ID RHG44_MOUSE Reviewed; 814 AA.
AC Q5SSM3; Q5SSM4; Q5SSM6; Q5SSM7; Q7TNB9; Q8BW90;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=Rho GTPase-activating protein 44 {ECO:0000305};
DE AltName: Full=Rho-type GTPase-activating protein RICH2 {ECO:0000303|PubMed:24352656};
DE AltName: Full=RhoGAP interacting with CIP4 homologs protein 2;
DE Short=RICH-2;
GN Name=Arhgap44 {ECO:0000312|MGI:MGI:2144423};
GN Synonyms=Rich2 {ECO:0000303|PubMed:24352656};
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 [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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).
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; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION IN LONG-TERM POTENTIATION, DOMAIN, INTERACTION WITH SHANK3,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-291.
RX PubMed=23739967; DOI=10.1523/jneurosci.2725-12.2013;
RA Raynaud F., Janossy A., Dahl J., Bertaso F., Perroy J., Varrault A.,
RA Vidal M., Worley P.F., Boeckers T.M., Bockaert J., Marin P., Fagni L.,
RA Homburger V.;
RT "Shank3-Rich2 interaction regulates AMPA receptor recycling and synaptic
RT long-term potentiation.";
RL J. Neurosci. 33:9699-9715(2013).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24352656; DOI=10.1074/jbc.m113.534636;
RA Raynaud F., Moutin E., Schmidt S., Dahl J., Bertaso F., Boeckers T.M.,
RA Homburger V., Fagni L.;
RT "Rho-GTPase-activating protein interacting with Cdc-42-interacting protein
RT 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1
RT (Rac1) GTPase-activating protein that controls dendritic spine
RT morphogenesis.";
RL J. Biol. Chem. 289:2600-2609(2014).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26969129; DOI=10.1186/s13041-016-0206-6;
RA Sarowar T., Grabrucker S., Foehr K., Mangus K., Eckert M., Bockmann J.,
RA Boeckers T.M., Grabrucker A.M.;
RT "Enlarged dendritic spines and pronounced neophobia in mice lacking the PSD
RT protein RICH2.";
RL Mol. Brain 9:28-28(2016).
CC -!- FUNCTION: GTPase-activating protein (GAP) that stimulates the GTPase
CC activity of Rho-type GTPases. Thereby, controls Rho-type GTPases
CC cycling between their active GTP-bound and inactive GDP-bound states.
CC Acts as a GAP at least for CDC42 and RAC1 (PubMed:24352656,
CC PubMed:26969129). In neurons, is involved in dendritic spine formation
CC and synaptic plasticity in a specific RAC1-GAP activity
CC (PubMed:23739967, PubMed:24352656, PubMed:26969129). Limits the
CC initiation of exploratory dendritic filopodia. Recruited to actin-
CC patches that seed filopodia, binds specifically to plasma membrane
CC sections that are deformed inward by acto-myosin mediated contractile
CC forces. Acts through GAP activity on RAC1 to reduce actin
CC polymerization necessary for filopodia formation (By similarity). In
CC association with SHANK3, promotes GRIA1 exocytosis from recycling
CC endosomes and spine morphological changes associated to long-term
CC potentiation (PubMed:23739967). {ECO:0000250|UniProtKB:F1LQX4,
CC ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24352656,
CC ECO:0000269|PubMed:26969129}.
CC -!- SUBUNIT: Interacts with BST2 (via cytoplasmic domain).Interacts
CC (probably via PDZ-binding motif) with SHANK3 (via PDZ domain); the
CC interaction takes place in dendritic spines and promotes GRIA1
CC exocytosis. {ECO:0000269|PubMed:23739967}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24352656}. Recycling
CC endosome {ECO:0000269|PubMed:23739967}. Presynapse
CC {ECO:0000269|PubMed:23739967}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:F1LQX4}. Note=In CA1 hippocampal synapses,
CC detected at both presynaptic and postsynaptic sites (PubMed:23739967).
CC Located in convoluted dendritic plasma membrane sections enriched in
CC polymerized actin and myosin (patches) along dendrites where often
CC emerge filopodia (By similarity). {ECO:0000250|UniProtKB:F1LQX4,
CC ECO:0000269|PubMed:23739967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5SSM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSM3-2; Sequence=VSP_023740, VSP_023741;
CC Name=3;
CC IsoId=Q5SSM3-3; Sequence=VSP_023741;
CC Name=4;
CC IsoId=Q5SSM3-4; Sequence=VSP_023737, VSP_023738, VSP_023739;
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain (at protein level)
CC (PubMed:26969129). Detected in olfactory bulb, cortex, hippocampus,
CC diencephalon and cerebellum (at protein level) (PubMed:26969129).
CC Expressed in hippocampal neurons (at protein level).
CC {ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24352656,
CC ECO:0000269|PubMed:26969129}.
CC -!- DOMAIN: Rho-GAP domain is required to promote GRIA1 exocytosis from
CC recycling endosomes. Rho-GAP and BAR domains are necessary for the
CC control of long-term potentiation in hippocampal neurons
CC (PubMed:23739967). In dendrites, BAR domain mediates the recruitment to
CC patches where plasma membrane is deformed by acto-myosin mediated
CC contractile forces (By similarity). {ECO:0000250|UniProtKB:F1LQX4,
CC ECO:0000269|PubMed:23739967}.
CC -!- DISRUPTION PHENOTYPE: Mutants display a selective and highly
CC significant fear of novel objects and increased stereotypic behavior as
CC well as impairment of motor learning (PubMed:26969129). They show a
CC nicrease in multiple synapses in the hippocampus and cerebellum
CC (PubMed:26969129). {ECO:0000269|PubMed:26969129}.
CC -!- MISCELLANEOUS: [Isoform 2]: Contains a PDZ-binding motif at positions
CC 761-764. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Contains a PDZ-binding motif at positions
CC 767-770. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35316.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAI24614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 4]:
CC Sequence=BAC35316.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK053220; BAC35316.1; ALT_FRAME; mRNA.
DR EMBL; AL663045; CAI24613.2; -; Genomic_DNA.
DR EMBL; AL663045; CAI24614.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663045; CAI24616.1; -; Genomic_DNA.
DR EMBL; AL663045; CAI24617.1; -; Genomic_DNA.
DR EMBL; BC056366; AAH56366.1; -; mRNA.
DR EMBL; BC059911; AAH59911.1; -; mRNA.
DR CCDS; CCDS36180.1; -. [Q5SSM3-2]
DR RefSeq; NP_001092758.1; NM_001099288.1.
DR RefSeq; NP_778168.2; NM_175003.3. [Q5SSM3-2]
DR RefSeq; XP_006532934.1; XM_006532871.3.
DR RefSeq; XP_006532935.1; XM_006532872.3.
DR AlphaFoldDB; Q5SSM3; -.
DR SMR; Q5SSM3; -.
DR BioGRID; 229799; 8.
DR IntAct; Q5SSM3; 3.
DR MINT; Q5SSM3; -.
DR STRING; 10090.ENSMUSP00000039139; -.
DR GlyGen; Q5SSM3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5SSM3; -.
DR PhosphoSitePlus; Q5SSM3; -.
DR SwissPalm; Q5SSM3; -.
DR MaxQB; Q5SSM3; -.
DR PaxDb; 10090-ENSMUSP00000039139; -.
DR PeptideAtlas; Q5SSM3; -.
DR ProteomicsDB; 254970; -. [Q5SSM3-1]
DR ProteomicsDB; 254971; -. [Q5SSM3-2]
DR ProteomicsDB; 254972; -. [Q5SSM3-3]
DR ProteomicsDB; 254973; -. [Q5SSM3-4]
DR Antibodypedia; 47980; 118 antibodies from 21 providers.
DR DNASU; 216831; -.
DR Ensembl; ENSMUST00000047463.15; ENSMUSP00000039139.9; ENSMUSG00000033389.17. [Q5SSM3-2]
DR Ensembl; ENSMUST00000093001.5; ENSMUSP00000090680.5; ENSMUSG00000033389.17. [Q5SSM3-4]
DR Ensembl; ENSMUST00000093002.12; ENSMUSP00000090681.6; ENSMUSG00000033389.17. [Q5SSM3-1]
DR GeneID; 216831; -.
DR KEGG; mmu:216831; -.
DR UCSC; uc007jku.1; mouse. [Q5SSM3-2]
DR UCSC; uc007jkv.1; mouse. [Q5SSM3-1]
DR UCSC; uc007jkw.1; mouse. [Q5SSM3-4]
DR AGR; MGI:2144423; -.
DR CTD; 9912; -.
DR MGI; MGI:2144423; Arhgap44.
DR VEuPathDB; HostDB:ENSMUSG00000033389; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000157296; -.
DR HOGENOM; CLU_013806_0_0_1; -.
DR InParanoid; Q5SSM3; -.
DR OMA; SDWIQAS; -.
DR OrthoDB; 7959at2759; -.
DR PhylomeDB; Q5SSM3; -.
DR TreeFam; TF316514; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 216831; 5 hits in 78 CRISPR screens.
DR ChiTaRS; Arhgap44; mouse.
DR PRO; PR:Q5SSM3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSM3; Protein.
DR Bgee; ENSMUSG00000033389; Expressed in medial vestibular nucleus and 214 other cell types or tissues.
DR ExpressionAtlas; Q5SSM3; baseline and differential.
DR Genevisible; Q5SSM3; MM.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:SynGO-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0031256; C:leading edge membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SynGO-UCL.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:SynGO-UCL.
DR GO; GO:0098886; P:modification of dendritic spine; IMP:SynGO.
DR GO; GO:0099010; P:modification of postsynaptic structure; IDA:SynGO.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IMP:SynGO.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IMP:SynGO.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:SynGO.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:SynGO-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:SynGO-UCL.
DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07619; BAR_Rich2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR PANTHER; PTHR14130:SF13; RHO GTPASE-ACTIVATING PROTEIN 44; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Endosome; GTPase activation;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..814
FT /note="Rho GTPase-activating protein 44"
FT /id="PRO_0000280481"
FT DOMAIN 14..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 255..445
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 467..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..814
FT /note="Interaction with BST2"
FT /evidence="ECO:0000250"
FT REGION 784..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 811..814
FT /note="PDZ-binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 541..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1LQX4"
FT VAR_SEQ 1..18
FT /note="MKKQFNRMRQLANQTVGR -> MELPGLELVRPSWVRAGRW (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023737"
FT VAR_SEQ 195..210
FT /note="DQLSADMYSFVAKEID -> VPVPLALLSRDRLRSP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023738"
FT VAR_SEQ 211..814
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023739"
FT VAR_SEQ 509..514
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023740"
FT VAR_SEQ 769..814
FT /note="DLVHFDVPSIHIELGSTLRLSPLEHARRHSATDKRDSEEESESTAL -> AV
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023741"
FT MUTAGEN 291
FT /note="R->A: Reduces GRIA1 recycling. Abolishes the
FT increase of spine density and size, as well as reduces the
FT increase of GRIA1 expression in surface associated with
FT long-term potentiation."
FT /evidence="ECO:0000269|PubMed:23739967"
SQ SEQUENCE 814 AA; 88994 MW; 466419A6D9471DDF CRC64;
MKKQFNRMRQ LANQTVGRAE KTEVLSEDLL QVEKRLELVK QVSHSTHKKL TACLQGQQGA
EADKRSKKLP LTTLAQCLVE GSAILGDDTL LGKMLKLCGE TEDKLAQELI HFELQVERDV
IEPLFLLAEV EIPNIQKQRK HLAKLVLDMD SSRTRWQQTS KSSGLSSSLQ PAGAKADALR
EEMEEAANRV EICRDQLSAD MYSFVAKEID YANYFQTLIE VQAEYHRKSL TLLQAVLPQI
KAQQEAWVEK PSFGKPLEEH LMISGREIAF PIEACVTMLL ECGMQEEGLF RVAPSASKLK
KLKAALDCCV VDVQEYSADP HAIAGALKSY LRELPEPLMT FELYDEWIQA SNIQEQDKRL
QALWNACEKL PKANHNNIKY LIKFLSKLSE YQDVNKMTPS NMAIVLGPNL LWPQSEGNIT
EMMTTVSLQI VGIIEPIIQH ADWFFPGEIE FNLTGSYGSP VHVNHNANYS SMPSPDMDPA
DRRQPEQARR PLSVATDNMM LEFYKKDGLR KIQSMGVRVM DTSWVARRGS SAGRKASCAP
PSMQPPAPPS ELAAPLPSPL PEQVPDSPAT PAPALSPSGA SLQPTPERPS VSKSKELSPG
SGQKGSPGSI QGTPCPGTQL GPQPAASPSQ LPADQSPHTL RKVSKKVAPI PPKVPFVQPG
TVSDQPVGQP SPVSLSPTPP STPSPYGLSY PPGYSMASGQ LSPASAPPLA SPSVFTSTLA
KSRPTPKPRQ RPTLPPPQPP SVSLSASSPQ STEHPMLDGM SPGESMSTDL VHFDVPSIHI
ELGSTLRLSP LEHARRHSAT DKRDSEEESE STAL
//
