ARP8_YEAST
ID ARP8_YEAST Reviewed; 881 AA.
AC Q12386; D6W2J7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Actin-like protein ARP8;
GN Name=ARP8; OrderedLocusNames=YOR141C; ORFNames=YOR3348C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP GENE NAME.
RX PubMed=9290209;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1053::aid-yea164>3.0.co;2-4;
RA Poch O., Winsor B.;
RT "Who's who among the Saccharomyces cerevisiae actin-related proteins? A
RT classification and nomenclature proposal for a large family.";
RL Yeast 13:1053-1058(1997).
RN [5]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8;
RA Shen X., Ranallo R., Choi E., Wu C.;
RT "Involvement of actin-related proteins in ATP-dependent chromatin
RT remodeling.";
RL Mol. Cell 12:147-155(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 248-881, ELECTRON MICROSCOPY,
RP FUNCTION, AND SUBUNIT.
RX PubMed=23213201; DOI=10.1073/pnas.1214735109;
RA Saravanan M., Wuerges J., Bose D., McCormack E.A., Cook N.J., Zhang X.,
RA Wigley D.B.;
RT "Interactions between the nucleosome histone core and Arp8 in the INO80
RT chromatin remodeling complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20883-20888(2012).
CC -!- FUNCTION: Probably involved in transcription regulation via its
CC interaction with the INO80 complex, a chromatin remodeling complex.
CC Exhibits low basal ATPase activity, and unable to polymerize. Strongly
CC prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting
CC it may act as a nucleosome recognition module within the complex.
CC {ECO:0000269|PubMed:23213201}.
CC -!- SUBUNIT: Component of the chromatin-remodeling INO80 complex, at least
CC composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3,
CC IES4, IES6, ACT1, IES2, IES5 and INO80. Exists as monomers and dimers,
CC but the dimer is most probably the biologically relevant form required
CC for stable interactions with histones that exploits the twofold
CC symmetry of the nucleosome core (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q12386; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-2967, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton.
CC -!- MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X94335; CAA64058.1; -; Genomic_DNA.
DR EMBL; Z75049; CAA99341.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10913.1; -; Genomic_DNA.
DR PIR; S67026; S67026.
DR RefSeq; NP_014784.1; NM_001183560.1.
DR PDB; 4AM6; X-ray; 2.70 A; A/B=248-881.
DR PDB; 4AM7; X-ray; 3.25 A; A/B=248-881.
DR PDB; 5NBN; X-ray; 4.00 A; E/F=255-881.
DR PDBsum; 4AM6; -.
DR PDBsum; 4AM7; -.
DR PDBsum; 5NBN; -.
DR AlphaFoldDB; Q12386; -.
DR SMR; Q12386; -.
DR BioGRID; 34535; 497.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR DIP; DIP-6706N; -.
DR IntAct; Q12386; 31.
DR MINT; Q12386; -.
DR STRING; 4932.YOR141C; -.
DR iPTMnet; Q12386; -.
DR MaxQB; Q12386; -.
DR PaxDb; Q12386; -.
DR PRIDE; Q12386; -.
DR EnsemblFungi; YOR141C_mRNA; YOR141C; YOR141C.
DR GeneID; 854309; -.
DR KEGG; sce:YOR141C; -.
DR SGD; S000005667; ARP8.
DR VEuPathDB; FungiDB:YOR141C; -.
DR eggNOG; KOG0797; Eukaryota.
DR GeneTree; ENSGT00390000001763; -.
DR HOGENOM; CLU_006974_0_1_1; -.
DR InParanoid; Q12386; -.
DR OMA; CFIQESL; -.
DR BioCyc; YEAST:G3O-33662-MON; -.
DR PRO; PR:Q12386; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12386; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031011; C:Ino80 complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR027668; Arp8/plant_Arp9.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF13; PTHR11937:SF13; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..881
FT /note="Actin-like protein ARP8"
FT /id="PRO_0000089128"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 502..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 321..341
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4AM7"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 386..390
FT /evidence="ECO:0007829|PDB:4AM6"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 418..433
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 484..491
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 530..543
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 556..569
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 593..602
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 603..609
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 615..619
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:4AM6"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 668..686
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 703..716
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 720..722
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 730..734
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 735..738
FT /evidence="ECO:0007829|PDB:4AM7"
FT HELIX 742..753
FT /evidence="ECO:0007829|PDB:4AM6"
FT TURN 757..759
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 763..778
FT /evidence="ECO:0007829|PDB:4AM6"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:4AM6"
FT TURN 793..797
FT /evidence="ECO:0007829|PDB:4AM7"
FT HELIX 798..817
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 838..840
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 841..849
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 853..858
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 862..868
FT /evidence="ECO:0007829|PDB:4AM6"
FT HELIX 869..874
FT /evidence="ECO:0007829|PDB:4AM6"
SQ SEQUENCE 881 AA; 100209 MW; 8174851B6B077A19 CRC64;
MSQEEAESSI IYEEPIDIPL EDDDDEDELE EENSVPLSSQ ADQENAENES DDSVDNVVGS
ETPRSVTGLS VDPRDVADEE DEDEEGEDED EDEDDNDVDN EDENDNDNAN ENENELGSSR
DKRAPPAVQT SKRYKKYPKL DPAKAPPGKK VPLHLLEKRR LGRIKAAEEF AKTLKKIGIE
KVETTTLPAT GLFQPLMLIN QKNYSSDYLK KDDQIFALRD RKFLRNNNTS QISSTNTPDV
IDLKSLPHSE ASAAPLNDEI DLNDPTATIV IHPGSNSIKI GFPKDDHPVV VPNCVAVPKK
WLDLENSEHV ENVCLQREQS EEFNNIKSEM EKNFRERMRY YKRKVPGNAH EQVVSFNENS
KPEIISEKND PSPIEWIFDD SKLYYGSDAL RCVDEKFVIR KPFRGGSFNV KSPYYKSLAE
LISDVTKLLE HALNSETLNV KPTKFNQYKV VLVIPDIFKK SHVETFIRVL LTELQFQAVA
IIQESLATCY GAGISTSTCV VNIGAAETRI ACVDEGTVLE HSAITLDYGG DDITRLFALF
LLQSDFPLQD WKIDSKHGWL LAERLKKNFT TFQDADVAVQ LYNFMNRSPN QPTEKYEFKL
FDEVMLAPLA LFFPQIFKLI RTSSHKNSSL EFQLPESRDL FTNELNDWNS LSQFESKEGN
LYCDLNDDLK ILNRILDAHN IIDQLQDKPE NYGNTLKENF APLEKAIVQS IANASITADV
TRMNSFYSNI LIVGGSSKIP ALDFILTDRI NIWRPSLLSS ASFPQFYKKL TKEIKDLEGH
YVNAPDKTED ENKQILQAQI KEKIVEELEE QHQNIEHQNG NEHIFPVSII PPPRDMNPAL
IIWKGASVLA QIKLVEELFI TNSDWDVHGS RILQYKCIFT Y
