ID A0A8C3XF63_9PASS Unreviewed; 587 AA.
AC A0A8C3XF63;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 19.
DE RecName: Full=Synapsin-2 {ECO:0000256|ARBA:ARBA00069141};
DE AltName: Full=Synapsin II {ECO:0000256|ARBA:ARBA00080999};
OS Cyanoderma ruficeps (rufous-capped babbler).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Timaliidae; Cyanoderma.
OX NCBI_TaxID=181631 {ECO:0000313|Ensembl:ENSCRFP00000016364.1, ECO:0000313|Proteomes:UP000694396};
RN [1] {ECO:0000313|Ensembl:ENSCRFP00000016364.1}
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; A0A8C3XF63; -.
DR Ensembl; ENSCRFT00000016935.1; ENSCRFP00000016364.1; ENSCRFG00000012553.1.
DR Proteomes; UP000694396; 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:UP000694396};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 110..211
FT /note="Synapsin pre-ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF02078"
FT DOMAIN 213..415
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 16..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..510
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 64788 MW; 141CF8136F9EA41F CRC64;
MMNFLRRRLS DSSFIANLPN GYMTDLQRPE PQQPPPPPPS AGSSAPASGS PAAERRQPPQ
PAPPQQQQPP PPQQSTGSSF FSSLSNAVKQ TAASAGLVDA SAAVSAAVGR KFKLLLVIDE
PHTDWAKAFR GKKVHGEYDI KVEQAEFSEI NLIAHADGNY AVDIQVIRNG TKVVRSFRPD
FVLVRQHSYS MAENEDFRNL IIGMQYAGIP SVNSLQSIYN FCDKPWVFAQ LVSVYKTLGP
EKFPLIEQTF YPNHKEMLTM PTFPVVVKIG HAHSGMGKIK VDNHYDFQDI ASVVALTQTY
ATTEPFIDSK YDIRIQKIGS NYKAYMRTSI SGNWKTNTGS AMLEQIAMSD KYKLWVDTCS
EIFGGLDICA VKAVHGKDGK DYIFEVMDSA MPLIGEHQAE DRQHITELVV SKMNQMLSKT
PIPSPQRPTA TQQPQSGSLK EPEPNKIPPQ RPPPQGGPVH PQGMQSQSQE PLQPQRVFPA
GQAAKPAASQ PQRPPGPTTQ QPRPQAQGPP SSRLSKEAEP QPQPQQEPQP APQQKPQSHP
QLNKSQSLTN AFSFTESSFF RSSVNEDEAK AETIRNLRKS FASLFSD
//
