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Entry version 115 (02 Dec 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Activity-regulated cytoskeleton-associated protein

Gene

Arc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system (PubMed:29328916). ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA can undergo activity-dependent translation (PubMed:29328916). ARC capsids are endocytosed and are able to transfer ARC mRNA into the cytoplasm of neurons (PubMed:29328916). Acts as a key regulator of synaptic plasticity: required for protein synthesis-dependent forms of long-term potentiation (LTP) and depression (LTD) and for the formation of long-term memory (PubMed:10818134, PubMed:17088211, PubMed:17088212, PubMed:17088213). Regulates synaptic plasticity by promoting endocytosis of AMPA receptors (AMPARs) in response to synaptic activity: this endocytic pathway maintains levels of surface AMPARs in response to chronic changes in neuronal activity through synaptic scaling, thereby contributing to neuronal homeostasis (PubMed:17088211, PubMed:17088212). Acts as a postsynaptic mediator of activity-dependent synapse elimination in the developing cerebellum by mediating elimination of surplus climbing fiber synapses (PubMed:23791196). Accumulates at weaker synapses, probably to prevent their undesired enhancement (PubMed:22579289). This suggests that ARC-containing virion-like capsids may be required to eliminate synaptic material (PubMed:29328916). Required to transduce experience into long-lasting changes in visual cortex plasticity and for long-term memory (PubMed:10818134). Involved in postsynaptic trafficking and processing of amyloid-beta A4 (APP) via interaction with PSEN1 (By similarity). In addition to its role in synapses, also involved in the regulation of the immune system: specifically expressed in skin-migratory dendritic cells and regulates fast dendritic cell migration, thereby regulating T-cell activation (By similarity).By similarity7 Publications

Miscellaneous

Transcripts enriched in dendrites may be translated locally.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, RNA-binding
Biological processEndocytosis, Transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Activity-regulated cytoskeleton-associated protein1 Publication
Alternative name(s):
Activity-regulated gene 3.1 proteinBy similarity
Short name:
ARC/ARG3.1By similarity
Short name:
Arg3.1By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Arc1 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Rat genome database

More...
RGDi
62037, Arc

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Membrane, Postsynaptic cell membrane, Synapse

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002732871 – 396Activity-regulated cytoskeleton-associated proteinAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei260PhosphoserineBy similarity1
Modified residuei278PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Palmitoylation anchors the protein into the membrane by allowing direct insertion into the hydrophobic core of the lipid bilayer.By similarity
Ubiquitinated by UBE3A, leading to its degradation by the proteasome, thereby promoting AMPA receptors (AMPARs) expression at synapses.By similarity
Phosphorylation at Ser-260 by CaMK2 prevents homooligomerization into virion-like capsids by disrupting an interaction surface essential for high-order oligomerization. Phosphorylation by CaMK2 inhibits synaptic activity.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q63053

PRoteomics IDEntifications database

More...
PRIDEi
Q63053

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q63053

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q63053

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed exclusively in certain parts of the brain including cortex and molecular layer of the hippocampus. Typically expressed at high level in a minority of neurons. Basal expression higher in cortex than in hippocampus, highest in visual cortex.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during postnatal development from day 8 (PubMed:7857651). Highest expression around day 23 with moderate levels expressed to adulthood (PubMed:7857651).1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Arc expression is regulated at transcription, post-transcription and translation levels (PubMed:9808461, PubMed:10570490, PubMed:11226315, PubMed:18614031). Transcription is tightly coupled to encoding of information in neuronal circuits (PubMed:10570490). Expression is induced by neuronal and synaptic activity (PubMed:7777577, PubMed:7857651, PubMed:10570490). Induced at highest level in hippocampus within 30 minutes, dropping to basal levels within 24 hours (PubMed:7777577, PubMed:7857651). Arc transcripts are transported to dendrites and become enriched at sites of local synaptic activity where they are locally translated into protein (PubMed:9808461, PubMed:18614031). Arc transcripts resemble some viral RNAs and contain an internal ribosomal entry site (IRES) that allows cap-independent translation (PubMed:11226315).6 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000043465, Expressed in frontal cortex and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q63053, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooligomer; homooligomerizes into virion-like capsids (PubMed:29328916, PubMed:30028513, PubMed:31080121).

Interacts with SH3GL1/endophilin-2, SH3GL3/endophilin-3 and DNM2/DYN2 (PubMed:17088211).

Interacts with CAMK2B (in the kinase inactive state); leading to target ARC to inactive synapses (PubMed:22579289).

Interacts with PSEN1 (By similarity).

Interacts with GRIN2A and GRIN2B; inhibiting homooligomerization (PubMed:31080121).

By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
248539, 8 interactors

Protein interaction database and analysis system

More...
IntActi
Q63053, 6 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000063719

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q63053

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni89 – 100Interaction with SH3GL1 or SH3GL31 PublicationAdd BLAST12
Regioni195 – 214Interaction with DNM21 PublicationAdd BLAST20

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili54 – 78Sequence analysisAdd BLAST25

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The protein is evolutionarily related to retrotransposon Gag proteins: it contains large N- and C-terminal domains that form a bi-lobar architecture similar to the capsid domain of human immunodeficiency virus (HIV) gag protein (PubMed:29328916, PubMed:25864631). It contains structural elements found within viral Gag polyproteins originated from the Ty3/gypsy retrotransposon family and retains the ability to form virion-like capsid structures that can mediate mRNA transfer between cells (PubMed:29328916). Tetrapod and fly Arc protein-coding genes originated independently from distinct lineages of Ty3/gypsy retrotransposons (PubMed:29328916).2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ARC/ARG3.1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QSPT, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000003914

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_782004_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q63053

Identification of Orthologs from Complete Genome Data

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OMAi
MGGKYPV

Database of Orthologous Groups

More...
OrthoDBi
904267at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q63053

TreeFam database of animal gene trees

More...
TreeFami
TF335604

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023263, Activity-reg_cytoskelet-assoc
IPR040814, Arc_C

The PANTHER Classification System

More...
PANTHERi
PTHR15962, PTHR15962, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18162, Arc_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR02027, ARCARG31

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q63053-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELDHMTTGG LHAYPAPRGG PAAKPNVILQ IGKCRAEMLE HVRRTHRHLL
60 70 80 90 100
TEVSKQVERE LKGLHRSVGK LENNLDGYVP TGDSQRWKKS IKACLCRCQE
110 120 130 140 150
TIANLERWVK REMHVWREVF YRLERWADRL ESMGGKYPVG SEPARHTVSV
160 170 180 190 200
GVGGPEPYCQ EADGYDYTVS PYAITPPPAA GELPEQESVG AQQYQSWVPG
210 220 230 240 250
EDGQPSPGVD TQIFEDPREF LSHLEEYLRQ VGGSEEYWLS QIQNHMNGPA
260 270 280 290 300
KKWWEFKQGS VKNWVEFKKE FLQYSEGTLS REAIQRELDL PQKQGEPLDQ
310 320 330 340 350
FLWRKRDLYQ TLYVDAEEEE IIQYVVGTLQ PKFKRFLRHP LPKTLEQLIQ
360 370 380 390
RGMEVQDGLE QAAEPSVTPL PTEDETEALT PALTSESVAS DRTQPE
Length:396
Mass (Da):45,353
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4E95B46B75853CA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti209V → L in AAA68695 (PubMed:7857651).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U19866 mRNA Translation: AAA68695.1
Z46925 mRNA Translation: CAA87033.1

Protein sequence database of the Protein Information Resource

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PIRi
I58168

NCBI Reference Sequences

More...
RefSeqi
NP_062234.1, NM_019361.1
XP_017450553.1, XM_017595064.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000067442; ENSRNOP00000063719; ENSRNOG00000043465
ENSRNOT00000076998; ENSRNOP00000068090; ENSRNOG00000043465

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
54323

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:54323

UCSC genome browser

More...
UCSCi
RGD:62037, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19866 mRNA Translation: AAA68695.1
Z46925 mRNA Translation: CAA87033.1
PIRiI58168
RefSeqiNP_062234.1, NM_019361.1
XP_017450553.1, XM_017595064.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4X3HX-ray2.40A207-277[»]
4X3IX-ray1.80A207-277[»]
4X3XX-ray2.00A278-362[»]
6GSENMR-A206-364[»]
SMRiQ63053
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi248539, 8 interactors
IntActiQ63053, 6 interactors
STRINGi10116.ENSRNOP00000063719

PTM databases

iPTMnetiQ63053
PhosphoSitePlusiQ63053

Proteomic databases

PaxDbiQ63053
PRIDEiQ63053

Genome annotation databases

EnsembliENSRNOT00000067442; ENSRNOP00000063719; ENSRNOG00000043465
ENSRNOT00000076998; ENSRNOP00000068090; ENSRNOG00000043465
GeneIDi54323
KEGGirno:54323
UCSCiRGD:62037, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23237
RGDi62037, Arc

Phylogenomic databases

eggNOGiENOG502QSPT, Eukaryota
GeneTreeiENSGT00390000003914
HOGENOMiCLU_782004_0_0_1
InParanoidiQ63053
OMAiMGGKYPV
OrthoDBi904267at2759
PhylomeDBiQ63053
TreeFamiTF335604

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q63053

Gene expression databases

BgeeiENSRNOG00000043465, Expressed in frontal cortex and 20 other tissues
GenevisibleiQ63053, RN

Family and domain databases

InterProiView protein in InterPro
IPR023263, Activity-reg_cytoskelet-assoc
IPR040814, Arc_C
PANTHERiPTHR15962, PTHR15962, 1 hit
PfamiView protein in Pfam
PF18162, Arc_C, 1 hit
PRINTSiPR02027, ARCARG31

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARC_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q63053
Secondary accession number(s): Q62743
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: November 1, 1996
Last modified: December 2, 2020
This is version 115 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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