ID A0A091D964_FUKDA Unreviewed; 519 AA.
AC A0A091D964;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Synapsin-3 {ECO:0000313|EMBL:KFO27612.1};
GN ORFNames=H920_10997 {ECO:0000313|EMBL:KFO27612.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27612.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27612.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27612.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the synapsin family.
CC {ECO:0000256|ARBA:ARBA00008243}.
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DR EMBL; KN122888; KFO27612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D964; -.
DR STRING; 885580.ENSFDAP00000017394; -.
DR eggNOG; KOG3895; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
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; IPR001359; Synapsin.
DR InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR PANTHER; PTHR10841; SYNAPSIN; 1.
DR PANTHER; PTHR10841:SF27; SYNAPSIN-3; 1.
DR Pfam; PF02750; Synapsin_C; 2.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 90..111
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT DOMAIN 200..337
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 110..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 55595 MW; A6BC369FE4752949 CRC64;
MQVWCGRWQQ RAWERLREGP AQLVRTSEAV FRALPCELTM EDHTSSVSGV DPSPAFCGLQ
GLQGWVKAPT AVTPPGAAAP ANGVLSVFQL TAPHFPMVVK LGHAHAGMGK WSSSETKAEE
RKEGSNSAHP RGGVCSSPAA AQAAAQEAVP GSAKFESELP ILHSPAMQPQ VPTAGLGAIS
DRRGALPWPR FLNTSSVGPR IKVENQLDYQ DITSVVAMAK TYATTEAFID SKYDIRIQKI
GSNYKAYMRT SISGNWKANT GSAMLEQVAM TERYRLWVDS CSEMFGGLDI CAVKAVHSKD
GRDFIIEVMD SSMPLIGEHV EDDRQLMADL VVSRMSQLLL PGATVPSPLR PWTKPAKSPG
QGQLGPQLGQ PQPRPPPQGG PRQAQSPQPP RSRSPSQQRL SPQGQHPLSP QPGSPQPQRS
PGSPQLARAS GGSSPGQASK PGSTLPSQPR PPAQGRSTSQ QVEEPKKTAP LHPHLNKSQS
LTNSLSTSDA SQHGTPSEDE AKAETIRNLR KSFASLFSD
//
