SYN2_MOUSE
ID SYN2_MOUSE Reviewed; 586 AA.
AC Q64332; Q6NZR0; Q9QWV7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Synapsin-2;
DE AltName: Full=Synapsin II;
GN Name=Syn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB).
RC STRAIN=H129; TISSUE=Brain;
RA Han S.J.;
RT "Identification of mouse synapsin IIb.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=8034599; DOI=10.1016/s0021-9258(17)32338-4;
RA Chin L.S., Li L., Greengard P.;
RT "Neuron-specific expression of the synapsin II gene is directed by a
RT specific core promoter and upstream regulatory elements.";
RL J. Biol. Chem. 269:18507-18513(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-586 (ISOFORM IIA).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 59-112; 116-129; 136-143; 178-213; 245-270; 338-353 AND
RP 405-414, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, PHOSPHORYLATION AT SER-426, AND TISSUE SPECIFICITY (ISOFORM IIB).
RX PubMed=22673524; DOI=10.1016/j.febslet.2012.04.021;
RA Inoue D., Kimura I., Wakabayashi M., Tsumoto H., Ozawa K., Hara T.,
RA Takei Y., Hirasawa A., Ishihama Y., Tsujimoto G.;
RT "Short-chain fatty acid receptor GPR41-mediated activation of sympathetic
RT neurons involves synapsin 2b phosphorylation.";
RL FEBS Lett. 586:1547-1554(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. {ECO:0000269|PubMed:22673524}.
CC -!- SUBUNIT: Interacts with CAPON. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=IIa;
CC IsoId=Q64332-1; Sequence=Displayed;
CC Name=IIb;
CC IsoId=Q64332-2; Sequence=VSP_015203, VSP_015204;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in neuronal cells. Isoform
CC IIb is enriched in sympathetic cervical ganglion.
CC {ECO:0000269|PubMed:8034599}.
CC -!- DOMAIN: The A region binds phospholipids with a preference for
CC negatively charged species. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-10 dissociates synapsins from synaptic
CC vesicles (By similarity). Phosphorylation at Ser-426 by MAPK1/ERK2
CC and/or MAPK3/ERK1 may play a role in noradrenaline secretion by
CC sympathetic neurons. {ECO:0000250, ECO:0000269|PubMed:22673524}.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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DR EMBL; AF096867; AAC72966.1; -; mRNA.
DR EMBL; L32026; AAA79964.1; -; Genomic_DNA.
DR EMBL; BC066004; AAH66004.1; -; mRNA.
DR EMBL; BC085129; AAH85129.1; -; mRNA.
DR CCDS; CCDS51874.1; -. [Q64332-1]
DR CCDS; CCDS51875.1; -. [Q64332-2]
DR PIR; I61260; I61260.
DR RefSeq; NP_001104485.1; NM_001111015.1. [Q64332-1]
DR RefSeq; NP_038709.1; NM_013681.3. [Q64332-2]
DR AlphaFoldDB; Q64332; -.
DR SMR; Q64332; -.
DR BioGRID; 203601; 17.
DR CORUM; Q64332; -.
DR IntAct; Q64332; 7.
DR STRING; 10090.ENSMUSP00000009538; -.
DR iPTMnet; Q64332; -.
DR PhosphoSitePlus; Q64332; -.
DR SwissPalm; Q64332; -.
DR MaxQB; Q64332; -.
DR PaxDb; Q64332; -.
DR PeptideAtlas; Q64332; -.
DR PRIDE; Q64332; -.
DR ProteomicsDB; 263175; -. [Q64332-1]
DR ProteomicsDB; 263176; -. [Q64332-2]
DR ABCD; Q64332; 1 sequenced antibody.
DR Antibodypedia; 4054; 126 antibodies from 28 providers.
DR DNASU; 20965; -.
DR Ensembl; ENSMUST00000009538; ENSMUSP00000009538; ENSMUSG00000009394. [Q64332-1]
DR Ensembl; ENSMUST00000169345; ENSMUSP00000133121; ENSMUSG00000009394. [Q64332-2]
DR Ensembl; ENSMUST00000203450; ENSMUSP00000144921; ENSMUSG00000009394. [Q64332-2]
DR GeneID; 20965; -.
DR KEGG; mmu:20965; -.
DR UCSC; uc009dim.3; mouse. [Q64332-2]
DR UCSC; uc009din.2; mouse. [Q64332-1]
DR CTD; 6854; -.
DR MGI; MGI:103020; Syn2.
DR VEuPathDB; HostDB:ENSMUSG00000009394; -.
DR eggNOG; KOG3895; Eukaryota.
DR GeneTree; ENSGT00940000156062; -.
DR HOGENOM; CLU_010582_3_0_1; -.
DR InParanoid; Q64332; -.
DR OMA; CCEIFGG; -.
DR OrthoDB; 799740at2759; -.
DR PhylomeDB; Q64332; -.
DR TreeFam; TF319919; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 20965; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Syn2; mouse.
DR PRO; PR:Q64332; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q64332; protein.
DR Bgee; ENSMUSG00000009394; Expressed in subiculum and 170 other tissues.
DR Genevisible; Q64332; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:SynGO.
DR GO; GO:0099504; P:synaptic vesicle cycle; IMP:SynGO.
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 Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..586
FT /note="Synapsin-2"
FT /id="PRO_0000183022"
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 448..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
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:0000250|UniProtKB:Q63537"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22673524,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 459..479
FT /note="GPGQPQGMQPPGKVLPPRRLP -> CLQYILDCNGIAVGPKQVQAS (in
FT isoform IIb)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015203"
FT VAR_SEQ 480..586
FT /note="Missing (in isoform IIb)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015204"
SQ SEQUENCE 586 AA; 63373 MW; 2B1B6A7453E286FC CRC64;
MMNFLRRRLS DSSFIANLPN GYMTDLQRPE PQQPPPAPGP GAATASAATS 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 PQRPPPQGGP GQPQGMQPPG KVLPPRRLPS
GPSLPSSSSS SSSSSSSSSA PQRPGGPTTT HGDASSSSNS LAEAQAPQAA PAQKPQPHPQ
LNKSQSLTNA FSFSESSFFR SSANEDEAKA ETIRSLRKSF ASLFSD
