SYN2_RAT
ID SYN2_RAT Reviewed; 586 AA.
AC Q63537; Q9Z1H0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Synapsin-2;
DE AltName: Full=Synapsin II;
GN Name=Syn2;
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] (ISOFORMS IIA AND IIB).
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 PROTEIN SEQUENCE OF 136-143; 178-200; 245-257; 405-414 AND 544-560, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
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 [4]
RP PHOSPHORYLATION AT SER-10, AND PHOSPHOLIPID-BINDING REGION.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422 AND SER-426, AND
RP IDENTIFICATION BY MASS 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. May play a role in noradrenaline secretion by
CC sympathetic neurons (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CAPON. {ECO:0000269|PubMed:11867766}.
CC -!- SUBCELLULAR LOCATION: Synapse.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=IIa;
CC IsoId=Q63537-1; Sequence=Displayed;
CC Name=IIb;
CC IsoId=Q63537-2; Sequence=VSP_006322, VSP_006323;
CC -!- DOMAIN: The A region binds phospholipids with a preference for
CC negatively charged species.
CC -!- PTM: Phosphorylation at Ser-426 by MAPK1/ERK2 and/or MAPK3/ERK1 may
CC play a role in noradrenaline secretion by sympathetic neurons (By
CC similarity). Phosphorylation at Ser-10 dissociates synapsins from
CC synaptic vesicles. {ECO:0000250, ECO:0000269|PubMed:10571231}.
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; M27925; AAA42100.1; -; mRNA.
DR EMBL; M27926; AAA42101.1; -; mRNA.
DR PIR; C30411; C30411.
DR RefSeq; NP_001029192.1; NM_001034020.1. [Q63537-1]
DR RefSeq; NP_062032.1; NM_019159.1. [Q63537-2]
DR PDB; 1I7L; X-ray; 2.35 A; A/B=113-421.
DR PDB; 1I7N; X-ray; 1.90 A; A/B=113-421.
DR PDBsum; 1I7L; -.
DR PDBsum; 1I7N; -.
DR AlphaFoldDB; Q63537; -.
DR SMR; Q63537; -.
DR BioGRID; 247859; 6.
DR IntAct; Q63537; 4.
DR MINT; Q63537; -.
DR STRING; 10116.ENSRNOP00000011292; -.
DR iPTMnet; Q63537; -.
DR PhosphoSitePlus; Q63537; -.
DR SwissPalm; Q63537; -.
DR World-2DPAGE; 0004:Q63537; -.
DR jPOST; Q63537; -.
DR PaxDb; Q63537; -.
DR PRIDE; Q63537; -.
DR ABCD; Q63537; 1 sequenced antibody.
DR GeneID; 29179; -.
DR KEGG; rno:29179; -.
DR UCSC; RGD:3798; rat. [Q63537-1]
DR CTD; 6854; -.
DR RGD; 3798; Syn2.
DR eggNOG; KOG3895; Eukaryota.
DR InParanoid; Q63537; -.
DR OrthoDB; 799740at2759; -.
DR PhylomeDB; Q63537; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR EvolutionaryTrace; Q63537; -.
DR PRO; PR:Q63537; -.
DR Proteomes; UP000002494; Unplaced.
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:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; TAS:RGD.
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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..586
FT /note="Synapsin-2"
FT /id="PRO_0000183023"
FT REGION 1..29
FT /note="A"
FT REGION 20..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..113
FT /note="B; linker"
FT REGION 114..421
FT /note="C; actin-binding and synaptic-vesicle binding"
FT REGION 421..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..458
FT /note="G; Pro-rich linker"
FT REGION 459..537
FT /note="H; Pro/Ser-rich linker"
FT REGION 538..586
FT /note="E"
FT COMPBIAS 55..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine; by PKA and CaMK1"
FT /evidence="ECO:0000269|PubMed:10571231"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 459..479
FT /note="GPGQPQGMQPPGKVLPPRRLP -> CLQYILNCNGIAVGPKQVQAS (in
FT isoform IIb)"
FT /evidence="ECO:0000303|PubMed:2506642"
FT /id="VSP_006322"
FT VAR_SEQ 480..586
FT /note="Missing (in isoform IIb)"
FT /evidence="ECO:0000303|PubMed:2506642"
FT /id="VSP_006323"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:1I7N"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:1I7N"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:1I7N"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:1I7N"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:1I7N"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:1I7N"
FT HELIX 400..418
FT /evidence="ECO:0007829|PDB:1I7N"
SQ SEQUENCE 586 AA; 63457 MW; 630B7071B2F38857 CRC64;
MMNFLRRRLS DSSFIANLPN GYMTDLQRPE PQQPPPAPGP GTATASAATS AASPGPERRP
PPAQAPAPQP APQPAPTPSV GSSFFSSLSQ AVKQTAASAG LVDAPAPSAA SRKAKVLLVV
DEPHTDWAKC FRGKKILGDY DIKVEQAEFS ELNLVAHADG TYAVDMQVLR NGTKVVRSFR
PDFVLIRQHA FGMAENEDFR HLVIGMQYAG LPSINSLESI YNFCDKPWVF AQMVAIFKTL
GGEKFPLIEQ TYYPNHREML TLPTFPVVVK IGHAHSGMGK VKVENHYDFQ DIASVVALTQ
TYATAEPFID AKYDIRVQKI GNNYKAYMRT SISGNWKTNT GSAMLEQIAM SDRYKLWVDA
CSEMFGGLDI CAVKAVHGKD GKDYIFEVMD CSMPLIGEHQ VEDRQLITDL VISKMNQLLS
RTPALSPQRP LTTQQPQSGT LKEPDSSKTP PQRPAPQGGP GQPQGMQPPG KVLPPRRLPS
GPSLPPSSSS SSSSSSSSSA PQRPGGPTST QVNASSSSNS LAEPQAPQAA PPQKPQPHPQ
LNKSQSLTNA FSFSESSFFR SSANEDEAKA ETIRSLRKSF ASLFSD
