ARP5_MOUSE
ID ARP5_MOUSE Reviewed; 605 AA.
AC Q80US4; A2ACC9; Q8BL26;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Actin-related protein 5;
GN Name=Actr5;
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Lung;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. Involved in DNA double-strand
CC break repair and UV-damage excision repair (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the helicase ATP-
CC binding domain and helicase C-terminal of INO80. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H9F9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80US4-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q80US4-3; Sequence=VSP_020073, VSP_020074;
CC -!- SIMILARITY: Belongs to the actin family. ARP5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK142980; Type=Frameshift; Evidence={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; AK046584; BAC32796.1; -; mRNA.
DR EMBL; AK142980; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL663091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q80US4; -.
DR SMR; Q80US4; -.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR IntAct; Q80US4; 2.
DR MINT; Q80US4; -.
DR STRING; 10090.ENSMUSP00000046658; -.
DR PhosphoSitePlus; Q80US4; -.
DR EPD; Q80US4; -.
DR MaxQB; Q80US4; -.
DR PaxDb; Q80US4; -.
DR PeptideAtlas; Q80US4; -.
DR PRIDE; Q80US4; -.
DR ProteomicsDB; 282025; -. [Q80US4-1]
DR ProteomicsDB; 282026; -. [Q80US4-3]
DR UCSC; uc008nql.1; mouse. [Q80US4-3]
DR MGI; MGI:1924748; Actr5.
DR eggNOG; KOG0681; Eukaryota.
DR InParanoid; Q80US4; -.
DR TreeFam; TF324227; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR ChiTaRS; Actr5; mouse.
DR PRO; PR:Q80US4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80US4; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR GO; GO:0070914; P:UV-damage excision repair; ISO:MGI.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR027664; Arp5.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 2.
DR PANTHER; PTHR11937:SF16; PTHR11937:SF16; 2.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..605
FT /note="Actin-related protein 5"
FT /id="PRO_0000247843"
FT REGION 581..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 287..328
FT /evidence="ECO:0000255"
FT COILED 355..384
FT /evidence="ECO:0000255"
FT COMPBIAS 584..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9F9"
FT VAR_SEQ 259..266
FT /note="ELQKWQCP -> GDTGGHGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020073"
FT VAR_SEQ 267..605
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020074"
SQ SEQUENCE 605 AA; 67845 MW; 7CABECB3ADF731A9 CRC64;
MEANVFRFRD ARSAPDPVLE AGPVAFGSQP VPLVLDNGSF QARAGWACPG PDPGPEPRLQ
FRAVCARGRG GARGGPGPQV GNALGSLEPL RWMLRSPFDR NVPVNLELQE LLLDYSFQHL
GVSSQGCVDH PIVLTEAVCN PLYSRQMMSE LLFECYRIPK VAYGIDSLFS FYHNVPKNAL
SSGLIISSGY QCTHILPVLE GRLDAKNCKR INLGGSQAAG YLQRLLQLKY PGHLAAITLS
RMEEILQEHS YIAEDYGAEL QKWQCPDYYE NNVHKMQLPF SSKLLGSTLT AEEKQERRQQ
QLRRLQELNA RRREEKLQLD QERLERLLYV QELLEEGQMD QFHKALIELN MDSPEELQSY
IQKLTLAVEQ AKQKILQAEA SLEVDVVDSK PETPDLEPLE PTMEDVENIS DFEPLFSEET
PEVEKPQVTT VQPVFNLAAY HQLSVGTERI RAPEIIFQPS LIGEEQAGIA ETLHFVLDRY
PKAIQDTLVQ NVFLTGGNVM YPGMKARVEK ELLEMRPFQS SFQVQLASNP VLDAWYGARD
WALDHLEDSG AWVTRKDYEE KGGEYLKEHC ASNTYVPIRL PKQASRASET QTSGRGSSAS
GSGAG
