ID ARC_RAT Reviewed; 396 AA. AC Q63053; Q62743; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Activity-regulated cytoskeleton-associated protein {ECO:0000303|PubMed:7857651}; DE AltName: Full=Activity-regulated gene 3.1 protein {ECO:0000250|UniProtKB:Q9WV31}; DE Short=ARC/ARG3.1 {ECO:0000250|UniProtKB:Q9WV31}; DE Short=Arg3.1 {ECO:0000250|UniProtKB:Q9WV31}; GN Name=Arc {ECO:0000303|PubMed:7857651, ECO:0000312|RGD:62037}; 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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND INDUCTION. RC TISSUE=Hippocampus; RX PubMed=7857651; DOI=10.1016/0896-6273(95)90299-6; RA Lyford G.L., Yamagata K., Kaufmann W.E., Barnes C.A., Sanders L.K., RA Copeland N.G., Gilbert D.J., Jenkins N.A., Lanahan A.A., Worley P.F.; RT "Arc, a growth factor and activity-regulated gene, encodes a novel RT cytoskeleton-associated protein that is enriched in neuronal dendrites."; RL Neuron 14:433-445(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RX PubMed=7777577; DOI=10.1073/pnas.92.12.5734; RA Link W., Konietzko U., Kauselmann G., Krug M., Schwanke B., Frey U., RA Kuhl D.; RT "Somatodendritic expression of an immediate early gene is regulated by RT synaptic activity."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5734-5738(1995). RN [3] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=9808461; DOI=10.1016/s0896-6273(00)80591-7; RA Steward O., Wallace C.S., Lyford G.L., Worley P.F.; RT "Synaptic activation causes the mRNA for the IEG Arc to localize RT selectively near activated postsynaptic sites on dendrites."; RL Neuron 21:741-751(1998). RN [4] RP INDUCTION. RX PubMed=10570490; DOI=10.1038/16046; RA Guzowski J.F., McNaughton B.L., Barnes C.A., Worley P.F.; RT "Environment-specific expression of the immediate-early gene Arc in RT hippocampal neuronal ensembles."; RL Nat. Neurosci. 2:1120-1124(1999). RN [5] RP FUNCTION. RX PubMed=10818134; DOI=10.1523/jneurosci.20-11-03993.2000; RA Guzowski J.F., Lyford G.L., Stevenson G.D., Houston F.P., McGaugh J.L., RA Worley P.F., Barnes C.A.; RT "Inhibition of activity-dependent arc protein expression in the rat RT hippocampus impairs the maintenance of long-term potentiation and the RT consolidation of long-term memory."; RL J. Neurosci. 20:3993-4001(2000). RN [6] RP INDUCTION. RX PubMed=11226315; DOI=10.1073/pnas.051623398; RA Pinkstaff J.K., Chappell S.A., Mauro V.P., Edelman G.M., Krushel L.A.; RT "Internal initiation of translation of five dendritically localized RT neuronal mRNAs."; RL Proc. Natl. Acad. Sci. U.S.A. 98:2770-2775(2001). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNM2; SH3GL1 AND RP SH3GL3. RX PubMed=17088211; DOI=10.1016/j.neuron.2006.08.033; RA Chowdhury S., Shepherd J.D., Okuno H., Lyford G., Petralia R.S., Plath N., RA Kuhl D., Huganir R.L., Worley P.F.; RT "Arc/Arg3.1 interacts with the endocytic machinery to regulate AMPA RT receptor trafficking."; RL Neuron 52:445-459(2006). RN [8] RP FUNCTION. RX PubMed=17088212; DOI=10.1016/j.neuron.2006.09.031; RA Rial Verde E.M., Lee-Osbourne J., Worley P.F., Malinow R., Cline H.T.; RT "Increased expression of the immediate-early gene arc/arg3.1 reduces AMPA RT receptor-mediated synaptic transmission."; RL Neuron 52:461-474(2006). RN [9] RP FUNCTION. RX PubMed=17088213; DOI=10.1016/j.neuron.2006.08.034; RA Shepherd J.D., Rumbaugh G., Wu J., Chowdhury S., Plath N., Kuhl D., RA Huganir R.L., Worley P.F.; RT "Arc/Arg3.1 mediates homeostatic synaptic scaling of AMPA Receptors."; RL Neuron 52:475-484(2006). RN [10] RP INDUCTION. RX PubMed=18614031; DOI=10.1016/j.neuron.2008.05.014; RA Waung M.W., Pfeiffer B.E., Nosyreva E.D., Ronesi J.A., Huber K.M.; RT "Rapid translation of Arc/Arg3.1 selectively mediates mGluR-dependent LTD RT through persistent increases in AMPAR endocytosis rate."; RL Neuron 59:84-97(2008). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAMK2B. RX PubMed=22579289; DOI=10.1016/j.cell.2012.02.062; RA Okuno H., Akashi K., Ishii Y., Yagishita-Kyo N., Suzuki K., Nonaka M., RA Kawashima T., Fujii H., Takemoto-Kimura S., Abe M., Natsume R., RA Chowdhury S., Sakimura K., Worley P.F., Bito H.; RT "Inverse synaptic tagging of inactive synapses via dynamic interaction of RT Arc/Arg3.1 with CaMKIIbeta."; RL Cell 149:886-898(2012). RN [12] RP FUNCTION. RX PubMed=23791196; DOI=10.1016/j.neuron.2013.04.036; RA Mikuni T., Uesaka N., Okuno H., Hirai H., Deisseroth K., Bito H., Kano M.; RT "Arc/Arg3.1 is a postsynaptic mediator of activity-dependent synapse RT elimination in the developing cerebellum."; RL Neuron 78:1024-1035(2013). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND RNA-BINDING. RX PubMed=29328916; DOI=10.1016/j.cell.2017.12.024; RA Pastuzyn E.D., Day C.E., Kearns R.B., Kyrke-Smith M., Taibi A.V., RA McCormick J., Yoder N., Belnap D.M., Erlendsson S., Morado D.R., RA Briggs J.A.G., Feschotte C., Shepherd J.D.; RT "The neuronal gene Arc encodes a repurposed retrotransposon Gag protein RT that mediates intercellular RNA transfer."; RL Cell 172:275-288(2018). RN [14] RP SUBUNIT. RX PubMed=30028513; DOI=10.1111/jnc.14556; RA Hallin E.I., Eriksen M.S., Baryshnikov S., Nikolaienko O., Groedem S., RA Hosokawa T., Hayashi Y., Bramham C.R., Kursula P.; RT "Structure of monomeric full-length ARC sheds light on molecular RT flexibility, protein interactions, and functional modalities."; RL J. Neurochem. 147:323-343(2018). RN [15] {ECO:0007744|PDB:4X3H, ECO:0007744|PDB:4X3I, ECO:0007744|PDB:4X3X} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 207-277, AND DOMAIN. RX PubMed=25864631; DOI=10.1016/j.neuron.2015.03.030; RA Zhang W., Wu J., Ward M.D., Yang S., Chuang Y.A., Xiao M., Li R., RA Leahy D.J., Worley P.F.; RT "Structural basis of arc binding to synaptic proteins: implications for RT cognitive disease."; RL Neuron 86:490-500(2015). RN [16] RP STRUCTURE BY NMR OF 206-364, SUBUNIT, AND INTERACTION WITH GRIN2A AND RP GRIN2B. RX PubMed=31080121; DOI=10.1016/j.str.2019.04.001; RA Nielsen L.D., Pedersen C.P., Erlendsson S., Teilum K.; RT "The capsid domain of Arc changes its oligomerization propensity through RT direct interaction with the NMDA receptor."; RL Structure 0:0-0(2019). 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 (PubMed:29328916). ARC CC protein is released from neurons in extracellular vesicles that mediate CC the transfer of ARC mRNA into new target cells, where ARC mRNA can CC undergo activity-dependent translation (PubMed:29328916). ARC capsids CC are endocytosed and are able to transfer ARC mRNA into the cytoplasm of CC neurons (PubMed:29328916). Acts as a key regulator of synaptic CC plasticity: required for protein synthesis-dependent forms of long-term CC potentiation (LTP) and depression (LTD) and for the formation of long- CC term memory (PubMed:10818134, PubMed:17088211, PubMed:17088212, CC PubMed:17088213). Regulates synaptic plasticity by promoting CC endocytosis of AMPA receptors (AMPARs) in response to synaptic CC activity: this endocytic pathway maintains levels of surface AMPARs in CC response to chronic changes in neuronal activity through synaptic CC scaling, thereby contributing to neuronal homeostasis (PubMed:17088211, CC PubMed:17088212). Acts as a postsynaptic mediator of activity-dependent CC synapse elimination in the developing cerebellum by mediating CC elimination of surplus climbing fiber synapses (PubMed:23791196). CC Accumulates at weaker synapses, probably to prevent their undesired CC enhancement (PubMed:22579289). This suggests that ARC-containing CC virion-like capsids may be required to eliminate synaptic material CC (PubMed:29328916). Required to transduce experience into long-lasting CC changes in visual cortex plasticity and for long-term memory CC (PubMed:10818134). Involved in postsynaptic trafficking and processing CC of amyloid-beta A4 (APP) via interaction with PSEN1 (By similarity). In CC addition to its role in synapses, also involved in the regulation of CC the immune system: specifically expressed in skin-migratory dendritic CC cells and regulates fast dendritic cell migration, thereby regulating CC T-cell activation (By similarity). {ECO:0000250|UniProtKB:Q9WV31, CC ECO:0000269|PubMed:10818134, ECO:0000269|PubMed:17088211, CC ECO:0000269|PubMed:17088212, ECO:0000269|PubMed:17088213, CC ECO:0000269|PubMed:22579289, ECO:0000269|PubMed:23791196, CC ECO:0000269|PubMed:29328916}. CC -!- SUBUNIT: Homooligomer; homooligomerizes into virion-like capsids CC (PubMed:29328916, PubMed:30028513, PubMed:31080121). Interacts with CC SH3GL1/endophilin-2, SH3GL3/endophilin-3 and DNM2/DYN2 CC (PubMed:17088211). Interacts with CAMK2B (in the kinase inactive CC state); leading to target ARC to inactive synapses (PubMed:22579289). CC Interacts with PSEN1 (By similarity). Interacts with GRIN2A and GRIN2B; CC inhibiting homooligomerization (PubMed:31080121). CC {ECO:0000250|UniProtKB:Q9WV31, ECO:0000269|PubMed:17088211, CC ECO:0000269|PubMed:22579289, ECO:0000269|PubMed:29328916, CC ECO:0000269|PubMed:30028513, ECO:0000269|PubMed:31080121}. CC -!- INTERACTION: CC Q63053; P08413: Camk2b; NbExp=6; IntAct=EBI-5275794, EBI-916155; CC Q63053; PRO_0000025591 [P49768]: PSEN1; Xeno; NbExp=3; IntAct=EBI-5275794, EBI-2606326; CC -!- SUBCELLULAR LOCATION: Extracellular vesicle membrane CC {ECO:0000269|PubMed:29328916}; Lipid-anchor CC {ECO:0000250|UniProtKB:Q9WV31}. Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:Q9WV31}; Lipid-anchor CC {ECO:0000250|UniProtKB:Q9WV31}. Synapse {ECO:0000269|PubMed:17088211, CC ECO:0000269|PubMed:22579289}. Postsynaptic density CC {ECO:0000269|PubMed:17088211}. Early endosome membrane CC {ECO:0000269|PubMed:17088211}. Cell projection, dendrite CC {ECO:0000269|PubMed:7857651, ECO:0000269|PubMed:9808461}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:7857651}. Cytoplasm, cell cortex CC {ECO:0000269|PubMed:7857651}. Cell projection, dendritic spine CC {ECO:0000269|PubMed:17088211}. Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000250|UniProtKB:Q9WV31}. Cytoplasmic vesicle, clathrin- CC coated vesicle membrane {ECO:0000250|UniProtKB:Q7LC44}. Note=Forms CC virion-like extracellular vesicles that are released from neurons CC (PubMed:29328916). Enriched in postsynaptic density of dendritic spines CC (PubMed:17088211). Targeted to inactive synapses following interaction CC with CAMK2B in the kinase inactive state (PubMed:22579289). CC Accumulation at weaker synapses may be required to prevent their CC undesired enhancement (PubMed:22579289). Associated with the cell CC cortex of neuronal soma and dendrites (PubMed:7857651). Associated with CC the sperm tail (By similarity). {ECO:0000250|UniProtKB:Q7LC44, CC ECO:0000250|UniProtKB:Q9WV31, ECO:0000269|PubMed:17088211, CC ECO:0000269|PubMed:22579289, ECO:0000269|PubMed:29328916, CC ECO:0000269|PubMed:7777577, ECO:0000269|PubMed:7857651}. CC -!- TISSUE SPECIFICITY: Expressed exclusively in certain parts of the brain CC including cortex and molecular layer of the hippocampus. Typically CC expressed at high level in a minority of neurons. Basal expression CC higher in cortex than in hippocampus, highest in visual cortex. CC {ECO:0000269|PubMed:7777577, ECO:0000269|PubMed:7857651}. CC -!- DEVELOPMENTAL STAGE: Expressed during postnatal development from day 8 CC (PubMed:7857651). Highest expression around day 23 with moderate levels CC expressed to adulthood (PubMed:7857651). {ECO:0000269|PubMed:7857651}. CC -!- INDUCTION: Arc expression is regulated at transcription, post- CC transcription and translation levels (PubMed:9808461, PubMed:10570490, CC PubMed:11226315, PubMed:18614031). Transcription is tightly coupled to CC encoding of information in neuronal circuits (PubMed:10570490). CC Expression is induced by neuronal and synaptic activity CC (PubMed:7777577, PubMed:7857651, PubMed:10570490). Induced at highest CC level in hippocampus within 30 minutes, dropping to basal levels within CC 24 hours (PubMed:7777577, PubMed:7857651). Arc transcripts are CC transported to dendrites and become enriched at sites of local synaptic CC activity where they are locally translated into protein CC (PubMed:9808461, PubMed:18614031). Arc transcripts resemble some viral CC RNAs and contain an internal ribosomal entry site (IRES) that allows CC cap-independent translation (PubMed:11226315). CC {ECO:0000269|PubMed:10570490, ECO:0000269|PubMed:11226315, CC ECO:0000269|PubMed:18614031, ECO:0000269|PubMed:7777577, CC ECO:0000269|PubMed:7857651, ECO:0000269|PubMed:9808461}. 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 (PubMed:29328916, CC PubMed:25864631). It contains structural elements found within viral CC Gag polyproteins originated from the Ty3/gypsy retrotransposon family CC and retains the ability to form virion-like capsid structures that can CC mediate mRNA transfer between cells (PubMed:29328916). Tetrapod and fly CC Arc protein-coding genes originated independently from distinct CC lineages of Ty3/gypsy retrotransposons (PubMed:29328916). CC {ECO:0000269|PubMed:25864631, ECO:0000269|PubMed:29328916}. 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 -!- PTM: Ubiquitinated by UBE3A, leading to its degradation by the CC proteasome, thereby promoting AMPA receptors (AMPARs) expression at CC synapses. Ubiquitinated by RNF216 at Lys-268 and Lys-269 limiting ARC CC protein levels induced by synaptic activity and thus regulating ARC- CC dependent forms of synaptic plasticity. {ECO:0000250|UniProtKB:Q7LC44, CC ECO:0000250|UniProtKB:Q9WV31}. CC -!- PTM: Phosphorylation at Ser-260 by CaMK2 prevents homooligomerization CC into virion-like capsids by disrupting an interaction surface essential CC for high-order oligomerization. Phosphorylation by CaMK2 inhibits CC synaptic activity. {ECO:0000250|UniProtKB:Q9WV31}. CC -!- MISCELLANEOUS: Transcripts enriched in dendrites may be translated CC locally. {ECO:0000269|PubMed:7777577}. CC -!- SIMILARITY: Belongs to the ARC/ARG3.1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U19866; AAA68695.1; -; mRNA. DR EMBL; Z46925; CAA87033.1; -; mRNA. DR PIR; I58168; I58168. DR RefSeq; NP_062234.1; NM_019361.1. DR RefSeq; XP_017450553.1; XM_017595064.1. DR PDB; 4X3H; X-ray; 2.40 A; A=207-277. DR PDB; 4X3I; X-ray; 1.80 A; A=207-277. DR PDB; 4X3X; X-ray; 2.00 A; A=278-362. DR PDB; 6GSE; NMR; -; A=206-364. DR PDB; 7R24; X-ray; 2.70 A; A=1-396. DR PDBsum; 4X3H; -. DR PDBsum; 4X3I; -. DR PDBsum; 4X3X; -. DR PDBsum; 6GSE; -. DR PDBsum; 7R24; -. DR AlphaFoldDB; Q63053; -. DR SMR; Q63053; -. DR BioGRID; 248539; 8. DR IntAct; Q63053; 6. DR STRING; 10116.ENSRNOP00000063719; -. DR iPTMnet; Q63053; -. DR PhosphoSitePlus; Q63053; -. DR PaxDb; 10116-ENSRNOP00000063719; -. DR Ensembl; ENSRNOT00000076998.3; ENSRNOP00000068090.1; ENSRNOG00000043465.4. DR Ensembl; ENSRNOT00055043515; ENSRNOP00055035508; ENSRNOG00055025242. DR Ensembl; ENSRNOT00060040062; ENSRNOP00060033063; ENSRNOG00060023163. DR Ensembl; ENSRNOT00065015439; ENSRNOP00065011615; ENSRNOG00065009634. DR GeneID; 54323; -. DR KEGG; rno:54323; -. DR UCSC; RGD:62037; rat. DR AGR; RGD:62037; -. DR CTD; 23237; -. DR RGD; 62037; Arc. DR eggNOG; ENOG502QSPT; Eukaryota. DR GeneTree; ENSGT00390000003914; -. DR HOGENOM; CLU_782004_0_0_1; -. DR InParanoid; Q63053; -. DR OMA; WEYKQGS; -. DR OrthoDB; 4578527at2759; -. DR PhylomeDB; Q63053; -. DR TreeFam; TF335604; -. DR PRO; PR:Q63053; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000043465; Expressed in frontal cortex and 16 other cell types or tissues. DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030425; C:dendrite; ISO:RGD. 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; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB. DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0098845; C:postsynaptic endosome; IDA:SynGO. DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB. DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD. 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:0007492; P:endoderm development; ISO:RGD. DR GO; GO:0007612; P:learning; IEP:RGD. DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB. DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; IMP:CACAO. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB. DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IGI:ARUK-UCL. DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISS:UniProtKB. DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:UniProtKB. DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEP:RGD. DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD. DR GO; GO:0043278; P:response to morphine; IEP:RGD. DR GO; GO:0110077; P:vesicle-mediated intercellular transport; IDA:UniProtKB. DR InterPro; IPR023263; Arc. DR InterPro; IPR040814; Arc_C. DR InterPro; IPR048965; Arc_capsid_dom. DR InterPro; IPR045557; Arc_N. DR PANTHER; PTHR15962; ACTIVITY-REGULATED CYTOSKELETON-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR15962:SF0; ACTIVITY-REGULATED CYTOSKELETON-ASSOCIATED PROTEIN; 1. DR Pfam; PF18162; Arc_C; 1. DR Pfam; PF21395; Arc_capsid_dom; 1. DR Pfam; PF19284; Arc_MA; 1. DR PRINTS; PR02027; ARCARG31. DR Genevisible; Q63053; RN. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cell projection; Coiled coil; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Developmental protein; Endocytosis; KW Endosome; Isopeptide bond; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; KW RNA-binding; Synapse; Transport; Ubl conjugation. FT CHAIN 1..396 FT /note="Activity-regulated cytoskeleton-associated protein" FT /id="PRO_0000273287" FT REGION 89..100 FT /note="Interaction with SH3GL1 or SH3GL3" FT /evidence="ECO:0000269|PubMed:17088211" FT REGION 195..214 FT /note="Interaction with DNM2" FT /evidence="ECO:0000269|PubMed:17088211" FT REGION 358..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 54..78 FT /evidence="ECO:0000255" FT COMPBIAS 378..396 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV31" FT MOD_RES 278 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV31" FT CROSSLNK 268 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q7LC44" FT CROSSLNK 269 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q7LC44" FT CONFLICT 209 FT /note="V -> L (in Ref. 1; AAA68695)" FT /evidence="ECO:0000305" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:4X3I" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 217..231 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 235..239 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 240..245 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 249..257 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 264..276 FT /evidence="ECO:0007829|PDB:4X3I" FT HELIX 279..288 FT /evidence="ECO:0007829|PDB:4X3X" FT HELIX 298..312 FT /evidence="ECO:0007829|PDB:4X3X" FT HELIX 318..327 FT /evidence="ECO:0007829|PDB:4X3X" FT HELIX 331..337 FT /evidence="ECO:0007829|PDB:4X3X" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:4X3X" FT HELIX 345..359 FT /evidence="ECO:0007829|PDB:4X3X" SQ SEQUENCE 396 AA; 45353 MW; 4E95B46B75853CA5 CRC64; MELDHMTTGG LHAYPAPRGG PAAKPNVILQ IGKCRAEMLE HVRRTHRHLL TEVSKQVERE LKGLHRSVGK LENNLDGYVP TGDSQRWKKS IKACLCRCQE TIANLERWVK REMHVWREVF YRLERWADRL ESMGGKYPVG SEPARHTVSV GVGGPEPYCQ EADGYDYTVS PYAITPPPAA GELPEQESVG AQQYQSWVPG EDGQPSPGVD TQIFEDPREF LSHLEEYLRQ VGGSEEYWLS QIQNHMNGPA KKWWEFKQGS VKNWVEFKKE FLQYSEGTLS REAIQRELDL PQKQGEPLDQ FLWRKRDLYQ TLYVDAEEEE IIQYVVGTLQ PKFKRFLRHP LPKTLEQLIQ RGMEVQDGLE QAAEPSVTPL PTEDETEALT PALTSESVAS DRTQPE //