ID   SHA9B_DANRE             Reviewed;         393 AA.
AC   B3DHW5; A8KB48;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Protein shisa-9B;
DE   Flags: Precursor;
GN   Name=shisa9b;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of some AMPA receptors (ionotropic glutamate
CC       receptors) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Synapse {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the shisa family. SHISA9 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI53965.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC153964; AAI53965.1; ALT_INIT; mRNA.
DR   EMBL; BC162913; AAI62913.1; -; mRNA.
DR   EMBL; BC162933; AAI62933.1; -; mRNA.
DR   RefSeq; NP_001129447.2; NM_001135975.2.
DR   AlphaFoldDB; B3DHW5; -.
DR   SMR; B3DHW5; -.
DR   STRING; 7955.ENSDARP00000069025; -.
DR   PaxDb; B3DHW5; -.
DR   GeneID; 566015; -.
DR   KEGG; dre:566015; -.
DR   CTD; 566015; -.
DR   ZFIN; ZDB-GENE-081022-105; shisa9b.
DR   eggNOG; ENOG502QT2A; Eukaryota.
DR   InParanoid; B3DHW5; -.
DR   OrthoDB; 659452at2759; -.
DR   PhylomeDB; B3DHW5; -.
DR   PRO; PR:B3DHW5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IBA:GO_Central.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0032591; C:dendritic spine membrane; ISS:UniProtKB.
DR   GO; GO:0008328; C:ionotropic glutamate receptor complex; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:2000311; P:regulation of AMPA receptor activity; IBA:GO_Central.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR   InterPro; IPR026910; Shisa.
DR   PANTHER; PTHR31774; PTHR31774; 1.
DR   Pfam; PF13908; Shisa; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Glycoprotein; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..393
FT                   /note="Protein shisa-9B"
FT                   /id="PRO_0000394256"
FT   TOPO_DOM        21..131
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          28..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        202
FT                   /note="Q -> R (in Ref. 1; AAI53965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="S -> N (in Ref. 1; AAI53965)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  43434 MW;  A949920A8D48FB07 CRC64;
     MKSTGLLLGY FLMKVLVCDA EGEPGKSLDG AVTASGSNDS RDGENGLSET PHTEDRCRGY
     YDVMGQWDPP FVCRTGSYLY CCGTCGFRFC CEFKNSRLDQ TTCKNYDTPP WSMTGRPPPK
     MMDQHDPTKD KTNLIVYIIC GVVAIMALVG IFTKLGLEKA HRPHRENMSR ALAQVMRQTA
     PGEHVEREES LAVHGQPYEN LQARATGNNL QSAQMNSVGP SSSMMQAMTP YPALGQVPVA
     HPYEPSPAAK ELNKYASLKA VAEKANENFY TNRRHLADLA AKGTLPMHSV SLEQEPTNPY
     SPELPCQKQN GHKSKSTKVH SSHPLAYGSN TIANPGRMSS WETTETLGRR HTYGPKKHSA
     TMEQMNELTS AQSQHYLPPH PYFVTNSKTE VTV