ARP6_MOUSE
ID ARP6_MOUSE Reviewed; 396 AA.
AC Q9D864; Q8BTV8;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Actin-related protein 6;
DE Short=mArp6;
GN Name=Actr6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Small intestine, and Thymus;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Required for formation and/or maintenance of the proper
CC nucleolar structure and function (By similarity). Plays a dual role in
CC the regulation of ribosomal DNA (rDNA) transcription (By similarity).
CC In the presence of high glucose, it maintains active rDNA transcription
CC through H2A.Z deposition and under glucose starvation, is required for
CC the repression of rDNA transcription, and this function may be
CC independent of H2A.Z (By similarity). {ECO:0000250|UniProtKB:Q9DEE9,
CC ECO:0000250|UniProtKB:Q9GZN1}.
CC -!- SUBUNIT: Interacts with CBX1, CBX3 and CBX5.
CC {ECO:0000250|UniProtKB:Q9GZN1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P45890}. Nucleus {ECO:0000250|UniProtKB:Q9GZN1}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9GZN1}. Note=Colocalizes
CC with HP1 family proteins at pericentric heterochromatin.
CC {ECO:0000250|UniProtKB:Q9GZN1}.
CC -!- SIMILARITY: Belongs to the actin family. ARP6 subfamily. {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; AK008409; BAB25654.1; -; mRNA.
DR EMBL; AK088571; BAC40429.1; -; mRNA.
DR EMBL; BC062137; AAH62137.1; -; mRNA.
DR CCDS; CCDS24118.1; -.
DR RefSeq; NP_080190.1; NM_025914.2.
DR AlphaFoldDB; Q9D864; -.
DR SMR; Q9D864; -.
DR BioGRID; 211880; 1.
DR ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR IntAct; Q9D864; 1.
DR STRING; 10090.ENSMUSP00000020109; -.
DR iPTMnet; Q9D864; -.
DR PhosphoSitePlus; Q9D864; -.
DR EPD; Q9D864; -.
DR MaxQB; Q9D864; -.
DR PaxDb; Q9D864; -.
DR PeptideAtlas; Q9D864; -.
DR PRIDE; Q9D864; -.
DR ProteomicsDB; 281802; -.
DR DNASU; 67019; -.
DR GeneID; 67019; -.
DR KEGG; mmu:67019; -.
DR UCSC; uc007gss.1; mouse.
DR CTD; 64431; -.
DR MGI; MGI:1914269; Actr6.
DR eggNOG; KOG0680; Eukaryota.
DR InParanoid; Q9D864; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q9D864; -.
DR TreeFam; TF105780; -.
DR BioGRID-ORCS; 67019; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Actr6; mouse.
DR PRO; PR:Q9D864; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D864; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0007000; P:nucleolus organization; ISS:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR030054; Arp6.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF47; PTHR11937:SF47; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9GZN1"
FT CHAIN 2..396
FT /note="Actin-related protein 6"
FT /id="PRO_0000089106"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZN1"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 26
FT /note="P -> T (in Ref. 1; BAC40429)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> F (in Ref. 1; BAB25654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45785 MW; 550B68A2CBEAC82C CRC64;
MTTLVLDNGA YNAKIGYSHD SVSVIPNCQF RSKTARLKTF TANQIDEIKD PSGLFYILPF
QKGYLVNWDV QRQVWDYLFG KEMYQVDFLD TNIIITEPYF NFTSIQESMN EILFEEYQFQ
AVLRVNAGAL SAHRYFRDNP SELCCIIVDS GYSFTHIVPY CRSKKKKEAI IRINVGGKLL
TNHLKEIISY RQLHVMDETH VINQVKEDVC YVSQDFYRDM DIAKLKGEDN TVMIDYVLPD
FSTIKKGFCK PREEMVLSGK YKSGEQILRL ANERFAVPEI LFNPSDIGIQ EMGIPEAIVY
SIQNLPEEMQ PHFFKNIVLT GGNSLFPGFR ERVYSEVRCL TPTDYDVSVV LPENPITYSW
EGGKLISEND DFEDMVVTRE DYEENGHSVC EEKFDI
