ID Q964P7_APLCA Unreviewed; 500 AA.
AC Q964P7;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Synapsin isoform 7.1 {ECO:0000313|EMBL:AAK83049.1};
OS Aplysia californica (California sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6500 {ECO:0000313|EMBL:AAK83049.1};
RN [1] {ECO:0000313|EMBL:AAK83049.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12097493;
RA Angers A., Fioravante D., Chin J., Cleary L.J., Bean A.J., Byrne J.H.;
RT "Serotonin stimulates phosphorylation of Aplysia synapsin and alters its
RT subcellular distribution in sensory neurons.";
RL J. Neurosci. 22:5412-5422(2002).
RN [2] {ECO:0000313|EMBL:AAK83049.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11978861;
RA Chin J., Angers A., Cleary L.J., Eskin A., Byrne J.H.;
RT "Transforming growth factor beta1 alters synapsin distribution and
RT modulates synaptic depression in Aplysia.";
RL J. Neurosci. 22:RC220-RC220(2002).
CC -!- SIMILARITY: Belongs to the synapsin family.
CC {ECO:0000256|ARBA:ARBA00008243}.
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DR EMBL; AF287984; AAK83049.1; -; mRNA.
DR AlphaFoldDB; Q964P7; -.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
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; IPR011761; ATP-grasp.
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; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR PANTHER; PTHR10841; SYNAPSIN; 1.
DR PANTHER; PTHR10841:SF17; SYNAPSIN; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 195..379
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 55025 MW; E440AAC5AC900637 CRC64;
MNYLRRRFSS GDLQGEASDN DDSPNVGGLN FRKGPSPSAP NSPSKSASSA NLGQRLFSSS
SSSSGKPSYN KDRCKTLLVI DDQHTDWSKY FRGKKLFGDW DVRVEQAEFS ELNLAAYSDS
GTMVDIQVTR NGTKVVRSFK PDFVLIRQHV RDAHEDWRNL LLGFKYGAIP SVNSLTAEYN
FLDKPWVFAQ LIEIQKRLGK ESFPLIDQAY YPNHKEMVSN MWLITPKFPV VVKIGHAHSG
LGKVRINNHY DFQDLAGVVA VTQGYSTTEP FIDAKYDLHI QKIGPSYKAF VRKSISGNWK
ANTGSAMLEQ IAMNERFKLW VDECSQLFGG LDVVAVEAIH GKDGREHIIE VNGSSMTLLG
EAQEEDRRLI AELVLAKMQA MCKPVQTSMS KATSSGAIMH QVNGSHSGPQ AGLRSSHAPR
KPGQGRGHDG GPPPQGPMRA PGMPGGPPAP VPRPRHMNNP PPQPFPGQGR PQGCSACASK
DEEDTMKNLR KTFAGIFGDM
//
