SYN3_MOUSE
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 03-AUG-2022, entry version 145.
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; 3.
DR IntAct; Q8JZP2; 3.
DR MINT; Q8JZP2; -.
DR STRING; 10090.ENSMUSP00000113720; -.
DR iPTMnet; Q8JZP2; -.
DR PhosphoSitePlus; Q8JZP2; -.
DR MaxQB; Q8JZP2; -.
DR PaxDb; Q8JZP2; -.
DR PRIDE; Q8JZP2; -.
DR ProteomicsDB; 263177; -.
DR ABCD; Q8JZP2; 2 sequenced antibodies.
DR Antibodypedia; 25287; 129 antibodies from 22 providers.
DR DNASU; 27204; -.
DR Ensembl; ENSMUST00000120638; ENSMUSP00000113720; ENSMUSG00000059602.
DR GeneID; 27204; -.
DR KEGG; mmu:27204; -.
DR UCSC; uc007gnn.2; mouse.
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; FFPNHTQ; -.
DR OrthoDB; 799740at2759; -.
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 71 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 54 other tissues.
DR ExpressionAtlas; Q8JZP2; baseline and differential.
DR Genevisible; Q8JZP2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR028712; SYN2/3.
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:SF20; PTHR10841:SF20; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR Pfam; PF10581; Synapsin_N; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS00415; SYNAPSIN_1; 1.
DR PROSITE; PS00416; SYNAPSIN_2; 1.
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
