SYN3_RAT
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 03-AUG-2022, entry version 148.
DE RecName: Full=Synapsin-3;
DE AltName: Full=Synapsin III;
GN Name=Syn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX 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 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 complex
RT with synapsin and CAPON.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-469; SER-474;
RP SER-480; SER-483 AND SER-540, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC -!- SUBUNIT: Interacts with CAPON. {ECO:0000269|PubMed:11867766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Peripheral membrane protein localized to the cytoplasmic surface
CC of synaptic vesicles.
CC -!- TISSUE SPECIFICITY: Expressed primarily in brain.
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.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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DR EMBL; AF056704; AAC24521.1; -; mRNA.
DR RefSeq; NP_058805.1; NM_017109.1.
DR AlphaFoldDB; O70441; -.
DR SMR; O70441; -.
DR DIP; DIP-358N; -.
DR MINT; O70441; -.
DR STRING; 10116.ENSRNOP00000036740; -.
DR iPTMnet; O70441; -.
DR PhosphoSitePlus; O70441; -.
DR PaxDb; O70441; -.
DR PRIDE; O70441; -.
DR ABCD; O70441; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000037918; ENSRNOP00000036740; ENSRNOG00000026866.
DR GeneID; 29130; -.
DR KEGG; rno:29130; -.
DR UCSC; RGD:3799; rat.
DR CTD; 8224; -.
DR RGD; 3799; Syn3.
DR eggNOG; KOG3895; Eukaryota.
DR GeneTree; ENSGT00940000155415; -.
DR InParanoid; O70441; -.
DR OrthoDB; 799740at2759; -.
DR PhylomeDB; O70441; -.
DR TreeFam; TF319919; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR PRO; PR:O70441; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0099504; P:synaptic vesicle cycle; ISO:RGD.
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_0000183026"
FT REGION 1..28
FT /note="A"
FT REGION 15..84
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 400..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..72
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; by PKA and CaMK1"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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
