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Database: UniProt
Entry: A0A8C5L8N1_JACJA
LinkDB: A0A8C5L8N1_JACJA
Original site: A0A8C5L8N1_JACJA 
ID   A0A8C5L8N1_JACJA        Unreviewed;       706 AA.
AC   A0A8C5L8N1;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   10-JUN-2026, entry version 20.
DE   RecName: Full=Synapsin-1 {ECO:0000256|ARBA:ARBA00017852};
DE   AltName: Full=Synapsin I {ECO:0000256|ARBA:ARBA00029646};
GN   Name=Syn1 {ECO:0000313|Ensembl:ENSJJAP00000019854.1};
OS   Jaculus jaculus (Lesser Egyptian jerboa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Dipodoidea;
OC   Dipodidae; Dipodinae; Jaculus.
OX   NCBI_TaxID=51337 {ECO:0000313|Ensembl:ENSJJAP00000019854.1, ECO:0000313|Proteomes:UP000694385};
RN   [1] {ECO:0000313|Ensembl:ENSJJAP00000019854.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBUNIT: Homodimer. Can form oligomers with SYN2. Interacts with CAPON.
CC       Forms a ternary complex with NOS1. Isoform Ib interacts with PRNP.
CC       {ECO:0000256|ARBA:ARBA00046960}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle {ECO:0000256|ARBA:ARBA00004234}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Presynapse
CC       {ECO:0000256|ARBA:ARBA00034106}.
CC   -!- SIMILARITY: Belongs to the synapsin family.
CC       {ECO:0000256|ARBA:ARBA00008243}.
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DR   RefSeq; XP_004668871.1; XM_004668814.2.
DR   AlphaFoldDB; A0A8C5L8N1; -.
DR   Ensembl; ENSJJAT00000026391.1; ENSJJAP00000019854.1; ENSJJAG00000020700.1.
DR   GeneID; 101606523; -.
DR   CTD; 6853; -.
DR   GeneTree; ENSGT00940000161978; -.
DR   OMA; MSDKYKM; -.
DR   OrthoDB; 10249572at2759; -.
DR   Proteomes; UP000694385; Unassembled WGS sequence.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0044297; C:cell body; IEA:Ensembl.
DR   GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR   GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0099504; P:synaptic vesicle cycle; IEA:Ensembl.
DR   FunFam; 3.30.1490.20:FF:000008; Synapsin I; 1.
DR   FunFam; 3.30.470.20:FF:000042; Synapsin III; 1.
DR   FunFam; 3.40.50.20:FF:000008; Synapsin III; 1.
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   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694385};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          113..212
FT                   /note="Synapsin pre-ATP-grasp"
FT                   /evidence="ECO:0000259|Pfam:PF02078"
FT   DOMAIN          214..416
FT                   /note="Synapsin ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02750"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..69
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..473
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..499
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..524
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..552
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..590
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..633
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  74305 MW;  A31D645CCEEBB84F CRC64;
     MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPSAASP GATPGSATAS TDRASTAAPV
     ASQAAPSPGS 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 VNKMAQALPR
     QRPRDASPGR GSHSQTPSPG ALPLGRQTSQ QPVGPPAQQR PPPQGGPPQP GPGPQRQGPP
     LQQRPPPQGQ QHLSGLGPPA GSPLPQRLPS PTSTPQQPVS QATPMTQGQG RQSRPVAGGP
     GAPPTARPPA SPSPQRQAGP PQAPRQASVS GPAPPKASGA PPGGQQRQGP PQKPPGPAGP
     TRQASQAGPG PRSGPPTTQQ PRPSGPSPAG RPAKPQLAQK SSQDVPPPAT AAAGGPPHPQ
     LNKSQSLTNA FNLPEPAPPR PSLSQDEVKA ETIRSLRKSF ASLFSD
//
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