ID   SYN3_RAT                Reviewed;         579 AA.
AC   O70441;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   21-SEP-2011, entry version 86.
DE   RecName: Full=Synapsin-3;
DE   AltName: Full=Synapsin III;
GN   Name=Syn3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98256247; PubMed=9593663; DOI=10.1074/jbc.273.22.13371;
RA   Hosaka M., Suedhof T.C.;
RT   "Synapsin III, a novel synapsin with an unusual regulation by Ca2+.";
RL   J. Biol. Chem. 273:13371-13374(1998).
RN   [2]
RP   INTERACTION WITH CAPON.
RX   MEDLINE=21874142; PubMed=11867766; DOI=10.1073/pnas.261705799;
RA   Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.;
RT   "Neuronal nitric-oxide synthase localization mediated by a ternary
RT   complex with synapsin and CAPON.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002).
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.
CC   -!- SUBUNIT: Interacts with CAPON.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Peripheral membrane protein localized to
CC       the cytoplasmic surface of synaptic vesicles.
CC   -!- TISSUE SPECIFICITY: Expressed primarily in brain.
CC   -!- MISCELLANEOUS: Regulated by calcium.
CC   -!- SIMILARITY: Belongs to the synapsin family.
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DR   EMBL; AF056704; AAC24521.1; -; mRNA.
DR   IPI; IPI00390215; -.
DR   RefSeq; NP_058805.1; NM_017109.1.
DR   UniGene; Rn.162920; -.
DR   ProteinModelPortal; O70441; -.
DR   SMR; O70441; 90-395.
DR   DIP; DIP-358N; -.
DR   MINT; MINT-232985; -.
DR   STRING; O70441; -.
DR   PhosphoSite; O70441; -.
DR   PRIDE; O70441; -.
DR   Ensembl; ENSRNOT00000037918; ENSRNOP00000036740; ENSRNOG00000026866.
DR   GeneID; 29130; -.
DR   KEGG; rno:29130; -.
DR   UCSC; NM_017109; rat.
DR   CTD; 8224; -.
DR   RGD; 3799; Syn3.
DR   eggNOG; roNOG13960; -.
DR   GeneTree; ENSGT00530000063319; -.
DR   HOVERGEN; HBG016354; -.
DR   InParanoid; O70441; -.
DR   OMA; MQVVRNG; -.
DR   OrthoDB; EOG4KPTB4; -.
DR   PhylomeDB; O70441; -.
DR   NextBio; 608075; -.
DR   ArrayExpress; O70441; -.
DR   Genevestigator; O70441; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007269; P:neurotransmitter secretion; TAS:RGD.
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_0000183026.
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 (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine (By similarity).
SQ   SEQUENCE   579 AA;  63349 MW;  EA69F25ED14A4722 CRC64;
     MNFLRRRLSD SSFVANLPNG YMPDLQRPES SSSSPASPAT ERRHPQPLAA SFSSPGSSLF
     SSFSSAMKQT PQAPTGLMEP 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 KAVHSKNGRD
     YIIEVMDSSM PLIGEHVEED KQLMADLVVS KMSQLLVPGA SVPSPLRPWG PQTKSAKSPG
     QGQLGPLLGQ PQPRPPPQGG PRQAQSPQPP RSRSPSQQRL SPQGQQPVSP QSGSPQQQRS
     PGSPQLSRAS GGSSPNQASK PTASLSSHTR PPVQGRSTSQ QGEEPQKTAS PHPHLNKSQS
     LTNSLSTSDT SHRGTPSEDE AKAETIRNLR KSFASLFSD
//