SYN1_BOVIN
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 03-AUG-2022, entry version 160.
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, binds
CC to the cytoskeleton, and is believed to function in the regulation of
CC neurotransmitter release. The complex formed with NOS1 and CAPON
CC proteins is necessary for specific nitric-oxid functions at a
CC presynaptic level (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with CAPON. Forms a ternary complex with
CC NOS1. Isoform Ib interacts with PRNP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse. Golgi apparatus {ECO:0000250}.
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 at least four different protein kinases.
CC Phosphorylation may play a role in the regulation of synapsin-1 in the
CC nerve terminal. {ECO:0000269|PubMed:2108963,
CC ECO:0000269|PubMed:3118371}.
CC -!- PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic
CC vesicles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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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-Linked glycan.
DR iPTMnet; P17599; -.
DR PaxDb; P17599; -.
DR PRIDE; P17599; -.
DR GeneID; 281510; -.
DR KEGG; bta:281510; -.
DR CTD; 6853; -.
DR eggNOG; KOG3895; Eukaryota.
DR InParanoid; P17599; -.
DR OrthoDB; 799740at2759; -.
DR EvolutionaryTrace; P17599; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; 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; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR028713; SYN1.
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:SF24; PTHR10841:SF24; 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 3D-structure; Actin-binding; Alternative splicing; Glycoprotein;
KW Golgi apparatus; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW 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
