ID M4AXZ2_XIPMA Unreviewed; 644 AA.
AC M4AXZ2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|ARBA:ARBA00021608, ECO:0000256|RuleBase:RU364121};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000019337.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000019337.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000019337.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in the functional organization of
CC mitotic chromosomes. Exhibits low basal ATPase activity, and unable to
CC polymerize. {ECO:0000256|ARBA:ARBA00025560,
CC ECO:0000256|RuleBase:RU364121}.
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. {ECO:0000256|RuleBase:RU364121}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the DBINO domain
CC of INO80. Exists as monomers and dimers, but the dimer is most probably
CC the biologically relevant form required for stable interactions with
CC histones that exploits the twofold symmetry of the nucleosome core.
CC {ECO:0000256|RuleBase:RU364121}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364121}.
CC Chromosome {ECO:0000256|RuleBase:RU364121}. Note=Specifically localizes
CC to mitotic chromosomes. {ECO:0000256|RuleBase:RU364121}.
CC -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00007720, ECO:0000256|RuleBase:RU364121}.
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DR RefSeq; XP_005800179.1; XM_005800122.1.
DR AlphaFoldDB; M4AXZ2; -.
DR STRING; 8083.ENSXMAP00000019337; -.
DR Ensembl; ENSXMAT00000019365.2; ENSXMAP00000019337.2; ENSXMAG00000019284.2.
DR GeneID; 102222685; -.
DR KEGG; xma:102222685; -.
DR CTD; 93973; -.
DR eggNOG; KOG0797; Eukaryota.
DR GeneTree; ENSGT00390000001763; -.
DR HOGENOM; CLU_006974_1_0_1; -.
DR InParanoid; M4AXZ2; -.
DR OMA; AYKCMWA; -.
DR OrthoDB; 11729at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 3.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF13; ACTIN-RELATED PROTEIN 8; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364121};
KW DNA damage {ECO:0000256|RuleBase:RU364121};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU364121}; DNA repair {ECO:0000256|RuleBase:RU364121};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364121};
KW Nucleus {ECO:0000256|RuleBase:RU364121};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 72023 MW; DA2C9658ADCE460D CRC64;
MTQAEKEQDS GKEKEKERDK EKEKEQQRGV KRPIAPAAIP EAAQEQIQSN FVIVIHPGSR
TLRIGRATDT LPVIIPHVIA RRHKQGGQAR HEDAWLLRDG LNKAESSEQR QNGLKMVDQA
IWSKKMSNGV RRTPVSAEQA RAYNCQIRPA VLDSSSRVKW TNTSHHPNYL VGEEALYVNP
SDCYNLHWPV IRGQLNVHSG SGGSLTAVLA DLETLWSYVI QKHLEIPLKE LKYYRCILLV
PDIYNRQHVK EIVNILLHNM GFSAIIAHQE SVCATFGSGL SSACVVDVGD QKTSICCVED
GVSHRNSRLC LAYGGSDVTR TFFWLLQRAG FPYRDCQLTN RLDCQLLQHL KETFCHLDQD
ISGLQDHEFQ TRFPEAPALL YQIRLGDEKL QAPMGLFYPS TFGIVGQKMT SLQHRSQGNS
EDPHDEHYLL STQSKGEQSS KSAAERKAVS RPGGGLDGDL NCQGRMGEMS DMPRGCGSGS
AAGGGMLGEM ELGPNQGECL MSPGEAEESL STHLSRKTAI ISQFESKALG LDKAILHSID
CCASDETKRK MYSSILVVGG GLMFHGAQEF LLHRIINKMP PSFRRLVDNV EVITRPKDMD
PRLISWKGGA VLACLDTTQE MWIHQREWQR FGVRMLRERA AFVW
//
