ID   ARC_MOUSE               Reviewed;         396 AA.
AC   Q9WV31; Q9ES15;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   14-DEC-2011, entry version 70.
DE   RecName: Full=Activity-regulated cytoskeleton-associated protein;
DE   AltName: Full=ARC/ARG3.1;
DE            Short=mArc;
DE   AltName: Full=Activity-regulated gene 3.1 protein homolog;
DE            Short=Arg3.1;
GN   Name=Arc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=21359664; PubMed=11466419;
RA   Waltereit R., Dammermann B., Wulff P., Scafidi J., Staubli U.,
RA   Kauselmann G., Bundman M., Kuhl D.;
RT   "Arg3.1/Arc mRNA induction by Ca2+ and cAMP requires protein kinase A
RT   and mitogen-activated protein kinase/extracellular regulated kinase
RT   activation.";
RL   J. Neurosci. 21:5484-5493(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Forebrain;
RA   Chowdhury S., Lanahan A.A., Worley P.F.;
RT   "The mArc gene, a mouse homolog of rat Arc.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242.
RC   STRAIN=C57BL/6 X CBA;
RA   Medrano S., Worley P.F., Chowdhury S., Lanahan A., Steward O.,
RA   Scrable H.;
RT   "Characterization of the promoter region of the immediate early gene
RT   Arc.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12493697; DOI=10.1095/biolreprod.102.004143;
RA   Maier B., Medrano S., Sleight S.B., Visconti P.E., Scrable H.;
RT   "Developmental association of the synaptic activity-regulated protein
RT   arc with the mouse acrosomal organelle and the sperm tail.";
RL   Biol. Reprod. 68:67-76(2003).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17088210; DOI=10.1016/j.neuron.2006.08.024;
RA   Plath N., Ohana O., Dammermann B., Errington M.L., Schmitz D.,
RA   Gross C., Mao X., Engelsberg A., Mahlke C., Welzl H., Kobalz U.,
RA   Stawrakakis A., Fernandez E., Waltereit R., Bick-Sander A.,
RA   Therstappen E., Cooke S.F., Blanquet V., Wurst W., Salmen B.,
RA   Bosl M.R., Lipp H.P., Grant S.G., Bliss T.V., Wolfer D.P., Kuhl D.;
RT   "Arc/Arg3.1 is essential for the consolidation of synaptic plasticity
RT   and memories.";
RL   Neuron 52:437-444(2006).
RN   [8]
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).
CC   -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. Required in the stress fiber dynamics
CC       and cell migration (By similarity). Required for consolidation of
CC       synaptic plasticity as well as formation of long-term memory.
CC       Regulates endocytosis of AMPA receptors in response to synaptic
CC       activity. Required for homeostatic synaptic scaling of AMPA
CC       receptors.
CC   -!- SUBUNIT: Interacts with SH3GL1/endophilin-2, SH3GL3/endophilin-3
CC       and DNM2/DYN2 (By similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=3; IntAct=EBI-397779, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Endosome (By similarity). Cytoplasmic vesicle, secretory vesicle,
CC       acrosome. Cell junction, synapse, postsynaptic cell membrane,
CC       postsynaptic density (By similarity). Cell projection, dendrite
CC       (By similarity). Cell projection, dendritic spine (By similarity).
CC       Cell junction, synapse (By similarity). Note=Associated with the
CC       cell cortex of neuronal soma and dendrites. Enriched in
CC       postsynaptic density of dendritic spines. Enriched on the plasma
CC       membrane (By similarity). Associated with the sperm tail.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC   -!- DEVELOPMENTAL STAGE: Detectable in brain from postnatal week 1, in
CC       testis from postnatal week 3.
CC   -!- DISRUPTION PHENOTYPE: Mice show deficits in several forms of long-
CC       term memory formation including spatial and fear-related learning,
CC       conditioned taste aversion as well as long-term object
CC       recognition. They show enhanced early-phase but impaired late-
CC       phase long-term potentiation (LTP) as well as impaired long-term
CC       depression (LTD). Neurons lacking Arc show an increase in surface
CC       levels of AMPA receptors.
CC   -!- MISCELLANEOUS: Widely used as activity-dependent neuronal marker
CC       to identify recently activated neurons in behavioral studies.
CC   -!- SIMILARITY: Belongs to the ARC/ARG3.1 family.
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DR   EMBL; AF177701; AAK91587.1; -; Genomic_DNA.
DR   EMBL; AF162777; AAD43586.1; -; mRNA.
DR   EMBL; AK157822; BAE34212.1; -; mRNA.
DR   EMBL; AK170446; BAE41804.1; -; mRNA.
DR   EMBL; BC023127; AAH23127.1; -; mRNA.
DR   EMBL; AF254662; AAG10254.1; -; Genomic_DNA.
DR   IPI; IPI00125140; -.
DR   RefSeq; NP_061260.1; NM_018790.2.
DR   UniGene; Mm.25405; -.
DR   ProteinModelPortal; Q9WV31; -.
DR   IntAct; Q9WV31; 3.
DR   STRING; Q9WV31; -.
DR   PRIDE; Q9WV31; -.
DR   Ensembl; ENSMUST00000023268; ENSMUSP00000023268; ENSMUSG00000022602.
DR   Ensembl; ENSMUST00000110009; ENSMUSP00000105636; ENSMUSG00000022602.
DR   GeneID; 11838; -.
DR   KEGG; mmu:11838; -.
DR   UCSC; uc007wfn.1; mouse.
DR   CTD; 23237; -.
DR   MGI; MGI:88067; Arc.
DR   eggNOG; maNOG11459; -.
DR   GeneTree; ENSGT00390000003914; -.
DR   HOGENOM; HBG269748; -.
DR   HOVERGEN; HBG080862; -.
DR   InParanoid; Q9WV31; -.
DR   OMA; RCQETIA; -.
DR   OrthoDB; EOG49S66B; -.
DR   PhylomeDB; Q9WV31; -.
DR   NextBio; 279775; -.
DR   ArrayExpress; Q9WV31; -.
DR   Bgee; Q9WV31; -.
DR   Genevestigator; Q9WV31; -.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; TAS:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
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; IMP:MGI.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR023263; Activity-reg_cytoskelet-assoc.
DR   PRINTS; PR02027; ARCARG31.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cell projection; Coiled coil;
KW   Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Developmental protein; Endocytosis; Endosome; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Synapse.
FT   CHAIN         1    396       Activity-regulated cytoskeleton-
FT                                associated protein.
FT                                /FTId=PRO_0000273286.
FT   REGION       89    100       Binds SH3GL1 or SH3GL3 (By similarity).
FT   REGION      195    214       Required for binding DNM2 (By
FT                                similarity).
FT   COILED       54     78       Potential.
SQ   SEQUENCE   396 AA;  45321 MW;  F4D3505FD477D18A CRC64;
     MELDHMTTGG LHAYPAPRGG PAAKPNVILQ IGKCRAEMLE HVRRTHRHLL TEVSKQVERE
     LKGLHRSVGK LENNLDGYVP TGDSQRWKKS IKACLCRCQE TIANLERWVK REMHVWREVF
     YRLERWADRL ESMGGKYPVG SEPARHTVSV GVGGPEPYCQ EADGYDYTVS PYAITPPPAA
     GELPEQESVE AQQYQSWGPG EDGQPSPGVD TQIFEDPREF LSHLEEYLRQ VGGSEEYWLS
     QIQNHMNGPA KKWWEFKQGS VKNWVEFKKE FLQYSEGTLS REAIQRELEL PQKQGEPLDQ
     FLWRKRDLYQ TLYVDAEEEE IIQYVVGTLQ PKLKRFLRHP LPKTLEQLIQ RGMEVQDGLE
     QAAEPSGTPL PTEDETEALT PALTSESVAS DRTQPE
//