ID A0A9J8DKV3_CYPCA Unreviewed; 612 AA.
AC A0A9J8DKV3;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 10-JUN-2026, entry version 13.
DE RecName: Full=Synapsin-2 {ECO:0000256|ARBA:ARBA00069141};
DE AltName: Full=Synapsin II {ECO:0000256|ARBA:ARBA00080999};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000179035.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000179035.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
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:0000256|ARBA:ARBA00056023}.
CC -!- SUBUNIT: Can form oligomers with SYN1. Interacts with CAPON.
CC {ECO:0000256|ARBA:ARBA00064131}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the synapsin family.
CC {ECO:0000256|ARBA:ARBA00008243}.
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DR AlphaFoldDB; A0A9J8DKV3; -.
DR Ensembl; ENSCCRT00000112713.1; ENSCCRP00000179035.1; ENSCCRG00000039284.2.
DR GeneTree; ENSGT00940000167517; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR FunFam; 3.30.1490.20:FF:000008; Synapsin I; 1.
DR FunFam; 3.40.50.20:FF:000008; Synapsin III; 1.
DR FunFam; 3.30.470.20:FF:000151; Synapsin-2; 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:SF20; SYNAPSIN-2; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001108240};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 105..207
FT /note="Synapsin pre-ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF02078"
FT DOMAIN 209..382
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 15..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..576
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..65
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..409
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 66639 MW; 3DBC08BF4811E504 CRC64;
MNFLRRRLSD SSFIANLPNG YMSDLQRPDP PPPPPPTAAT KAPAGSTPAP SAPPAAKSPT
ASPAPERQPQ PAQSAGSGFF SSFTNVVKQT AASAGLVEQS PAAVSRKFKI LLVIDEPQHE
WAKVFRGKKV QGDHDVKVEQ AEFSEINLVA HANGTCSVDM QVIRNGTKVV RSFKPDFVLV
RQHAYSMAQN EDFRNIIIGL QYAGIPSVNS LESIYNLCDK PWAFSQLISI YKKLGADKFP
LVDQTFYSNY RDMISMPTFP AVVKIGHAHS GMGKVKVDNH SDFQDIASVV AITQTYTTTE
PFIDAKYDIR VQKIGSDYKA YMRTSISGNW KSNTGSAMLE QVAMTDKYKL WVDTCADVFG
GLDICAVKAI HGKDGKDYIT EVRPVPKAGP TPTLPPTTQQ PKPQAQATPE PTPGKPTELP
PKRHPPKPLP PKPVPPVRRN SKPQIQPKPQ TPPPTKAQPK AQLGERDQNP GQTPPDPVLA
QEQSPAKVPI KPPSPAKPQL QPKPVLREQV KPEAQDQTTA PSEALSAPVR ATPSPAPNPA
QPTPMKPTHS QPPVEEQPAP QQKSTHPLLN KSQSLTNAFN AFGETFRSSN EDEAKAETIR
NLRKSFASLF SD
//
