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Homer protein homolog 1 (PSD-Zip45) (VASP/Ena-related gene up-regulated during seizure and LTP 1) (Vesl-1)

 HOME1_RAT               Reviewed;         366 AA.
Q9Z214; O08567; O88800; Q9QUJ8; Q9QWN5;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
28-NOV-2003, sequence version 2.
22-NOV-2017, entry version 141.
RecName: Full=Homer protein homolog 1;
AltName: Full=PSD-Zip45;
AltName: Full=VASP/Ena-related gene up-regulated during seizure and LTP 1;
Short=Vesl-1;
Name=Homer1; Synonyms=Homer, Vesl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH GRM1 AND
GRM5.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=9069287; DOI=10.1038/386284a0;
Brakeman P.R., Lanahan A.A., O'Brien R., Roche K., Barnes C.A.,
Huganir R.L., Worley P.F.;
"Homer: a protein that selectively binds metabotropic glutamate
receptors.";
Nature 386:284-288(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
STRAIN=Wistar; TISSUE=Hippocampus;
PubMed=9257717; DOI=10.1016/S0014-5793(97)00775-8;
Kato A., Ozawa F., Saitoh Y., Hirai K., Inokuchi K.;
"Vesl, a gene encoding VASP/Ena family related protein, is upregulated
during seizure, long-term potentiation and synaptogenesis.";
FEBS Lett. 412:183-189(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), CHARACTERIZATION, AND
INTERACTION WITH GRM1 AND GRM5.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=9808458; DOI=10.1016/S0896-6273(00)80588-7;
Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
"Homer regulates the association of group 1 metabotropic glutamate
receptors with multivalent complexes of homer-related, synaptic
proteins.";
Neuron 21:707-716(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=9824313; DOI=10.1016/S0014-5793(98)01256-3;
Sun J., Tadokoro S., Imanaka T., Murakami S.D., Nakamura M.,
Kashiwada K., Ko J., Nishida W., Sobue K.;
"Isolation of PSD-Zip45, a novel Homer/vesl family protein containing
leucine zipper motifs, from rat brain.";
FEBS Lett. 437:304-308(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH GRM1 AND
GRM5.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=9727012; DOI=10.1074/jbc.273.37.23969;
Kato A., Ozawa F., Saitoh Y., Fukazawa Y., Sugiyama H., Inokuchi K.;
"Novel members of the Vesl/Homer family of PDZ-proteins that bind
metabotropic glutamate receptors.";
J. Biol. Chem. 273:23969-23975(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
TISSUE=Fast-twitch skeletal muscle;
PubMed=11118290; DOI=10.1006/bbrc.2000.3948;
Sandona D., Tibaldo E., Volpe P.;
"Evidence for the presence of two homer 1 transcripts in skeletal and
cardiac muscles.";
Biochem. Biophys. Res. Commun. 279:348-353(2000).
[7]
INTERACTION WITH GRM1; GRM5; DYN3 AND ITPR1.
PubMed=9808459; DOI=10.1016/S0896-6273(00)80589-9;
Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M.,
Linden D.J., Worley P.F.;
"Homer binds a novel proline-rich motif and links group 1 metabotropic
glutamate receptors with IP3 receptors.";
Neuron 21:717-726(1998).
[8]
INTERACTION WITH SHANK1 AND SHANK3, AND SUBCELLULAR LOCATION.
PubMed=10433269; DOI=10.1016/S0896-6273(00)80810-7;
Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P.,
Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.;
"Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
postsynaptic density proteins.";
Neuron 23:583-592(1999).
[9]
INTERACTION WITH RYR2.
PubMed=12887973; DOI=10.1016/S0143-4160(03)00112-X;
Westhoff J.H., Hwang S.-Y., Scott Duncan R., Ozawa F., Volpe P.,
Inokuchi K., Koulen P.;
"Vesl/Homer proteins regulate ryanodine receptor type 2 function and
intracellular calcium signaling.";
Cell Calcium 34:261-269(2003).
[10]
INTERACTION WITH RYR1.
PubMed=12810060; DOI=10.1016/S0143-4160(03)00082-4;
Hwang S.-Y., Wei J., Westhoff J.H., Duncan R.S., Ozawa F., Volpe P.,
Inokuchi K., Koulen P.;
"Differential functional interaction of two Vesl/Homer protein
isoforms with ryanodine receptor type 1: a novel mechanism for control
of intracellular calcium signaling.";
Cell Calcium 34:177-184(2003).
[11]
REVIEW.
PubMed=10851183; DOI=10.1016/S0959-4388(00)00087-8;
Xiao B., Tu J.C., Worley P.F.;
"Homer: a link between neural activity and glutamate receptor
function.";
Curr. Opin. Neurobiol. 10:370-374(2000).
[12]
INTERACTION WITH AGAP2, AND FUNCTION.
PubMed=14528310; DOI=10.1038/nn1134;
Rong R., Ahn J.-Y., Huang H., Nagata E., Kalman D., Kapp J.A., Tu J.,
Worley P.F., Snyder S.H., Ye K.;
"PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase,
preventing neuronal apoptosis.";
Nat. Neurosci. 6:1153-1161(2003).
[13]
INTERACTION WITH OPHN1.
PubMed=15034583; DOI=10.1038/nn1210;
Govek E.E., Newey S.E., Akerman C.J., Cross J.R., Van der Veken L.,
Van Aelst L.;
"The X-linked mental retardation protein oligophrenin-1 is required
for dendritic spine morphogenesis.";
Nat. Neurosci. 7:364-372(2004).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5,
AND MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
PubMed=10798399; DOI=10.1016/S0896-6273(00)81145-9;
Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F.,
Leahy D.J.;
"Structure of the Homer EVH1 domain-peptide complex reveals a new
twist in polyproline recognition.";
Neuron 26:143-154(2000).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-163.
PubMed=12054806; DOI=10.1016/S0022-2836(02)00170-5;
Irie K., Nakatsu T., Mitsuoka K., Miyazawa A., Sobue K., Hiroaki Y.,
Doi T., Fujiyoshi Y., Kato H.;
"Crystal structure of the Homer 1 family conserved region reveals the
interaction between the EVH1 domain and own proline-rich motif.";
J. Mol. Biol. 318:1117-1126(2002).
-!- FUNCTION: Postsynaptic density scaffolding protein. Binds and
cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1,
RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with
ER-associated ITPR1 receptors, it aids the coupling of surface
receptors to intracellular calcium release. May also couple GRM1
to PI3 kinase through its interaction with AGAP2. Differentially
regulates the functions of the calcium activated channel ryanodine
receptors RYR1 and RYR2. Isoform 1 decreases the activity of RYR2,
and increases the activity of RYR1, whereas isoform 3 counteracts
the effects by competing for binding sites. Isoform 1 regulates
the trafficking and surface expression of GRM5. Isoform 3 acts as
a natural dominant negative, in dynamic competition with
constitutively expressed isoform 1, and isoform 2 to regulate
synaptic metabotropic glutamate function. Isoform 3, may be
involved in the structural changes that occur at synapses during
long-lasting neuronal plasticity and development.
{ECO:0000269|PubMed:14528310}.
-!- SUBUNIT: Interacts with GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2,
SHANK1 and SHANK3. Interacts with IFT57 and OPHN1. Isoform 1 and
isoform 2 encode coiled-coil structures that mediate homo- and
heteromultimerization. {ECO:0000269|PubMed:10433269,
ECO:0000269|PubMed:10798399, ECO:0000269|PubMed:12810060,
ECO:0000269|PubMed:12887973, ECO:0000269|PubMed:14528310,
ECO:0000269|PubMed:15034583, ECO:0000269|PubMed:9069287,
ECO:0000269|PubMed:9727012, ECO:0000269|PubMed:9808458,
ECO:0000269|PubMed:9808459}.
-!- INTERACTION:
Q8CGU4:Agap2; NbExp=4; IntAct=EBI-4410552, EBI-4409108;
Q3UVX5:Grm5 (xeno); NbExp=3; IntAct=EBI-4410552, EBI-8795045;
Q9WV48:Shank1; NbExp=4; IntAct=EBI-2338999, EBI-80909;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction,
synapse, postsynaptic cell membrane, postsynaptic density
{ECO:0000250}. Cell junction, synapse
{ECO:0000269|PubMed:10433269}. Note=Isoform 1 inhibits surface
expression of GRM5 causing it to be retained in the endoplasmic
reticulum. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=1c, Vesl-1L;
IsoId=Q9Z214-1; Sequence=Displayed;
Name=2; Synonyms=1b;
IsoId=Q9Z214-2; Sequence=VSP_009066;
Name=3; Synonyms=1a, Vesl;
IsoId=Q9Z214-3; Sequence=VSP_009067, VSP_009068;
-!- TISSUE SPECIFICITY: Highly expressed in cortex, Purkinje cells of
the cerebellum, hippocampus, striatum and olfactory bulb. Isoform
1 and isoform 3 are expressed in skeletal and cardiac muscle.
{ECO:0000269|PubMed:11118290}.
-!- DEVELOPMENTAL STAGE: In the developing hippocampus, the expression
of isoform 1 is high at P8, then decreased with progression of
hippocampal development. Isoform 3 expression was constitutively
low, and not regulated during hippocampal development.
-!- INDUCTION: Isoform 3 is induced in the hippocampus, by seizure and
synaptic mechanisms in association with long-term potentiation
(LTP). It is also induced in the striatum by drugs that alter
dopamine signaling.
-!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1,
GRM5, RYR1, RYR2, ITPR1, SHANK 1 and SHANK3.
-!- SIMILARITY: Belongs to the Homer family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC53113.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U92079; AAC53113.1; ALT_INIT; mRNA.
EMBL; AB003726; BAA21671.1; -; mRNA.
EMBL; AF093267; AAC71031.1; -; mRNA.
EMBL; AF093268; AAC71032.1; -; mRNA.
EMBL; AB017140; BAA34311.1; -; mRNA.
EMBL; AB007688; BAA32477.1; -; mRNA.
EMBL; AJ276327; CAB77249.1; -; mRNA.
EMBL; AJ276328; CAB77250.1; -; mRNA.
RefSeq; NP_113895.1; NM_031707.1. [Q9Z214-1]
RefSeq; XP_006231837.1; XM_006231775.3. [Q9Z214-2]
UniGene; Rn.37500; -.
PDB; 1DDV; X-ray; 1.90 A; A=1-111.
PDB; 1DDW; X-ray; 1.70 A; A=1-120.
PDB; 1I2H; X-ray; 1.80 A; A=1-163.
PDB; 3CVE; X-ray; 1.75 A; A/B/C/D=302-366.
PDBsum; 1DDV; -.
PDBsum; 1DDW; -.
PDBsum; 1I2H; -.
PDBsum; 3CVE; -.
ProteinModelPortal; Q9Z214; -.
SMR; Q9Z214; -.
BioGrid; 248180; 11.
ELM; Q9Z214; -.
IntAct; Q9Z214; 9.
MINT; MINT-1891037; -.
STRING; 10116.ENSRNOP00000065989; -.
iPTMnet; Q9Z214; -.
PhosphoSitePlus; Q9Z214; -.
PaxDb; Q9Z214; -.
PRIDE; Q9Z214; -.
Ensembl; ENSRNOT00000073871; ENSRNOP00000066634; ENSRNOG00000047014. [Q9Z214-2]
GeneID; 29546; -.
KEGG; rno:29546; -.
CTD; 9456; -.
RGD; 628725; Homer1.
eggNOG; ENOG410IGRQ; Eukaryota.
eggNOG; ENOG410XQWT; LUCA.
GeneTree; ENSGT00390000017850; -.
HOVERGEN; HBG051918; -.
InParanoid; Q9Z214; -.
KO; K15010; -.
OrthoDB; EOG091G0CQ0; -.
PhylomeDB; Q9Z214; -.
Reactome; R-RNO-6794361; Neurexins and neuroligins.
EvolutionaryTrace; Q9Z214; -.
PRO; PR:Q9Z214; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000047014; -.
ExpressionAtlas; Q9Z214; baseline and differential.
Genevisible; Q9Z214; RN.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0030424; C:axon; ISO:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0043034; C:costamere; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0098794; C:postsynapse; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0030018; C:Z disc; ISO:RGD.
GO; GO:0035256; F:G-protein coupled glutamate receptor binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; ISO:RGD.
GO; GO:0032947; F:protein complex scaffold activity; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0005102; F:receptor binding; IDA:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:RGD.
GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
GO; GO:0048875; P:chemical homeostasis within a tissue; ISO:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0007216; P:G-protein coupled glutamate receptor signaling pathway; IDA:RGD.
GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:RGD.
GO; GO:0035418; P:protein localization to synapse; IDA:BHF-UCL.
GO; GO:0090279; P:regulation of calcium ion import; ISO:RGD.
GO; GO:2001257; P:regulation of cation channel activity; ISO:RGD.
GO; GO:2001256; P:regulation of store-operated calcium entry; ISO:RGD.
GO; GO:0051592; P:response to calcium ion; ISO:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0003009; P:skeletal muscle contraction; ISO:RGD.
GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000697; WH1/EVH1_dom.
Pfam; PF00568; WH1; 1.
SMART; SM00461; WH1; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50229; WH1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Membrane;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Synapse.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q86YM7}.
CHAIN 2 366 Homer protein homolog 1.
/FTId=PRO_0000191007.
DOMAIN 1 110 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
COILED 193 364 {ECO:0000255}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:Q86YM7}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2Y3}.
VAR_SEQ 176 187 Missing (in isoform 2).
{ECO:0000303|PubMed:9808458}.
/FTId=VSP_009066.
VAR_SEQ 176 186 SAGDRTQGLSH -> RYTFNSAIMIK (in isoform
3). {ECO:0000303|PubMed:11118290,
ECO:0000303|PubMed:9069287,
ECO:0000303|PubMed:9257717,
ECO:0000303|PubMed:9808458,
ECO:0000303|PubMed:9824313}.
/FTId=VSP_009067.
VAR_SEQ 187 366 Missing (in isoform 3).
{ECO:0000303|PubMed:11118290,
ECO:0000303|PubMed:9069287,
ECO:0000303|PubMed:9257717,
ECO:0000303|PubMed:9808458,
ECO:0000303|PubMed:9824313}.
/FTId=VSP_009068.
MUTAGEN 24 24 W->A: Disrupts binding to both GRM1 and
SHANK3. {ECO:0000269|PubMed:10798399}.
MUTAGEN 24 24 W->Y: Disrupts binding to GRM1.
{ECO:0000269|PubMed:10798399}.
MUTAGEN 70 70 T->A: Normal binding.
{ECO:0000269|PubMed:10798399}.
MUTAGEN 70 70 T->E: Disrupts binding to SHANK3.
{ECO:0000269|PubMed:10798399}.
MUTAGEN 74 74 F->A: Eliminates binding to both GRM1 and
SHANK3. {ECO:0000269|PubMed:10798399}.
MUTAGEN 76 76 Q->A: Normal binding.
{ECO:0000269|PubMed:10798399}.
MUTAGEN 76 76 Q->R: Normal binding.
{ECO:0000269|PubMed:10798399}.
MUTAGEN 85 85 V->A: Diminishes binding to GRM1.
{ECO:0000269|PubMed:10798399}.
MUTAGEN 89 89 G->A: Eliminates binding to both GRM1 and
SHANK3. {ECO:0000269|PubMed:10798399}.
MUTAGEN 89 89 G->N: Eliminates binding to both GRM1 and
SHANK3. {ECO:0000269|PubMed:10798399}.
CONFLICT 268 268 L -> R (in Ref. 5; BAA32477).
{ECO:0000305}.
STRAND 3 16 {ECO:0000244|PDB:1DDW}.
TURN 18 20 {ECO:0000244|PDB:1DDW}.
STRAND 23 27 {ECO:0000244|PDB:1DDW}.
STRAND 32 39 {ECO:0000244|PDB:1DDW}.
TURN 40 43 {ECO:0000244|PDB:1DDW}.
STRAND 44 51 {ECO:0000244|PDB:1DDW}.
STRAND 54 60 {ECO:0000244|PDB:1DDW}.
STRAND 71 79 {ECO:0000244|PDB:1DDW}.
TURN 80 83 {ECO:0000244|PDB:1DDW}.
STRAND 84 89 {ECO:0000244|PDB:1DDW}.
HELIX 93 110 {ECO:0000244|PDB:1DDW}.
HELIX 302 362 {ECO:0000244|PDB:3CVE}.
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


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