HOME1_BOVIN
ID HOME1_BOVIN Reviewed; 354 AA.
AC Q2KJ56;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Homer protein homolog 1 {ECO:0000250|UniProtKB:Q86YM7};
DE Short=Homer-1;
GN Name=HOMER1 {ECO:0000250|UniProtKB:Q86YM7};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Forms a high-order
CC complex with SHANK1, which in turn is necessary for the structural and
CC functional integrity of dendritic spines (By similarity). Negatively
CC regulates T cell activation by inhibiting the calcineurin-NFAT pathway.
CC Acts by competing with calcineurin/PPP3CA for NFAT protein binding,
CC hence preventing NFAT activation by PPP3CA (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q86YM7,
CC ECO:0000250|UniProtKB:Q9Z214}.
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 (By
CC similarity). Interacts with GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2 and
CC SHANK3. Interacts with IFT57 and OPHN1. Encodes a coiled-coil structure
CC that mediates homo- and heteromultimerization (By similarity).
CC Interacts with SHANK1; forms high-order polymerized complex with a
CC mesh-like network structure, at least composed of SHANK1, HOMER1 and
CC DLGAP1; the complex formation is SHANK1 multimerization dependent (By
CC similarity). Interacts with NFATC4 (By similarity). Interacts with
CC DAGLA (via PPXXF motif); this interaction is required for the cell
CC membrane localization of DAGLA (By similarity). Interacts with SRGAP2
CC (By similarity). {ECO:0000250|UniProtKB:Q86YM7,
CC ECO:0000250|UniProtKB:Q9Z214, ECO:0000250|UniProtKB:Q9Z2Y3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Synapse {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q9Z214}.
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 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9Z214}.
CC -!- SIMILARITY: Belongs to the Homer family. {ECO:0000305}.
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DR EMBL; BC105509; AAI05510.1; -; mRNA.
DR RefSeq; NP_001069520.1; NM_001076052.1.
DR AlphaFoldDB; Q2KJ56; -.
DR BMRB; Q2KJ56; -.
DR SMR; Q2KJ56; -.
DR STRING; 9913.ENSBTAP00000017647; -.
DR PaxDb; Q2KJ56; -.
DR Ensembl; ENSBTAT00000017647; ENSBTAP00000017647; ENSBTAG00000025853.
DR GeneID; 535311; -.
DR KEGG; bta:535311; -.
DR CTD; 9456; -.
DR VEuPathDB; HostDB:ENSBTAG00000025853; -.
DR VGNC; VGNC:29901; HOMER1.
DR eggNOG; ENOG502QR3K; Eukaryota.
DR GeneTree; ENSGT00940000156354; -.
DR HOGENOM; CLU_033940_0_0_1; -.
DR InParanoid; Q2KJ56; -.
DR OMA; GKMGEQP; -.
DR OrthoDB; 1251658at2759; -.
DR TreeFam; TF325627; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000025853; Expressed in occipital lobe and 106 other tissues.
DR ExpressionAtlas; Q2KJ56; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0043034; C:costamere; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0044309; C:neuron spine; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR GO; GO:0048875; P:chemical homeostasis within a tissue; IEA:Ensembl.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0090279; P:regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:2001257; P:regulation of cation channel activity; IEA:Ensembl.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISS:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IEA:Ensembl.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IBA:GO_Central.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86YM7"
FT CHAIN 2..354
FT /note="Homer protein homolog 1"
FT /id="PRO_0000284055"
FT DOMAIN 1..110
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 114..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..354
FT /note="Required for tetramerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z214"
FT COILED 181..352
FT /evidence="ECO:0000255"
FT COMPBIAS 122..147
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 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Y3"
SQ SEQUENCE 354 AA; 40370 MW; 8519126E1F25D966 CRC64;
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL DGSKAIINST
ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA EKFQEFKEAA RLAKEKSQEK
MELTSTPSQE SAGGDLQSPL TPESINGTDD ERTPDLTQNS EPRPEPTQNA LPFTHSSAIS
KHWEAELATL KGNNAKLTAA LLESTANVKQ WKQQLAAYQE EAERLHKRVT ELECVSSQAN
AVHTHKTELN QTIQELEETL KVKEEEIERL KQEIDNAREL QEQRDSLTQK LQEVEIRNKD
LEGQLSDLEQ RLEKSQNEQE AFRNNLKTLL EILDGKIFEL TELRDNLAKL LERS
