HOME1_RAT
ID HOME1_RAT Reviewed; 366 AA.
AC Q9Z214; O08567; O88800; Q9QUJ8; Q9QWN5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Homer protein homolog 1 {ECO:0000305};
DE AltName: Full=PSD-Zip45 {ECO:0000303|PubMed:9824313};
DE AltName: Full=VASP/Ena-related gene up-regulated during seizure and LTP 1;
DE Short=Vesl-1 {ECO:0000250|UniProtKB:Q9Z2Y3};
GN Name=Homer1 {ECO:0000312|RGD:628725}; Synonyms=Homer, Vesl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH GRM1 AND GRM5.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=9069287; DOI=10.1038/386284a0;
RA Brakeman P.R., Lanahan A.A., O'Brien R., Roche K., Barnes C.A.,
RA Huganir R.L., Worley P.F.;
RT "Homer: a protein that selectively binds metabotropic glutamate
RT receptors.";
RL Nature 386:284-288(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=9257717; DOI=10.1016/s0014-5793(97)00775-8;
RA Kato A., Ozawa F., Saitoh Y., Hirai K., Inokuchi K.;
RT "Vesl, a gene encoding VASP/Ena family related protein, is upregulated
RT during seizure, long-term potentiation and synaptogenesis.";
RL FEBS Lett. 412:183-189(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), CHARACTERIZATION, AND
RP INTERACTION WITH GRM1 AND GRM5.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=9808458; DOI=10.1016/s0896-6273(00)80588-7;
RA Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
RA Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
RT "Homer regulates the association of group 1 metabotropic glutamate
RT receptors with multivalent complexes of homer-related, synaptic proteins.";
RL Neuron 21:707-716(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9824313; DOI=10.1016/s0014-5793(98)01256-3;
RA Sun J., Tadokoro S., Imanaka T., Murakami S.D., Nakamura M., Kashiwada K.,
RA Ko J., Nishida W., Sobue K.;
RT "Isolation of PSD-Zip45, a novel Homer/vesl family protein containing
RT leucine zipper motifs, from rat brain.";
RL FEBS Lett. 437:304-308(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH GRM1 AND GRM5.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=9727012; DOI=10.1074/jbc.273.37.23969;
RA Kato A., Ozawa F., Saitoh Y., Fukazawa Y., Sugiyama H., Inokuchi K.;
RT "Novel members of the Vesl/Homer family of PDZ-proteins that bind
RT metabotropic glutamate receptors.";
RL J. Biol. Chem. 273:23969-23975(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Fast-twitch skeletal muscle;
RX PubMed=11118290; DOI=10.1006/bbrc.2000.3948;
RA Sandona D., Tibaldo E., Volpe P.;
RT "Evidence for the presence of two homer 1 transcripts in skeletal and
RT cardiac muscles.";
RL Biochem. Biophys. Res. Commun. 279:348-353(2000).
RN [7]
RP INTERACTION WITH GRM1; GRM5; DYN3 AND ITPR1.
RX PubMed=9808459; DOI=10.1016/s0896-6273(00)80589-9;
RA Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M., Linden D.J.,
RA Worley P.F.;
RT "Homer binds a novel proline-rich motif and links group 1 metabotropic
RT glutamate receptors with IP3 receptors.";
RL Neuron 21:717-726(1998).
RN [8]
RP INTERACTION WITH SHANK1 AND SHANK3, AND SUBCELLULAR LOCATION.
RX PubMed=10433269; DOI=10.1016/s0896-6273(00)80810-7;
RA Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P.,
RA Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.;
RT "Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
RT postsynaptic density proteins.";
RL Neuron 23:583-592(1999).
RN [9]
RP INTERACTION WITH RYR2.
RX PubMed=12887973; DOI=10.1016/s0143-4160(03)00112-x;
RA Westhoff J.H., Hwang S.-Y., Scott Duncan R., Ozawa F., Volpe P.,
RA Inokuchi K., Koulen P.;
RT "Vesl/Homer proteins regulate ryanodine receptor type 2 function and
RT intracellular calcium signaling.";
RL Cell Calcium 34:261-269(2003).
RN [10]
RP INTERACTION WITH RYR1.
RX PubMed=12810060; DOI=10.1016/s0143-4160(03)00082-4;
RA Hwang S.-Y., Wei J., Westhoff J.H., Duncan R.S., Ozawa F., Volpe P.,
RA Inokuchi K., Koulen P.;
RT "Differential functional interaction of two Vesl/Homer protein isoforms
RT with ryanodine receptor type 1: a novel mechanism for control of
RT intracellular calcium signaling.";
RL Cell Calcium 34:177-184(2003).
RN [11]
RP REVIEW.
RX PubMed=10851183; DOI=10.1016/s0959-4388(00)00087-8;
RA Xiao B., Tu J.C., Worley P.F.;
RT "Homer: a link between neural activity and glutamate receptor function.";
RL Curr. Opin. Neurobiol. 10:370-374(2000).
RN [12]
RP INTERACTION WITH AGAP2, AND FUNCTION.
RX PubMed=14528310; DOI=10.1038/nn1134;
RA Rong R., Ahn J.-Y., Huang H., Nagata E., Kalman D., Kapp J.A., Tu J.,
RA Worley P.F., Snyder S.H., Ye K.;
RT "PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing
RT neuronal apoptosis.";
RL Nat. Neurosci. 6:1153-1161(2003).
RN [13]
RP INTERACTION WITH OPHN1.
RX PubMed=15034583; DOI=10.1038/nn1210;
RA Govek E.E., Newey S.E., Akerman C.J., Cross J.R., Van der Veken L.,
RA Van Aelst L.;
RT "The X-linked mental retardation protein oligophrenin-1 is required for
RT dendritic spine morphogenesis.";
RL Nat. Neurosci. 7:364-372(2004).
RN [14]
RP INTERACTION WITH DAGLA.
RX PubMed=17584991; DOI=10.1124/mol.107.037796;
RA Jung K.M., Astarita G., Zhu C., Wallace M., Mackie K., Piomelli D.;
RT "A key role for diacylglycerol lipase-alpha in metabotropic glutamate
RT receptor-dependent endocannabinoid mobilization.";
RL Mol. Pharmacol. 72:612-621(2007).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, AND
RP MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
RX PubMed=10798399; DOI=10.1016/s0896-6273(00)81145-9;
RA Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F.,
RA Leahy D.J.;
RT "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in
RT polyproline recognition.";
RL Neuron 26:143-154(2000).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-163.
RX PubMed=12054806; DOI=10.1016/s0022-2836(02)00170-5;
RA Irie K., Nakatsu T., Mitsuoka K., Miyazawa A., Sobue K., Hiroaki Y.,
RA Doi T., Fujiyoshi Y., Kato H.;
RT "Crystal structure of the Homer 1 family conserved region reveals the
RT interaction between the EVH1 domain and own proline-rich motif.";
RL J. Mol. Biol. 318:1117-1126(2002).
RN [18] {ECO:0007744|PDB:3CVE}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 302-366 OF TETRAMER OF MUTANT
RP MET-320, INTERACTION WITH SHANK1, MUTAGENESIS OF TRP-24; ILE-344 AND
RP ILE-349, FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=19345194; DOI=10.1016/j.cell.2009.01.050;
RA Hayashi M.K., Tang C., Verpelli C., Narayanan R., Stearns M.H., Xu R.M.,
RA Li H., Sala C., Hayashi Y.;
RT "The postsynaptic density proteins Homer and Shank form a polymeric network
RT structure.";
RL Cell 137:159-171(2009).
CC -!- FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-
CC links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2,
CC SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-
CC associated ITPR1 receptors, it aids the coupling of surface receptors
CC to intracellular calcium release. May also couple GRM1 to PI3 kinase
CC through its interaction with AGAP2. Differentially regulates the
CC functions of the calcium activated channel ryanodine receptors RYR1 and
CC RYR2. Isoform 1 decreases the activity of RYR2, and increases the
CC activity of RYR1, whereas isoform 3 counteracts the effects by
CC competing for binding sites. Isoform 1 regulates the trafficking and
CC surface expression of GRM5. Isoform 3 acts as a natural dominant
CC negative, in dynamic competition with constitutively expressed isoform
CC 1, and isoform 2 to regulate synaptic metabotropic glutamate function.
CC Isoform 3, may be involved in the structural changes that occur at
CC synapses during long-lasting neuronal plasticity and development. Forms
CC a high-order complex with SHANK1, which in turn is necessary for the
CC structural and functional integrity of dendritic spines
CC (PubMed:19345194). Negatively regulates T cell activation by inhibiting
CC the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA
CC for NFAT protein binding, hence preventing NFAT activation by PPP3CA
CC (By similarity). {ECO:0000250|UniProtKB:Q86YM7,
CC ECO:0000269|PubMed:14528310, ECO:0000269|PubMed:19345194}.
CC -!- SUBUNIT: Tetramer; this tetrameric structure is critical for forming
CC the high-order complex with SHANK1, which in turn is necessary for the
CC structural and functional integrity of dendritic spines
CC (PubMed:19345194). Interacts with GRM1, GRM5, ITPR1, DYN3, RYR1, RYR2
CC and SHANK3 (PubMed:10433269, PubMed:10798399, PubMed:12810060,
CC PubMed:12887973, PubMed:9069287, PubMed:9808458, PubMed:9808459,
CC PubMed:9727012). Interacts with IFT57 and OPHN1 (PubMed:15034583).
CC Isoform 1 and isoform 2 encode coiled-coil structures that mediate
CC homo- and heteromultimerization. Interacts with SHANK1; forms high-
CC order polymerized complex with a mesh-like network structure, at least
CC composed of SHANK1, HOMER1 and DLGAP1; the complex formation is SHANK1
CC multimerization dependent (PubMed:10433269, PubMed:19345194). Interacts
CC with NFATC4 (By similarity). Interacts with DAGLA (via PPXXF motif);
CC this interaction is required for the cell membrane localization of
CC DAGLA (PubMed:17584991). Interacts with SRGAP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q86YM7, ECO:0000250|UniProtKB:Q9Z2Y3,
CC ECO:0000269|PubMed:10433269, ECO:0000269|PubMed:10798399,
CC ECO:0000269|PubMed:12810060, ECO:0000269|PubMed:12887973,
CC ECO:0000269|PubMed:14528310, ECO:0000269|PubMed:15034583,
CC ECO:0000269|PubMed:17584991, ECO:0000269|PubMed:19345194,
CC ECO:0000269|PubMed:9069287, ECO:0000269|PubMed:9727012,
CC ECO:0000269|PubMed:9808458, ECO:0000269|PubMed:9808459}.
CC -!- INTERACTION:
CC Q9Z214; Q3UVX5: Grm5; Xeno; NbExp=2; IntAct=EBI-2338940, EBI-8795045;
CC Q9Z214-1; Q8CGU4: Agap2; NbExp=4; IntAct=EBI-4410552, EBI-4409108;
CC Q9Z214-1; Q14CM0: FRMPD4; Xeno; NbExp=2; IntAct=EBI-4410552, EBI-311279;
CC Q9Z214-1; Q3UVX5: Grm5; Xeno; NbExp=3; IntAct=EBI-4410552, EBI-8795045;
CC Q9Z214-2; Q9Z214-2: Homer1; NbExp=4; IntAct=EBI-2338999, EBI-2338999;
CC Q9Z214-2; Q9WV48: Shank1; NbExp=4; IntAct=EBI-2338999, EBI-80909;
CC Q9Z214-3; Q3UVX5: Grm5; Xeno; NbExp=2; IntAct=EBI-2339003, EBI-8795045;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Synapse {ECO:0000269|PubMed:10433269}. Cell projection,
CC dendritic spine {ECO:0000269|PubMed:19345194,
CC ECO:0000269|PubMed:30021165}. Note=Isoform 1 inhibits surface
CC expression of GRM5 causing it to be retained in the endoplasmic
CC reticulum. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=1c, Vesl-1L;
CC IsoId=Q9Z214-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=Q9Z214-2; Sequence=VSP_009066;
CC Name=3; Synonyms=1a, Vesl;
CC IsoId=Q9Z214-3; Sequence=VSP_009067, VSP_009068;
CC -!- TISSUE SPECIFICITY: Highly expressed in cortex, Purkinje cells of the
CC cerebellum, hippocampus, striatum and olfactory bulb. Isoform 1 and
CC isoform 3 are expressed in skeletal and cardiac muscle.
CC {ECO:0000269|PubMed:11118290}.
CC -!- DEVELOPMENTAL STAGE: In the developing hippocampus, the expression of
CC isoform 1 is high at P8, then decreased with progression of hippocampal
CC development. Isoform 3 expression was constitutively low, and not
CC regulated during hippocampal development.
CC -!- INDUCTION: [Isoform 3]: Induced in the hippocampus, by seizure and
CC synaptic mechanisms in association with long-term potentiation (LTP).
CC It is also induced in the striatum by drugs that alter dopamine
CC signaling.
CC -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5,
CC RYR1, RYR2, ITPR1, SHANK 1 and SHANK3. The coiled-Coil domain forms an
CC antiparallel tetrameric arrangement (PubMed:19345194).
CC {ECO:0000269|PubMed:19345194}.
CC -!- SIMILARITY: Belongs to the Homer family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U92079; AAC53113.1; ALT_INIT; mRNA.
DR EMBL; AB003726; BAA21671.1; -; mRNA.
DR EMBL; AF093267; AAC71031.1; -; mRNA.
DR EMBL; AF093268; AAC71032.1; -; mRNA.
DR EMBL; AB017140; BAA34311.1; -; mRNA.
DR EMBL; AB007688; BAA32477.1; -; mRNA.
DR EMBL; AJ276327; CAB77249.1; -; mRNA.
DR EMBL; AJ276328; CAB77250.1; -; mRNA.
DR RefSeq; NP_113895.1; NM_031707.1. [Q9Z214-1]
DR RefSeq; XP_006231837.1; XM_006231775.3. [Q9Z214-2]
DR PDB; 1DDV; X-ray; 1.90 A; A=1-111.
DR PDB; 1DDW; X-ray; 1.70 A; A=1-120.
DR PDB; 1I2H; X-ray; 1.80 A; A=1-163.
DR PDB; 3CVE; X-ray; 1.75 A; A/B/C/D=302-366.
DR PDBsum; 1DDV; -.
DR PDBsum; 1DDW; -.
DR PDBsum; 1I2H; -.
DR PDBsum; 3CVE; -.
DR AlphaFoldDB; Q9Z214; -.
DR BMRB; Q9Z214; -.
DR SMR; Q9Z214; -.
DR BioGRID; 248180; 16.
DR ELM; Q9Z214; -.
DR IntAct; Q9Z214; 11.
DR MINT; Q9Z214; -.
DR STRING; 10116.ENSRNOP00000065989; -.
DR iPTMnet; Q9Z214; -.
DR PhosphoSitePlus; Q9Z214; -.
DR SwissPalm; Q9Z214; -.
DR PaxDb; Q9Z214; -.
DR PRIDE; Q9Z214; -.
DR ABCD; Q9Z214; 4 sequenced antibodies.
DR Ensembl; ENSRNOT00000071804; ENSRNOP00000065989; ENSRNOG00000047014. [Q9Z214-1]
DR GeneID; 29546; -.
DR KEGG; rno:29546; -.
DR CTD; 9456; -.
DR RGD; 628725; Homer1.
DR eggNOG; ENOG502QR3K; Eukaryota.
DR GeneTree; ENSGT00940000156354; -.
DR HOGENOM; CLU_033940_0_0_1; -.
DR InParanoid; Q9Z214; -.
DR OrthoDB; 1251658at2759; -.
DR PhylomeDB; Q9Z214; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR EvolutionaryTrace; Q9Z214; -.
DR PRO; PR:Q9Z214; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000047014; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; Q9Z214; baseline and differential.
DR Genevisible; Q9Z214; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0044309; C:neuron spine; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0099186; F:structural constituent of postsynapse; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR GO; GO:0048875; P:chemical homeostasis within a tissue; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0035418; P:protein localization to synapse; IDA:BHF-UCL.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0090279; P:regulation of calcium ion import; ISO:RGD.
DR GO; GO:2001257; P:regulation of cation channel activity; ISO:RGD.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IMP:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:RGD.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISO:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:RGD.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR CDD; cd01206; EVH1_Homer_Vesl; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045027; Homer.
DR InterPro; IPR044100; Homer_EVH1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR10918; PTHR10918; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86YM7"
FT CHAIN 2..366
FT /note="Homer protein homolog 1"
FT /id="PRO_0000191007"
FT DOMAIN 1..110
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 114..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..366
FT /note="Required for tetramerization"
FT /evidence="ECO:0000269|PubMed:19345194"
FT COILED 193..364
FT /evidence="ECO:0000255"
FT COMPBIAS 122..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q86YM7"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Y3"
FT VAR_SEQ 176..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9808458"
FT /id="VSP_009066"
FT VAR_SEQ 176..186
FT /note="SAGDRTQGLSH -> RYTFNSAIMIK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11118290,
FT ECO:0000303|PubMed:9069287, ECO:0000303|PubMed:9257717,
FT ECO:0000303|PubMed:9808458, ECO:0000303|PubMed:9824313"
FT /id="VSP_009067"
FT VAR_SEQ 187..366
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11118290,
FT ECO:0000303|PubMed:9069287, ECO:0000303|PubMed:9257717,
FT ECO:0000303|PubMed:9808458, ECO:0000303|PubMed:9824313"
FT /id="VSP_009068"
FT MUTAGEN 24
FT /note="W->A: Disrupts binding to both GRM1 and SHANK3. Does
FT not form the high-order complex with SHANK1."
FT /evidence="ECO:0000269|PubMed:10798399,
FT ECO:0000269|PubMed:19345194"
FT MUTAGEN 24
FT /note="W->Y: Disrupts binding to GRM1."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 70
FT /note="T->A: Normal binding."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 70
FT /note="T->E: Disrupts binding to SHANK3."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 74
FT /note="F->A: Eliminates binding to both GRM1 and SHANK3."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 76
FT /note="Q->A: Normal binding."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 76
FT /note="Q->R: Normal binding."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 85
FT /note="V->A: Diminishes binding to GRM1."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 89
FT /note="G->A: Eliminates binding to both GRM1 and SHANK3."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 89
FT /note="G->N: Eliminates binding to both GRM1 and SHANK3."
FT /evidence="ECO:0000269|PubMed:10798399"
FT MUTAGEN 344
FT /note="I->R: Dimeric form; when associated with E-349. Does
FT not form the high-order complex with SHANK1; when
FT associated with E-349. Does not change its interaction with
FT STX12; when associated with E-349. Reduces localization to
FT the spine; when associated with E-349. Affects dendritic
FT spine structure; when associated with E-349. Decreases
FT synaptic transmission; when associated with E-349. Does not
FT affect glutamate receptors ratio; when associated with E-
FT 349."
FT /evidence="ECO:0000269|PubMed:19345194"
FT MUTAGEN 349
FT /note="I->E: Dimeric form; when associated with R-344. Does
FT not form the high-order complex with SHANK1; when
FT associated with R-344. Does not change its interaction with
FT STX12; when associated with R-344. Reduces localization to
FT the spine; when associated with R-344. Affects dendritic
FT spine structure; when associated with R-344. Decreases
FT synaptic transmission; when associated with R-344. Does not
FT affect glutamate receptors ratio; when associated with R-
FT 344."
FT /evidence="ECO:0000269|PubMed:19345194"
FT CONFLICT 268
FT /note="L -> R (in Ref. 5; BAA32477)"
FT /evidence="ECO:0000305"
FT STRAND 3..16
FT /evidence="ECO:0007829|PDB:1DDW"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1DDW"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1DDW"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1DDW"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1DDW"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1DDW"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1DDW"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:1DDW"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:1DDW"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1DDW"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:1DDW"
FT HELIX 302..362
FT /evidence="ECO:0007829|PDB:3CVE"
SQ SEQUENCE 366 AA; 41305 MW; A6A21CB14207A384 CRC64;
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL DGSKAIINST
ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA EKFQEFKEAA RLAKEKSQEK
MELTSTPSQE SAGGDLQSPL TPESINGTDD ERTPDVTQNS EPRAEPAQNA LPFSHSAGDR
TQGLSHASSA ISKHWEAELA TLKGNNAKLT AALLESTANV KQWKQQLAAY QEEAERLHKR
VTELECVSSQ ANAVHSHKTE LSQTVQELEE TLKVKEEEIE RLKQEIDNAR ELQEQRDSLT
QKLQEVEIRN KDLEGQLSEL EQRLEKSQSE QDAFRSNLKT LLEILDGKIF ELTELRDNLA
KLLECS
