FIGL1_MOUSE
ID FIGL1_MOUSE Reviewed; 683 AA.
AC Q8BPY9; Q3UF48; Q8C2I6; Q9ERZ5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Fidgetin-like protein 1;
DE EC=3.6.4.-;
GN Name=Fignl1;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11017077; DOI=10.1038/79923;
RA Cox G.A., Mahaffey C.L., Nystuen A., Letts V.A., Frankel W.N.;
RT "The mouse fidgetin gene defines a new role for AAA family proteins in
RT mammalian development.";
RL Nat. Genet. 26:198-202(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Eye, Spleen, Sympathetic ganglion, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [5]
RP FUNCTION.
RX PubMed=17352653; DOI=10.1359/jbmr.070311;
RA Park S.J., Kim S.J., Rhee Y., Byun J.H., Kim S.H., Kim M.H., Lee E.J.,
RA Lim S.K.;
RT "Fidgetin-like 1 gene inhibited by basic fibroblast growth factor regulates
RT the proliferation and differentiation of osteoblasts.";
RL J. Bone Miner. Res. 22:889-896(2007).
RN [6]
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).
RN [7]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=22110678; DOI=10.1371/journal.pone.0027582;
RA L'Hote D., Vatin M., Auer J., Castille J., Passet B., Montagutelli X.,
RA Serres C., Vaiman D.;
RT "Fidgetin-like1 is a strong candidate for a dynamic impairment of male
RT meiosis leading to reduced testis weight in mice.";
RL PLoS ONE 6:E27582-E27582(2011).
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
CC (PubMed:17352653). May play a role in the control of male meiosis
CC dynamic (PubMed:22110678). {ECO:0000250|UniProtKB:Q6PIW4,
CC ECO:0000269|PubMed:17352653, ECO:0000269|PubMed:22110678}.
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:0000269|PubMed:22110678}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:22110678}. Note=Together with RAD51 and a subset of
CC H2A histone proteins, redistributed in discrete nuclear DNA damage-
CC induced foci after ionizing radiation (IR) treatment.
CC {ECO:0000250|UniProtKB:Q6PIW4}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in the testis
CC (PubMed:22110678). Detected in pachytene spermatocytes and in metaphase
CC spermatocytes (at protein level). {ECO:0000269|PubMed:22110678}.
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; AF263914; AAG17290.1; -; mRNA.
DR EMBL; AK088574; BAC40431.1; -; mRNA.
DR EMBL; AK051874; BAC34796.1; -; mRNA.
DR EMBL; AK143850; BAE25569.1; -; mRNA.
DR EMBL; AK148994; BAE28713.1; -; mRNA.
DR EMBL; AL596450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051942; AAH51942.1; -; mRNA.
DR EMBL; BC052415; AAH52415.1; -; mRNA.
DR CCDS; CCDS24438.1; -.
DR RefSeq; NP_001156831.1; NM_001163359.1.
DR RefSeq; NP_001156832.1; NM_001163360.1.
DR RefSeq; NP_068691.2; NM_021891.3.
DR RefSeq; XP_011242040.1; XM_011243738.2.
DR AlphaFoldDB; Q8BPY9; -.
DR SMR; Q8BPY9; -.
DR BioGRID; 208599; 1.
DR STRING; 10090.ENSMUSP00000126340; -.
DR iPTMnet; Q8BPY9; -.
DR PhosphoSitePlus; Q8BPY9; -.
DR EPD; Q8BPY9; -.
DR jPOST; Q8BPY9; -.
DR MaxQB; Q8BPY9; -.
DR PaxDb; Q8BPY9; -.
DR PeptideAtlas; Q8BPY9; -.
DR PRIDE; Q8BPY9; -.
DR ProteomicsDB; 267585; -.
DR Antibodypedia; 27700; 149 antibodies from 26 providers.
DR DNASU; 60530; -.
DR Ensembl; ENSMUST00000047689; ENSMUSP00000036932; ENSMUSG00000035455.
DR Ensembl; ENSMUST00000109664; ENSMUSP00000105290; ENSMUSG00000035455.
DR Ensembl; ENSMUST00000171080; ENSMUSP00000127489; ENSMUSG00000035455.
DR Ensembl; ENSMUST00000171938; ENSMUSP00000126340; ENSMUSG00000035455.
DR GeneID; 60530; -.
DR KEGG; mmu:60530; -.
DR UCSC; uc007ias.2; mouse.
DR CTD; 63979; -.
DR MGI; MGI:1890648; Fignl1.
DR VEuPathDB; HostDB:ENSMUSG00000035455; -.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000161552; -.
DR HOGENOM; CLU_000688_21_10_1; -.
DR InParanoid; Q8BPY9; -.
DR OMA; YSDKWES; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q8BPY9; -.
DR TreeFam; TF105013; -.
DR BioGRID-ORCS; 60530; 23 hits in 114 CRISPR screens.
DR ChiTaRS; Fignl1; mouse.
DR PRO; PR:Q8BPY9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BPY9; protein.
DR Bgee; ENSMUSG00000035455; Expressed in spermatocyte and 178 other tissues.
DR ExpressionAtlas; Q8BPY9; baseline and differential.
DR Genevisible; Q8BPY9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA: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; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0033687; P:osteoblast proliferation; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP: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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..683
FT /note="Fidgetin-like protein 1"
FT /id="PRO_0000302724"
FT REGION 279..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 453..458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT CONFLICT 386
FT /note="K -> R (in Ref. 2; BAC40431)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> V (in Ref. 1; AAG17290)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="T -> A (in Ref. 2; BAC40431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 74850 MW; 17DE9C0738344F4C CRC64;
METSSSMSVE TTRSVQVDEW QKNYCVVTSS ICTPKQKADA YRALLLHIQY AYANSEISQV
FATNLFKRYT EKYSAIIDSD NVVTGLNNYA ESIFALAGSR QADSNKWQSG LSIDNVFKMS
CVQEMMQAGK KFEESLLEPA DASVVLCKEP TAFEVPQLSV CGGSEDADIL SSSGHDTDKT
QAIPGSSLRC SPFQSARLPK ETNTTKTCLT SSTSLGESAT AAFHMTPLFG NTEKDTQSFP
KTSTGLNMFL SNLSCVPSGC ENPQERKAFN DSDIIDILSN PTLNKAPSKT EDRGRREDNS
LPTFKTAKEQ LWVDQKKKGH QSQHTSKSSN GVMKKSLGAG RSRGIFGKFV PPVSNKQDGS
EQHAKKHKSS RAGSAEPAHL TDDCLKNVEP RMVELIMNEI MDHGPPVHWD DIAGVEFAKA
TIKEIVVWPM MRPDIFTGLR GPPKGILLFG PPGTGKTLIG KCIASQSGAT FFSISASSLT
SKWVGEGEKM VRALFAVARC QQPAVIFIDE IDSLLSQRGD GEHESSRRIK TEFLVQLDGA
TTSSEDRILV VGATNRPQEI DEAARRRLVK RLYIPLPEAS ARKQIVGNLM SKEQCCLSDE
ETDLVVQQSD GFSGADMTQL CREASLGPIR SLHAADIATI SPDQVRPIAY IDFENAFKTV
RPTVSPKDLE LYENWNETFG CGK
