FIGL1_RAT
ID FIGL1_RAT Reviewed; 677 AA.
AC Q6GX84;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Fidgetin-like protein 1;
DE EC=3.6.4.-;
GN Name=Fignl1; Synonyms=S30;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=16288221; DOI=10.1038/sj.onc.1209210;
RA Iwanaga R., Komori H., Ishida S., Okamura N., Nakayama K., Nakayama K.,
RA Ohtani K.;
RT "Identification of novel E2F1 target genes regulated in cell cycle-
RT dependent and independent manners.";
RL Oncogene 25:1786-1798(2006).
CC -!- FUNCTION: Involved in DNA double-strand break (DBS) repair via
CC homologous recombination (HR). Recruited at DSB sites independently of
CC BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May
CC regulate osteoblast proliferation and differentiation (By similarity).
CC May play a role in the control of male meiosis dynamic (By similarity).
CC {ECO:0000250|UniProtKB:Q6PIW4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Hexamer. Interacts (via N-terminal one-half region) with
CC RAD51; the interaction is direct. Interacts (via N-terminal one-half
CC region) with SPIDR (via the C-terminal region); the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8BPY9}. Note=Together with RAD51 and a subset
CC of H2A histone proteins, redistributed in discrete nuclear DNA damage-
CC induced foci after ionizing radiation (IR) treatment.
CC {ECO:0000250|UniProtKB:Q6PIW4}.
CC -!- INDUCTION: By E2F1 and serum stimulation.
CC {ECO:0000269|PubMed:16288221}.
CC -!- DOMAIN: The N-terminus is necessary for its recruitment to DNA damage
CC sites. {ECO:0000250|UniProtKB:Q6PIW4}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AY623031; AAT46048.1; -; mRNA.
DR EMBL; AY623032; AAT46049.1; -; mRNA.
DR RefSeq; NP_001011913.1; NM_001011913.1.
DR RefSeq; XP_006251538.1; XM_006251476.2.
DR RefSeq; XP_006251539.1; XM_006251477.3.
DR RefSeq; XP_008768483.1; XM_008770261.2.
DR AlphaFoldDB; Q6GX84; -.
DR SMR; Q6GX84; -.
DR STRING; 10116.ENSRNOP00000005857; -.
DR PaxDb; Q6GX84; -.
DR PRIDE; Q6GX84; -.
DR Ensembl; ENSRNOT00000005857; ENSRNOP00000005857; ENSRNOG00000004440.
DR Ensembl; ENSRNOT00000107994; ENSRNOP00000078689; ENSRNOG00000004440.
DR GeneID; 289777; -.
DR KEGG; rno:289777; -.
DR UCSC; RGD:1307112; rat.
DR CTD; 63979; -.
DR RGD; 1307112; Fignl1.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000161552; -.
DR HOGENOM; CLU_000688_21_10_1; -.
DR InParanoid; Q6GX84; -.
DR OMA; YSDKWES; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q6GX84; -.
DR TreeFam; TF105013; -.
DR PRO; PR:Q6GX84; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000004440; Expressed in thymus and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033687; P:osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Hydrolase; Isopeptide bond; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..677
FT /note="Fidgetin-like protein 1"
FT /id="PRO_0000302725"
FT REGION 203..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 447..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT MOD_RES 341
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
SQ SEQUENCE 677 AA; 74197 MW; 189C08E1509BF4F2 CRC64;
METSSSRSVQ VDDWQKNYSV VASSICTPKQ KADAYRALLL HIQDAYANSE ISQVFATNLF
KRYTEKYSAI IDSDNVVTGL NNYAESIFAL AGSQQADSDK WQSGLSINNV FKMSTVQEMM
QAGQKFKESL LEPADASVVM CKEPTIFEVP QLGVCGGSEE ADLLSSSVHG TEKTQAIPGN
SLRCSPFQST LFPMATNTKT CLTSSAPSGE STTATFHRTP LFGNTKKEPQ SFPKTSTGLN
MFLSNPSCVP SGCENPRERK AFNDSDTINM LSNPTLNKAP SKTEDSGQRE DNSLPTFKTA
KEQLWADQKK RSHQSQHTSK SFNGAIKKSL GAGRSRGIFG KFVPPVSNKQ DGSEQNGNVK
PKSSRAGSAE PAHLTDDRLK NVEPRMVELI MNEIMDHGPP VHWEDIAGVE FAKATIKEIV
VWPMMRPDIF TGLRGPPKGI LLFGPPGTGK TLIGKCIASQ SGATFFSISA SSLTSKWVGE
GEKMVRALFA VARCQQPAVI FIDEIDSLLS QRGDGEHESS RRIKTEFLVQ LDGATTSSED
RILVVGATNR PQEIDEAARR RLVKRLYIPL PEASARKQIV VNLMSKEQCC LTDEETELVV
QQSDGFSGAD MTQLCREASL GPIRSLHTAD IATISPDQVR PIAYIDFENA FRTVRPSVSP
KDLELYENWN KTFGCGK
