SHSA8_MOUSE
ID SHSA8_MOUSE Reviewed; 399 AA.
AC J3QNX5;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein shisa-8 {ECO:0000305};
DE AltName: Full=Cystine-knot AMPAR modulating protein of 39 kDa {ECO:0000303|PubMed:26623514};
DE Short=CKAMP39 {ECO:0000303|PubMed:26623514};
DE AltName: Full=Shisa family member 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=Shisa8 {ECO:0000303|PubMed:26623514, ECO:0000312|MGI:MGI:2146080};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP FUNCTION, AND INTERACTION WITH GRIA1 AND GRIA2.
RC STRAIN=C57BL/6N;
RX PubMed=26623514; DOI=10.7554/elife.09693;
RA Farrow P., Khodosevich K., Sapir Y., Schulmann A., Aslam M., Stern-Bach Y.,
RA Monyer H., von Engelhardt J.;
RT "Auxiliary subunits of the CKAMP family differentially modulate AMPA
RT receptor properties.";
RL Elife 4:E09693-E09693(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May regulate trafficking and current kinetics of AMPA-type
CC glutamate receptor (AMPAR) at synapses. {ECO:0000269|PubMed:26623514}.
CC -!- SUBUNIT: Interacts with AMPAR subunits GRIA1 and GRIA2.
CC {ECO:0000305|PubMed:26623514}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain-specific. Highly expressed in cerebellum and
CC olfactory bulb. {ECO:0000269|PubMed:26623514}.
CC -!- DEVELOPMENTAL STAGE: Undetectable in the brain of 17 dpc embryos.
CC Expressed in olfactory bulb from postnatal day 1 (P1) and then in
CC cerebellum from postnatal day 14 (P14). {ECO:0000269|PubMed:26623514}.
CC -!- SIMILARITY: Belongs to the shisa family. {ECO:0000305}.
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DR EMBL; KU707903; AND76926.1; -; mRNA.
DR EMBL; AC105358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS56994.1; -.
DR RefSeq; NP_001193950.1; NM_001207021.1.
DR AlphaFoldDB; J3QNX5; -.
DR SMR; J3QNX5; -.
DR STRING; 10090.ENSMUSP00000137002; -.
DR GlyGen; J3QNX5; 1 site.
DR iPTMnet; J3QNX5; -.
DR PhosphoSitePlus; J3QNX5; -.
DR PaxDb; J3QNX5; -.
DR PRIDE; J3QNX5; -.
DR ProteomicsDB; 334882; -.
DR Antibodypedia; 71661; 4 antibodies from 4 providers.
DR Ensembl; ENSMUST00000179269; ENSMUSP00000137002; ENSMUSG00000096883.
DR GeneID; 435145; -.
DR KEGG; mmu:435145; -.
DR UCSC; uc029sua.1; mouse.
DR CTD; 440829; -.
DR MGI; MGI:2146080; Shisa8.
DR VEuPathDB; HostDB:ENSMUSG00000096883; -.
DR eggNOG; ENOG502R5Y2; Eukaryota.
DR GeneTree; ENSGT00940000163233; -.
DR HOGENOM; CLU_045403_1_0_1; -.
DR InParanoid; J3QNX5; -.
DR OMA; INASQMP; -.
DR OrthoDB; 558642at2759; -.
DR TreeFam; TF330800; -.
DR BioGRID-ORCS; 435145; 4 hits in 73 CRISPR screens.
DR PRO; PR:J3QNX5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; J3QNX5; protein.
DR Bgee; ENSMUSG00000096883; Expressed in cerebellar cortex and 24 other tissues.
DR ExpressionAtlas; J3QNX5; baseline and differential.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0032591; C:dendritic spine membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR026910; Shisa.
DR PANTHER; PTHR31774; PTHR31774; 1.
DR Pfam; PF13908; Shisa; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..399
FT /note="Protein shisa-8"
FT /evidence="ECO:0000255"
FT /id="PRO_5011942382"
FT TOPO_DOM 37..136
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 207..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 399 AA; 42462 MW; EECF5CE3B1B8664F CRC64;
MERAGARGQR CGRRSHGLPL ALRLALLLAG SPSGRAGAPE EQEIAGSGTV APAGGDRCRG
YYDVMGQWDP PFNCSSGVYS FCCGTCGYRF CCHDGPRRLD QSRCSNYDTP AWVQTGRPPA
RARDTAAPRD PARERSHTAV YAVCGVAALL VLVGIGARLG LERAHSPRAR RTVTRTLTEL
LKQPGPQEPL PPPLGPPLGN CVQVQMGDGV LRGSPHNSTD KKRLNNAPLG SATPGPPRGP
RLQGGGSLTL QPDYAKFATL KAAALKATEV APQDFYQRFP STETGPRTLP ARVPRPPEDL
PALLDACPWA PPGYVPPAGP VSSVPYAAWT AGRPARPLPR SHLVAQVSPA PRRPNHAPRR
QFSVEKLPEA FSAQQASFYS SAGRGPRHLS TNSKAEVTV
