   REGION          401..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..579
FT                   /note="E"
FT   COMPBIAS        25..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..444
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70441"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        65
FT                   /note="G -> S (in Ref. 1; AAM22969/AAM22970)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   579 AA;  63315 MW;  2B84E36A1663D50F CRC64;
     MNFLRRRLSD SSFVANLPNG YMPDLQRPES SSSSPASPAT ERRHPQPLAA SFSSPGSSLF
     SSFSGAMKQT PQAPSGLMEP PTPVTPVVQR PRILLVIDDA HTDWSKYFHG KKVNGDIEIR
     VEQAEFSELN LAAYVTGGCM VDMQVVRNGT KIVRSFKPDF ILVRQHAYSM ALAEDYRSLV
     IGLQYGGLPA VNSLYSVYNF CSKPWVFSQL IKIFHSLGPE KFPLVEQTFF PNHKPMLTAP
     NFPVVIKLGH AHAGMGKIKV ENQHDYQDIT SVVAMAKTYA TTEAFIDSKY DIRIQKIGSN
     YKAYMRTSIS GNWKANTGSA MLEQVAMTER YRLWVDSCSE MFGGLDICAV KAVHSKDGRD
     YIIEVMDSSM PLIGEHVEED KQLMADLVVS KMSQLLVPGA TVPSPLRPWG PQTKPAKSPG
     QGQLGPLLGQ PQPRPPPQGG PRQAQSPQPP RSRSPSQQRL SPQGQQPVSP QSGSPQQQRS
     PGSPQLSRAS GGSSPNQASK PSASLSSHNR PPVQGRSTSQ QGEEPQKSAS PHPHLNKSQS
     LTNSLSTSDT SHRGTPSEDE AKAETIRNLR KSFASLFSD
//