SYN1_RAT
ID SYN1_RAT Reviewed; 704 AA.
AC P09951; Q9WUX7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Synapsin-1;
DE AltName: Full=Synapsin I;
GN Name=Syn1;
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=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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3028773; DOI=10.1002/j.1460-2075.1986.tb04625.x;
RA McCaffery C.A., Degennaro L.J.;
RT "Determination and analysis of the primary structure of the nerve terminal
RT specific phosphoprotein, synapsin I.";
RL EMBO J. 5:3167-3173(1986).
RN [3]
RP PROTEIN SEQUENCE OF 177-186 AND 239-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION AT SER-566 AND SER-603.
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 [5]
RP GLYCOSYLATION AT SER-55; THR-56; THR-87; SER-516; THR-524; THR-562 AND
RP SER-576.
RX PubMed=10386995; DOI=10.1046/j.1471-4159.1999.0730418.x;
RA Cole R.N., Hart G.W.;
RT "Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-
RT acetylglucosamine residues are localized within domains mediating synapsin
RT I interactions.";
RL J. Neurochem. 73:418-428(1999).
RN [6]
RP PHOSPHORYLATION AT SER-9.
RX PubMed=10571231; DOI=10.1016/s0896-6273(00)80851-x;
RA Hosaka M., Hammer R.E., Sudhof T.C.;
RT "A phospho-switch controls the dynamic association of synapsins with
RT synaptic vesicles.";
RL Neuron 24:377-387(1999).
RN [7]
RP GLYCOSYLATION AT SER-55; THR-87; SER-96; SER-103; SER-261; SER-430 AND
RP SER-516.
RX PubMed=12438562; DOI=10.1074/mcp.m200048-mcp200;
RA Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J., Hart G.W.;
RT "Mapping sites of O-GlcNAc modification using affinity tags for serine and
RT threonine post-translational modifications.";
RL Mol. Cell. Proteomics 1:791-804(2002).
RN [8]
RP INTERACTION WITH NOS1 AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-62; SER-67; SER-425;
RP THR-434; SER-436; SER-566 AND SER-664, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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: Neuronal phosphoprotein that coats synaptic vesicles, binds
CC to the cytoskeleton, and is believed to function in the regulation of
CC neurotransmitter release.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CAPON. Forms a
CC ternary complex with NOS1. Isoform Ib interacts with PRNP (By
CC 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=P09951-1; Sequence=Displayed;
CC Name=IB;
CC IsoId=P09951-2; Sequence=VSP_006318, VSP_006319;
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. It is
CC probable that phosphorylation plays a role in the regulation of
CC synapsin-1 in the nerve terminal (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic
CC vesicles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28353.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; M27812; AAA42145.1; -; mRNA.
DR EMBL; M27924; AAA42148.1; -; mRNA.
DR EMBL; X04655; CAA28353.1; ALT_SEQ; mRNA.
DR PIR; A25704; A25704.
DR PIR; A30411; A30411.
DR RefSeq; NP_001104252.1; NM_001110782.2. [P09951-2]
DR RefSeq; NP_062006.1; NM_019133.2. [P09951-1]
DR PDB; 1PK8; X-ray; 2.10 A; A/B/C/D/E/F/G/H=2-421.
DR PDB; 1PX2; X-ray; 2.23 A; A/B=2-421.
DR PDBsum; 1PK8; -.
DR PDBsum; 1PX2; -.
DR AlphaFoldDB; P09951; -.
DR SMR; P09951; -.
DR BioGRID; 247051; 6.
DR CORUM; P09951; -.
DR IntAct; P09951; 7.
DR MINT; P09951; -.
DR STRING; 10116.ENSRNOP00000014250; -.
DR GlyGen; P09951; 11 sites.
DR iPTMnet; P09951; -.
DR PhosphoSitePlus; P09951; -.
DR jPOST; P09951; -.
DR PaxDb; P09951; -.
DR PRIDE; P09951; -.
DR ABCD; P09951; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000014250; ENSRNOP00000014250; ENSRNOG00000010365. [P09951-1]
DR GeneID; 24949; -.
DR KEGG; rno:24949; -.
DR UCSC; RGD:3797; rat. [P09951-1]
DR CTD; 6853; -.
DR RGD; 3797; Syn1.
DR eggNOG; KOG3895; Eukaryota.
DR GeneTree; ENSGT00940000161978; -.
DR HOGENOM; CLU_010582_3_0_1; -.
DR InParanoid; P09951; -.
DR OMA; APMTQGQ; -.
DR OrthoDB; 799740at2759; -.
DR PhylomeDB; P09951; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR EvolutionaryTrace; P09951; -.
DR PRO; PR:P09951; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000010365; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; P09951; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0000795; C:synaptonemal complex; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; IMP:RGD.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0099504; P:synaptic vesicle cycle; ISO:RGD.
DR DisProt; DP02741; -.
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;
KW Direct protein sequencing; Glycoprotein; Golgi apparatus; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..704
FT /note="Synapsin-1"
FT /id="PRO_0000183020"
FT REGION 1..28
FT /note="A"
FT REGION 15..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..112
FT /note="B; linker"
FT REGION 113..420
FT /note="C; actin-binding and synaptic-vesicle binding"
FT REGION 418..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..655
FT /note="D; Pro-rich linker"
FT REGION 656..704
FT /note="E"
FT COMPBIAS 25..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
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:0000305|PubMed:10571231"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 312
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 428
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 430
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 434
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 474
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 532
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 545
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 551
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P17600"
FT MOD_RES 554
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 566
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000305|PubMed:3118371,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 603
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000305|PubMed:3118371"
FT MOD_RES 620
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 678
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT CARBOHYD 55
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:10386995,
FT ECO:0000269|PubMed:12438562"
FT CARBOHYD 56
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000305|PubMed:10386995"
FT CARBOHYD 87
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:10386995,
FT ECO:0000269|PubMed:12438562"
FT CARBOHYD 96
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:12438562"
FT CARBOHYD 103
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000305|PubMed:12438562"
FT CARBOHYD 261
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:12438562"
FT CARBOHYD 430
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:12438562"
FT CARBOHYD 516
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:10386995,
FT ECO:0000269|PubMed:12438562"
FT CARBOHYD 524
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:10386995"
FT CARBOHYD 562
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:10386995"
FT CARBOHYD 576
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:10386995"
FT VAR_SEQ 660..668
FT /note="NKSQSLTNA -> KASPAQAQP (in isoform IB)"
FT /evidence="ECO:0000305"
FT /id="VSP_006318"
FT VAR_SEQ 669..704
FT /note="Missing (in isoform IB)"
FT /evidence="ECO:0000305"
FT /id="VSP_006319"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:1PK8"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:1PK8"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:1PK8"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 322..333
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:1PK8"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:1PK8"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1PX2"
FT HELIX 399..415
FT /evidence="ECO:0007829|PDB:1PK8"
SQ SEQUENCE 704 AA; 73988 MW; 65799FEF7CFE18B5 CRC64;
MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPSAASP GATPGSAAAS AERASTAAPV
ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG GGSGGAGRGG AAARVLLVID
EPHTDWAKYF KGKKIHGEID IKVEQAEFSD LNLVAHANGG FSVDMEVLRN GVKVVRSLKP
DFVLIRQHAF SMARNGDYRS LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG
TEEFPLIDQT FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT
YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS DRYKLWVDTC
SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD EDKQLIVELV VNKMTQALPR
QRDASPGRGS HSQTPSPGAL PLGRQTSQQP AGPPAQQRPP PQGGPPQPGP GPQRQGPPLQ
QRPPPQGQQH LSGLGPPAGS PLPQRLPSPT AAPQQSASQA TPMTQGQGRQ SRPVAGGPGA
PPAARPPASP SPQRQAGPPQ ATRQASISGP APPKVSGASP GGQQRQGPPQ KPPGPAGPIR
QASQAGPGPR TGPPTTQQPR PSGPGPAGRP TKPQLAQKPS QDVPPPIIAA AGGPPHPQLN
KSQSLTNAFN LPEPAPPRPS LSQDEVKAET IRSLRKSFAS LFSD
