INSY1_BOVIN
ID INSY1_BOVIN Reviewed; 292 AA.
AC A7YWL5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Inhibitory synaptic factor 1 {ECO:0000305};
DE Short=InSyn1 {ECO:0000250|UniProtKB:Q8CD60};
GN Name=INSYN1 {ECO:0000250|UniProtKB:Q2T9L4};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the protein machinery at the inhibitory
CC synapses, probably acting as a scaffold. Inhibitory synapses dampen
CC neuronal activity through postsynaptic hyperpolarization. This synaptic
CC inhibition is fundamental for the functioning of the central nervous
CC system, shaping and orchestrating the flow of information through
CC neuronal networks to generate a precise neural code.
CC {ECO:0000250|UniProtKB:Q8CD60}.
CC -!- SUBUNIT: Interacts with GPHN. {ECO:0000250|UniProtKB:Q8CD60}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000250|UniProtKB:Q8CD60}.
CC -!- SIMILARITY: Belongs to the INSYN1 family. {ECO:0000305}.
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DR EMBL; BC134648; AAI34649.1; -; mRNA.
DR RefSeq; NP_001098902.1; NM_001105432.1.
DR AlphaFoldDB; A7YWL5; -.
DR SMR; A7YWL5; -.
DR STRING; 9913.ENSBTAP00000036346; -.
DR PaxDb; A7YWL5; -.
DR GeneID; 613490; -.
DR KEGG; bta:613490; -.
DR CTD; 388135; -.
DR eggNOG; ENOG502R2SS; Eukaryota.
DR OrthoDB; 1272531at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISS:UniProtKB.
DR InterPro; IPR027997; Largen/INSYN1.
DR PANTHER; PTHR15917; PTHR15917; 1.
DR Pfam; PF15252; DUF4589; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Reference proteome; Synapse.
FT CHAIN 1..292
FT /note="Inhibitory synaptic factor 1"
FT /id="PRO_0000337044"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..63
FT /evidence="ECO:0000255"
FT COMPBIAS 200..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 31695 MW; 69F6D42CB9D60B6D CRC64;
MNIRGTPDLG QPSDDPSSGG ERERIRQRMK MVIGQLEDIL RELKEVAKEL REVVSQIDKL
TSDFDFELEP DDWTTATVSS TSSSDKAGVG GPFDLGHLDF MTADILSDSW EFCSFLDIST
PSDSVDCPES TRPGAGPDYQ LMNGGLPVPN GPRVETPDSS SEEAFSAGPV KGQLPQRTPG
TRERVRFSDK VLYHALCCDD EEGDGEEEAA EEEGGLSPEP AHTEAPAGPL KPSPAPYKPR
RSPLTGRRSG PTSVPEQTRR VTRNSSTQTV SDKSTQTVLP YTATRQKAKG KN