ARC_CHICK
ID ARC_CHICK Reviewed; 404 AA.
AC Q8AWC3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Activity-regulated cytoskeleton-associated protein {ECO:0000305};
DE AltName: Full=Activity-regulated gene 3.1 protein homolog {ECO:0000303|PubMed:15908132};
DE Short=ARC/ARG3.1 {ECO:0000303|PubMed:15908132};
DE Short=Arg3.1 {ECO:0000303|PubMed:15908132};
GN Name=ARC {ECO:0000250|UniProtKB:Q7LC44};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC81239.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Brain {ECO:0000312|EMBL:CAC81239.1};
RX PubMed=15908132; DOI=10.1016/j.neuroscience.2005.02.048;
RA Bock J., Thode C., Hannemann O., Braun K., Darlison M.G.;
RT "Early socio-emotional experience induces expression of the immediate-early
RT gene Arc/arg3.1 (activity-regulated cytoskeleton-associated
RT protein/activity-regulated gene) in learning-relevant brain regions of the
RT newborn chick.";
RL Neuroscience 133:625-633(2005).
CC -!- FUNCTION: Master regulator of synaptic plasticity that self-assembles
CC into virion-like capsids that encapsulate RNAs and mediate
CC intercellular RNA transfer in the nervous system. ARC protein is
CC released from neurons in extracellular vesicles that mediate the
CC transfer of ARC mRNA into new target cells, where ARC mRNA can undergo
CC activity-dependent translation. ARC capsids are endocytosed and are
CC able to transfer ARC mRNA into the cytoplasm of neurons. Acts as a key
CC regulator of synaptic plasticity: required for protein synthesis-
CC dependent forms of long-term potentiation (LTP) and depression (LTD)
CC and for the formation of long-term memory. Regulates synaptic
CC plasticity by promoting endocytosis of AMPA receptors (AMPARs) in
CC response to synaptic activity: this endocytic pathway maintains levels
CC of surface AMPARs in response to chronic changes in neuronal activity
CC through synaptic scaling, thereby contributing to neuronal homeostasis.
CC Acts as a postsynaptic mediator of activity-dependent synapse
CC elimination in the developing cerebellum by mediating elimination of
CC surplus climbing fiber synapses. Accumulates at weaker synapses,
CC probably to prevent their undesired enhancement. This suggests that
CC ARC-containing virion-like capsids may be required to eliminate
CC synaptic material. {ECO:0000250|UniProtKB:Q63053,
CC ECO:0000250|UniProtKB:Q9WV31}.
CC -!- SUBUNIT: Homooligomer; homooligomerizes into virion-like capsids.
CC {ECO:0000250|UniProtKB:Q63053, ECO:0000250|UniProtKB:Q9WV31}.
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle membrane
CC {ECO:0000250|UniProtKB:Q63053}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9WV31}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9WV31}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9WV31}. Synapse {ECO:0000250|UniProtKB:Q63053}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q63053}. Early endosome
CC membrane {ECO:0000250|UniProtKB:Q63053}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63053}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q63053}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q63053}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q63053}. Note=Forms virion-like extracellular
CC vesicles that are released from neurons. Enriched in postsynaptic
CC density of dendritic spines. Accumulates at weaker synapses may be
CC required to prevent their undesired enhancement. Associated with the
CC cell cortex of neuronal soma and dendrites.
CC {ECO:0000250|UniProtKB:Q63053, ECO:0000250|UniProtKB:Q9WV31}.
CC -!- TISSUE SPECIFICITY: Expressed at various levels throughout the brain.
CC {ECO:0000269|PubMed:15908132}.
CC -!- INDUCTION: By synaptic activity. Transcript level significantly
CC increased in auditory cortex as well as two higher-associative brain
CC regions by auditory imprinting stimulus in newborn chicks.
CC {ECO:0000269|PubMed:15908132}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins: it contains large N- and C-terminal domains that form a bi-
CC lobar architecture similar to the capsid domain of human
CC immunodeficiency virus (HIV) gag protein. It contains structural
CC elements found within viral Gag polyproteins originated from the
CC Ty3/gypsy retrotransposon family and retains the ability to form
CC virion-like capsid structures that can mediate mRNA transfer between
CC cells. Tetrapod and fly Arc protein-coding genes originated
CC independently from distinct lineages of Ty3/gypsy retrotransposons.
CC {ECO:0000250|UniProtKB:Q63053}.
CC -!- PTM: Palmitoylation anchors the protein into the membrane by allowing
CC direct insertion into the hydrophobic core of the lipid bilayer.
CC {ECO:0000250|UniProtKB:Q9WV31}.
CC -!- SIMILARITY: Belongs to the ARC/ARG3.1 family. {ECO:0000305}.
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DR EMBL; AJ272062; CAC81239.1; -; mRNA.
DR RefSeq; NP_989763.1; NM_204432.1.
DR RefSeq; XP_015138650.1; XM_015283164.1.
DR AlphaFoldDB; Q8AWC3; -.
DR SMR; Q8AWC3; -.
DR STRING; 9031.ENSGALP00000025980; -.
DR PaxDb; Q8AWC3; -.
DR Ensembl; ENSGALT00000026027; ENSGALP00000025980; ENSGALG00000016154.
DR GeneID; 395075; -.
DR KEGG; gga:395075; -.
DR CTD; 23237; -.
DR VEuPathDB; HostDB:geneid_395075; -.
DR eggNOG; ENOG502QSPT; Eukaryota.
DR GeneTree; ENSGT00390000003914; -.
DR HOGENOM; CLU_782004_0_0_1; -.
DR InParanoid; Q8AWC3; -.
DR OMA; AKKWWEY; -.
DR OrthoDB; 904267at2759; -.
DR PhylomeDB; Q8AWC3; -.
DR TreeFam; TF335604; -.
DR PRO; PR:Q8AWC3; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000016154; Expressed in brain and 3 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1903561; C:extracellular vesicle; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:0110077; P:vesicle-mediated intercellular transport; ISS:UniProtKB.
DR InterPro; IPR023263; Arc.
DR InterPro; IPR040814; Arc_C.
DR InterPro; IPR045557; Arc_N.
DR PANTHER; PTHR15962; PTHR15962; 1.
DR Pfam; PF18162; Arc_C; 1.
DR Pfam; PF19284; Arc_MA; 1.
DR PRINTS; PR02027; ARCARG31.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Endocytosis; Endosome; Lipoprotein; Membrane;
KW Palmitate; Postsynaptic cell membrane; Reference proteome; RNA-binding;
KW Synapse; Transport.
FT CHAIN 1..404
FT /note="Activity-regulated cytoskeleton-associated protein"
FT /id="PRO_0000273288"
FT REGION 351..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..78
FT /evidence="ECO:0000255"
FT COMPBIAS 357..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 46307 MW; 8052650A72C9DC40 CRC64;
MQLDNVTNAG IHSFQGHRGV ANKPNVILQI GKCRAEMLEH VRRTHRHLLS EVSKQVEREL
KGLQKSVGKL ENNLEDHVPT DNQRWKKSIK ACLARCQETI AHLERWVKRE MNVWKEVFFR
LEKWADRLES MGGKYCPGEH GKQTVSVGVG GPEIRPSEGE IYDYALDMSQ MYALTPAPGE
VPSIPQAHDS YQWVSVSEDA PASPVETQIF EDPHEFLSHL EEYLKQVGGT EEYWLSQIQN
HMNGPAKKWW EYKQDSVKNW VEFKKEFLQY SEGTLTRDAI KRELDLPQKE GEPLDQFLWR
KRDLYQTLYV DADEEEIIQY VVGTLQPKLK RFLSYPLPKT LEQLIQRGKE VQGNMDHSEE
PSPQRTPEIQ SGDSVESMPP STTASPVPSN GTQPEPPSPP ATVI
