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   14-DEC-2011, entry version 71.
DE   RecName: Full=Synapsin-3;
DE   AltName: Full=Synapsin III;
GN   Name=Syn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; 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
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-469, AND
RP   MASS SPECTROMETRY.
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.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May be involved in the regulation of neurotransmitter
CC       release and synaptogenesis. Binds ATP with high affinity and ADP
CC       with a lower affinity. This is consistent with a catalytic role of
CC       the C-domain in which ADP would be dissociated by cellular ATP
CC       after bound ATP was hydrolyzed (By similarity).
CC   -!- SUBUNIT: Interacts with CAPON (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Note=Peripheral membrane protein
CC       localized to the cytoplasmic surface of synaptic vesicles (By
CC       similarity).
CC   -!- MISCELLANEOUS: Regulated by calcium. Calcium inhibits ATP binding
CC       to the C-domain (By similarity).
CC   -!- SIMILARITY: Belongs to the synapsin family.
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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   IPI; IPI00463761; -.
DR   RefSeq; NP_038750.2; NM_013722.3.
DR   UniGene; Mm.394931; -.
DR   UniGene; Mm.444790; -.
DR   ProteinModelPortal; Q8JZP2; -.
DR   SMR; Q8JZP2; 90-395.
DR   IntAct; Q8JZP2; 1.
DR   STRING; Q8JZP2; -.
DR   PRIDE; Q8JZP2; -.
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   HOGENOM; HBG445598; -.
DR   HOVERGEN; HBG016354; -.
DR   InParanoid; Q8JZP2; -.
DR   OrthoDB; EOG4KPTB4; -.
DR   ArrayExpress; Q8JZP2; -.
DR   Bgee; Q8JZP2; -.
DR   CleanEx; MM_SYN3; -.
DR   Genevestigator; Q8JZP2; -.
DR   GermOnline; ENSMUSG00000059602; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
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   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 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; PreATP-grasp-like; 1.
DR   PROSITE; PS00415; SYNAPSIN_1; 1.
DR   PROSITE; PS00416; SYNAPSIN_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cell junction; Complete proteome;
KW   Cytoplasmic vesicle; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   CHAIN         1    579       Synapsin-3.
FT                                /FTId=PRO_0000183025.
FT   REGION        1     28       A.
FT   REGION       28     90       B; linker.
FT   REGION       91    398       C; actin-binding and synaptic-vesicle
FT                                binding.
FT   REGION      399    530       J; Pro-rich linker.
FT   REGION      531    579       E.
FT   MOD_RES     461    461       Phosphoserine.
FT   MOD_RES     469    469       Phosphoserine.
FT   MOD_RES     483    483       Phosphoserine.
FT   CONFLICT     65     65       G -> S (in Ref. 1; AAM22969/AAM22970).
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
//