HOME3_RAT
ID HOME3_RAT Reviewed; 358 AA.
AC Q9Z2X5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Homer protein homolog 3 {ECO:0000305};
DE Short=Homer-3;
DE AltName: Full=VASP/Ena-related gene up-regulated during seizure and LTP 3;
DE Short=Vesl-3 {ECO:0000303|Ref.1};
GN Name=Homer3 {ECO:0000312|RGD:620706}; Synonyms=Vesl3;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Kato A., Ageta H., Sugiyama H.;
RT "Rattus norvegicus mRNA for Vesl-3, complete cds.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-158, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Negatively regulates
CC T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by
CC competing with calcineurin/PPP3CA for NFAT protein binding, hence
CC preventing NFAT activation by PPP3CA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q99JP6, ECO:0000250|UniProtKB:Q9NSC5}.
CC -!- SUBUNIT: Tetramer (By similarity). Encodes coiled-coil structures that
CC mediate homo- and heteromultimerization. Interacts with NFATC2;
CC interaction is calcium independent; interaction competes with PPP3CA
CC for NFATC2 binding; interaction is reduced by AKT activation. Interacts
CC with NFATC1 and NFATC4. Interacts with SHANK1; forms a high-order
CC complex at least composed of SHANK1 and HOMER3; the complex formation
CC is regulated by CAMK2A-mediated phosphorylation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9NSC5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Synapse {ECO:0000250}. Note=Postsynaptic density of
CC neuronal cells. {ECO:0000250}.
CC -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5,
CC RYR1, RYR2, ITPR1, SHANK 1 and SHANK3.
CC -!- SIMILARITY: Belongs to the Homer family. {ECO:0000305}.
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DR EMBL; AB020879; BAA35110.2; -; mRNA.
DR RefSeq; NP_445762.1; NM_053310.1.
DR RefSeq; XP_006252953.1; XM_006252891.3.
DR AlphaFoldDB; Q9Z2X5; -.
DR BMRB; Q9Z2X5; -.
DR SMR; Q9Z2X5; -.
DR BioGRID; 248182; 5.
DR IntAct; Q9Z2X5; 5.
DR MINT; Q9Z2X5; -.
DR STRING; 10116.ENSRNOP00000027428; -.
DR iPTMnet; Q9Z2X5; -.
DR PhosphoSitePlus; Q9Z2X5; -.
DR PaxDb; Q9Z2X5; -.
DR PRIDE; Q9Z2X5; -.
DR GeneID; 29548; -.
DR KEGG; rno:29548; -.
DR UCSC; RGD:620706; rat.
DR CTD; 9454; -.
DR RGD; 620706; Homer3.
DR VEuPathDB; HostDB:ENSRNOG00000020229; -.
DR eggNOG; ENOG502R3T0; Eukaryota.
DR HOGENOM; CLU_033940_0_0_1; -.
DR InParanoid; Q9Z2X5; -.
DR OMA; KICDLKD; -.
DR OrthoDB; 1251658at2759; -.
DR PhylomeDB; Q9Z2X5; -.
DR TreeFam; TF325627; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:Q9Z2X5; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000020229; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q9Z2X5; baseline and differential.
DR Genevisible; Q9Z2X5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045178; C:basal part of cell; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISS: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; IBA:GO_Central.
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 Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..358
FT /note="Homer protein homolog 3"
FT /id="PRO_0000191013"
FT DOMAIN 1..113
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 1..80
FT /note="Required for interaction with NFATC2"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC5"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..122
FT /evidence="ECO:0000255"
FT COILED 190..355
FT /evidence="ECO:0000255"
FT COMPBIAS 249..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 358 AA; 39891 MW; 4896E23D6A63517E CRC64;
MSTAREQPIF STRAHVFQID PATKRNWIPA GKHALTVSYF YDATRNVYRI ISIGGAKAII
NSTVTPNMTF TKTSQKFGQW ADSRANTVYG LGFGSEQQLT QFAEKFQEVK EAARLAREKS
QDGGELTSTA LAMASHQVPP SPLVSTNGPE EKLFRSQSAD APGPTERERL KKMLSEGSVG
EVQWEAEFFA LQDSNQRLAG ALREANAAAT QWRQQLEVQR AEAEHLRQRV AELEAQVAAE
PVRAGEKEAT SQSVEQLEAR VQTKDQEIQT LKNQSTGPRE APDTAEREET QQQVQDLETR
NAELEQQLRA MESNLEEARA ERERARAEVG RAAQLLDVRL FELSELREGL ARLAEAAP
