ID A0A2K6ERX8_PROCO Unreviewed; 424 AA.
AC A0A2K6ERX8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Shisa family member 9 {ECO:0000313|Ensembl:ENSPCOP00000004493.1};
GN Name=SHISA9 {ECO:0000313|Ensembl:ENSPCOP00000004493.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000004493.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000004493.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Regulator of short-term neuronal synaptic plasticity in the
CC dentate gyrus. Associates with AMPA receptors (ionotropic glutamate
CC receptors) in synaptic spines and promotes AMPA receptor
CC desensitization at excitatory synapses.
CC {ECO:0000256|ARBA:ARBA00037492}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane
CC {ECO:0000256|ARBA:ARBA00029429}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00029429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the shisa family. SHISA9 subfamily.
CC {ECO:0000256|ARBA:ARBA00038448}.
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DR AlphaFoldDB; A0A2K6ERX8; -.
DR STRING; 379532.ENSPCOP00000004493; -.
DR Ensembl; ENSPCOT00000014658.1; ENSPCOP00000004493.1; ENSPCOG00000012842.1.
DR GeneTree; ENSGT00940000161478; -.
DR OMA; EKTHRPH; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IEA:Ensembl.
DR InterPro; IPR026910; Shisa.
DR PANTHER; PTHR31774:SF1; PROTEIN SHISA-9; 1.
DR PANTHER; PTHR31774; PROTEIN SHISA-9-RELATED; 1.
DR Pfam; PF13908; Shisa; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..424
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014450085"
FT TRANSMEM 152..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 333..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46815 MW; 376EA0603EDA39B8 CRC64;
MRRVLRLLLG CFLTELCARV CRAQERAGHG QLAQLGGVLV LAGGNRSGAA SGEAGEGAGV
SDAPPTRAPT PDFCRGYFDV MGQWDPPFNC SSGDFIFCCG TCGFRFCCTF KKRRLNQSTC
TNYDTPLWLN TGKPPARKDD PLHDPTKDKT NLIVYIICGV VAVMVLVGIF TKLGLEKAHR
PQREHMSRAL ADVMRPQGHC NTDHMERDLN IVVHVQHYEN MDTRTPINNL HTTQMNNAVP
TSPLLQQMGH PHSYPSLGQI SNPYEQQPPG KELNKYASLK AVGSSDGDWT VSTLKSPKAD
KVNDDFYSKR RHLAELASKG NLPLHPVRVE DEPRAFSPEH GPAKQNGQKS RTNKMPPHPL
AYNSTANFKG WDPNEQSLRR QAYGNKGKLG TAESGSSDPL GTRTQHYPPP QPYFITNSKT
EVTV
//