SHSA9_MOUSE
ID SHSA9_MOUSE Reviewed; 424 AA.
AC Q9CZN4; D4NZG2; D4NZG3;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein shisa-9;
DE AltName: Full=Cystine-knot AMPAR modulating protein of 44 kDa;
DE Short=CKAMP44;
DE Flags: Precursor;
GN Name=Shisa9;
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] (ISOFORMS 3 AND 4), FUNCTION, IDENTIFICATION BY
RP MASS SPECTROMETRY, IDENTIFICATION IN A AMPA RECEPTOR COMPLEX, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20185686; DOI=10.1126/science.1184178;
RA von Engelhardt J., Mack V., Sprengel R., Kavenstock N., Li K.W.,
RA Stern-Bach Y., Smit A.B., Seeburg P.H., Monyer H.;
RT "CKAMP44: A brain-specific protein attenuating short-term synaptic
RT plasticity in the dentate gyrus.";
RL Science 327:1518-1522(2010).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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. {ECO:0000269|PubMed:20185686}.
CC -!- SUBUNIT: Component of some AMPA receptors (ionotropic glutamate
CC receptors) complex, at least composed of some AMPA receptor (GRIA1,
CC GRIA2 and/or GRIA3), CACNG2 and SHISA9, as well as low level of DLG4.
CC {ECO:0000269|PubMed:20185686}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane
CC {ECO:0000269|PubMed:20185686}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:20185686}. Synapse {ECO:0000269|PubMed:20185686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9CZN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZN4-2; Sequence=VSP_039229, VSP_039230;
CC Name=3; Synonyms=Ckamp44a;
CC IsoId=Q9CZN4-3; Sequence=VSP_039231;
CC Name=4; Synonyms=Ckamp44b;
CC IsoId=Q9CZN4-4; Sequence=VSP_039231, VSP_039232;
CC -!- TISSUE SPECIFICITY: Brain-specific. Mainly expressed in neurons,
CC including in hippocampus, cerebral cortex, striatum, thalamus,
CC olfactory bulb and cerebellum. Expressed in most brain structures
CC during embryonic and postnatal development.
CC {ECO:0000269|PubMed:20185686}.
CC -!- DOMAIN: The extracellular domain contains a pattern of cysteine similar
CC to the snail conotoxin Con-ikot-ikot (AC P0CB20), a toxin known to
CC disrupt AMPA receptors (ionotropic glutamate receptor) desensitization.
CC {ECO:0000269|PubMed:20185686}.
CC -!- DISRUPTION PHENOTYPE: Induces an increase in the paired-pulse ratio of
CC AMPA currents in lateral and medial perforant path-granule cell
CC synapses. {ECO:0000269|PubMed:20185686}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by aberrant splicing sites.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by aberrant splicing sites.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the shisa family. SHISA9 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28201.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU479981; ADD64956.1; -; mRNA.
DR EMBL; GU479982; ADD64957.1; -; mRNA.
DR EMBL; AC154289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK012380; BAB28201.1; ALT_INIT; mRNA.
DR CCDS; CCDS49766.1; -. [Q9CZN4-1]
DR RefSeq; NP_082553.2; NM_028277.2. [Q9CZN4-1]
DR AlphaFoldDB; Q9CZN4; -.
DR SMR; Q9CZN4; -.
DR CORUM; Q9CZN4; -.
DR STRING; 10090.ENSMUSP00000132646; -.
DR GlyGen; Q9CZN4; 3 sites.
DR iPTMnet; Q9CZN4; -.
DR PhosphoSitePlus; Q9CZN4; -.
DR PaxDb; Q9CZN4; -.
DR PRIDE; Q9CZN4; -.
DR ProteomicsDB; 257165; -. [Q9CZN4-1]
DR ProteomicsDB; 257166; -. [Q9CZN4-2]
DR ProteomicsDB; 257167; -. [Q9CZN4-3]
DR ProteomicsDB; 257168; -. [Q9CZN4-4]
DR Antibodypedia; 56266; 88 antibodies from 23 providers.
DR Ensembl; ENSMUST00000170672; ENSMUSP00000132646; ENSMUSG00000022494. [Q9CZN4-1]
DR GeneID; 72555; -.
DR KEGG; mmu:72555; -.
DR UCSC; uc007yfr.1; mouse. [Q9CZN4-2]
DR UCSC; uc007yfs.2; mouse. [Q9CZN4-1]
DR CTD; 729993; -.
DR MGI; MGI:1919805; Shisa9.
DR VEuPathDB; HostDB:ENSMUSG00000022494; -.
DR eggNOG; ENOG502QT2A; Eukaryota.
DR GeneTree; ENSGT00940000161478; -.
DR InParanoid; Q9CZN4; -.
DR OMA; EKTHRPH; -.
DR OrthoDB; 659452at2759; -.
DR PhylomeDB; Q9CZN4; -.
DR TreeFam; TF330800; -.
DR BioGRID-ORCS; 72555; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q9CZN4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZN4; protein.
DR Bgee; ENSMUSG00000022494; Expressed in lumbar subsegment of spinal cord and 107 other tissues.
DR ExpressionAtlas; Q9CZN4; baseline and differential.
DR Genevisible; Q9CZN4; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032591; C:dendritic spine membrane; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0098839; C:postsynaptic density membrane; IC:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:MGI.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:SynGO.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:UniProtKB.
DR InterPro; IPR026910; Shisa.
DR PANTHER; PTHR31774; PTHR31774; 1.
DR Pfam; PF13908; Shisa; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..424
FT /note="Protein shisa-9"
FT /id="PRO_0000394254"
FT TOPO_DOM 24..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 333..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 189..194
FT /note="ALADVM -> RIQRSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039229"
FT VAR_SEQ 195..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039230"
FT VAR_SEQ 231
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:20185686"
FT /id="VSP_039231"
FT VAR_SEQ 283..298
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:20185686"
FT /id="VSP_039232"
SQ SEQUENCE 424 AA; 46842 MW; 0DE039C1C29E9947 CRC64;
MRRVLRLLLG CFLTELCARM CRAQERSGHG QLAQLGGVLL LTGGNRSGAA SGEAGEGVGG
SDAPPTRAPT PDSCRGYFDV MGQWDPPFNC SSGDFIFCCG TCGFRFCCTF KKRRLNQSTC
TNYDTPLWLN TGKPPARKDD PLHDPTKDKT NLIVYIICGV VAVMVLVGIF TKLGLEKAHR
PQREHMSRAL ADVMRPQGHC NTDHMERDLN IVVHVQHYEN MDSRTPINNL HTTQMNNAVP
TSPLLQQMGH PHSYPNLGQI SNPYEQQPPG KELNKYASLK AVGNSDGDWA VATLKSPKAD
KVNDDFYAKR RHLAELAVKG NLPLHPVRVE DEPRAFSPEH GPAQQNGQKS RTNKMPPHPL
AYNSTANFKT WDPSDQSLRR QAYGNKGKLG IAESGSCDPL GTRTQHFPPT QPYFITNSKT
EVTV
