ID   SYN1_BOVIN              Reviewed;         706 AA.
AC   P17599;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-NOV-2023, entry version 164.
DE   RecName: Full=Synapsin-1;
DE   AltName: Full=Synapsin I;
GN   Name=SYN1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IA AND IB).
RC   TISSUE=Brain;
RX   PubMed=2506642; DOI=10.1126/science.2506642;
RA   Suedhof T.C., Czernik A.J., Kao H.-T., Takei K., Johnston P.A.,
RA   Horiuchi A., Kanazir S.D., Wagner M.A., Perin M.S., de Camilli P.,
RA   Greengard P.;
RT   "Synapsins: mosaics of shared and individual domains in a family of
RT   synaptic vesicle phosphoproteins.";
RL   Science 245:1474-1480(1989).
RN   [2]
RP   PHOSPHORYLATION AT SER-568 AND SER-605.
RX   PubMed=3118371; DOI=10.1073/pnas.84.21.7518;
RA   Czernik A.J., Pang D.T., Greengard P.;
RT   "Amino acid sequences surrounding the cAMP-dependent and
RT   calcium/calmodulin-dependent phosphorylation sites in rat and bovine
RT   synapsin I.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:7518-7522(1987).
RN   [3]
RP   PHOSPHORYLATION AT SER-551 BY PDPK.
RX   PubMed=2108963; DOI=10.1016/s0021-9258(19)39241-5;
RA   Hall F.L., Mitchell J.P., Vulliet P.R.;
RT   "Phosphorylation of synapsin I at a novel site by proline-directed protein
RT   kinase.";
RL   J. Biol. Chem. 265:6944-6948(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 112-417.
RX   PubMed=9463376; DOI=10.1093/emboj/17.4.977;
RA   Esser L., Wang C.-R., Hosaka M., Smagula C.S., Suedhof T.C.,
RA   Deisenhofer J.;
RT   "Synapsin I is structurally similar to ATP-utilizing enzymes.";
RL   EMBO J. 17:977-984(1998).
CC   -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and
CC       binds to the cytoskeleton. Acts as a regulator of synaptic vesicles
CC       trafficking, involved in the control of neurotransmitter release at the
CC       pre-synaptic terminal (By similarity). Also involved in the regulation
CC       of axon outgrowth and synaptogenesis (By similarity). The complex
CC       formed with NOS1 and CAPON proteins is necessary for specific nitric-
CC       oxid functions at a presynaptic level (By similarity).
CC       {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951,
CC       ECO:0000250|UniProtKB:P17600}.
CC   -!- SUBUNIT: Homodimer (By similarity). Can form oligomers with SYN2 (By
CC       similarity). Interacts with CAPON. Forms a ternary complex with NOS1
CC       (By similarity). Isoform Ib interacts with PRNP (By similarity).
CC       {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951,
CC       ECO:0000250|UniProtKB:P17600}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:O88935}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:O88935}. Presynapse
CC       {ECO:0000250|UniProtKB:P17600}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle {ECO:0000250|UniProtKB:P09951}. Note=Dissociates from
CC       synaptic vesicles and redistributes into the axon during action
CC       potential firing, in a step that precedes fusion of vesicles with the
CC       plasma membrane. Reclusters to presynapses after the cessation of
CC       synaptic activity. {ECO:0000250|UniProtKB:P09951}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=IA;
CC         IsoId=P17599-1; Sequence=Displayed;
CC       Name=IB;
CC         IsoId=P17599-2; Sequence=VSP_006314, VSP_006315;
CC   -!- DOMAIN: The A region binds phospholipids with a preference for
CC       negatively charged species. {ECO:0000250}.
CC   -!- PTM: Substrate of different protein kinases. Phosphorylation, including
CC       phosphorylation at Ser-9, promotes synapsin-1 dissociation from
CC       synaptic vesicles, regulates its rate of dispersion, and controls the
CC       kinetics of vesicle pool turnover and neurotransmitter release (By
CC       similarity). {ECO:0000250|UniProtKB:P09951, ECO:0000269|PubMed:2108963,
CC       ECO:0000269|PubMed:3118371}.
CC   -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M27810; AAA30761.1; -; mRNA.
DR   EMBL; M27811; AAA30762.1; -; mRNA.
DR   PIR; E30411; E30411.
DR   RefSeq; NP_776616.1; NM_174191.2. [P17599-1]
DR   PDB; 1AUV; X-ray; 2.15 A; A/B=110-420.
DR   PDB; 1AUX; X-ray; 2.30 A; A/B=110-420.
DR   PDBsum; 1AUV; -.
DR   PDBsum; 1AUX; -.
DR   AlphaFoldDB; P17599; -.
DR   SMR; P17599; -.
DR   STRING; 9913.ENSBTAP00000027503; -.
DR   BindingDB; P17599; -.
DR   ChEMBL; CHEMBL3817719; -.
DR   GlyConnect; 581; 1 O-GlcNAc glycan.
DR   GlyCosmos; P17599; 9 sites, 1 glycan.
DR   iPTMnet; P17599; -.
DR   PaxDb; 9913-ENSBTAP00000027503; -.
DR   GeneID; 281510; -.
DR   KEGG; bta:281510; -.
DR   CTD; 6853; -.
DR   eggNOG; KOG3895; Eukaryota.
DR   InParanoid; P17599; -.
DR   OrthoDB; 5487039at2759; -.
DR   EvolutionaryTrace; P17599; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:AgBase.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
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:SF24; SYNAPSIN-1; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW   Cytoplasmic vesicle; Glycoprotein; Golgi apparatus; Methylation;
KW   Phosphoprotein; Reference proteome; Repeat; Synapse.
FT   CHAIN           1..706
FT                   /note="Synapsin-1"
FT                   /id="PRO_0000183016"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..28
FT                   /note="A"
FT   REGION          29..112
FT                   /note="B; linker"
FT   REGION          113..420
FT                   /note="C; actin-binding and synaptic-vesicle binding"
FT   REGION          418..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..656
FT                   /note="D; Pro-rich linker"
FT   REGION          657..706
FT                   /note="E"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..41
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..556
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..630
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine; by CaMK1 and PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P09951"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09951"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09951"
FT   MOD_RES         312
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         430
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         432
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09951"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         476
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         534
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         547
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         551
FT                   /note="Phosphoserine; by PDPK1"
FT                   /evidence="ECO:0000269|PubMed:2108963"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17600"
FT   MOD_RES         556
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         568
FT                   /note="Phosphoserine; by CaMK2"
FT                   /evidence="ECO:0000305|PubMed:3118371"
FT   MOD_RES         605
FT                   /note="Phosphoserine; by CaMK2"
FT                   /evidence="ECO:0000305|PubMed:3118371"
FT   MOD_RES         622
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         666
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         680
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   MOD_RES         684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88935"
FT   CARBOHYD        55
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        87
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        96
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        261
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        432
FT                   /note="O-linked (GlcNAc) serine; alternate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        526
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        564
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        578
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         662..670
FT                   /note="NKSQSLTNA -> KASPAQAQP (in isoform IB)"
FT                   /evidence="ECO:0000303|PubMed:2506642"
FT                   /id="VSP_006314"
FT   VAR_SEQ         671..706
FT                   /note="Missing (in isoform IB)"
FT                   /evidence="ECO:0000303|PubMed:2506642"
FT                   /id="VSP_006315"
FT   STRAND          114..119
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           126..130
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          161..169
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   TURN            192..195
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           199..207
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           216..221
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           225..239
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   TURN            241..243
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          250..254
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          262..272
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   TURN            275..278
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           285..296
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          310..319
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          322..328
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           351..360
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           361..365
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          368..377
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   STRAND          382..388
FT                   /evidence="ECO:0007829|PDB:1AUV"
FT   HELIX           399..415
FT                   /evidence="ECO:0007829|PDB:1AUV"
SQ   SEQUENCE   706 AA;  74518 MW;  89373750BF014340 CRC64;
     MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPAAPSP GATTGPATAT AERASSAAPV
     ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG GGSGGAGRGG AAARVLLVID
     EPHTDWAKYF KGKKIHGEID IKVEQAEFSD LNLVAHANGG FSVDMEVLRN GVKVVRSLKP
     DFVLIRQHAF SMARNGDYRS LVIGLQYAGI PSINSLHSVY NFCDKPWVFA QMVRLHKKLG
     TEEFPLINQT FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT
     YATTEPFIDA KYDVRIQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS DRYKLWVDTC
     SEIFGGLDIC AVEALHGKDG RDHIIQVVGS SMPLIGDHQD EDKQLIVELV VNKMAQALPR
     QRQRDASPGR GSHSQTPSPG ALPLGRQISQ QPAGPPAQQR PPPQGGPPQP GPGPQRQGPP
     LQQRPTPQGQ QHLSGLGPPA GSPLPQRLPS PTSVPQQPAS QATPMTQGQG RQSRPVAGGP
     GAPPATRPPA SPSPQRQAGP PQATRQTSVS GQAPPKASGV PPGGQQRQGP PQKPPGPAGP
     TRQASQAGPM PRTGPPTTQQ PRPSGPGPAG RPTKPQLAQK PSQDVPPPAT AAAGGPPHPQ
     LNKSQSLTNA FNLPEPAPPR PSLSQDEVKA ETIRSLRKSF ASLFSD
//