FIGN_MOUSE
ID FIGN_MOUSE Reviewed; 759 AA.
AC Q9ERZ6; Q3TPB0; Q3UP57; Q6PCM0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fidgetin;
GN Name=Fign;
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] (ISOFORMS 1 AND 2), DISEASE, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=EL/Suz;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Heart, and Spleen;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH AKAP8, AND DISRUPTION PHENOTYPE.
RX PubMed=16751186; DOI=10.1074/jbc.m603626200;
RA Yang Y., Mahaffey C.L., Berube N., Frankel W.N.;
RT "Interaction between fidgetin and protein kinase A-anchoring protein AKAP95
RT is critical for palatogenesis in the mouse.";
RL J. Biol. Chem. 281:22352-22359(2006).
CC -!- FUNCTION: ATP-dependent microtubule severing protein. Severs
CC microtubules along their length and depolymerizes their ends, primarily
CC the minus-end, suppressing microtubule growth from and attachment to
CC centrosomes. Microtubule severing may promote rapid reorganization of
CC cellular microtubule arrays and the release of microtubules from the
CC centrosome following nucleation. Microtubule release from the mitotic
CC spindle poles may allow depolymerization of the microtubule end
CC proximal to the spindle pole, leading to poleward microtubule flux and
CC poleward motion of chromosome (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AKAP8 (via C-terminus).
CC {ECO:0000269|PubMed:16751186}.
CC -!- INTERACTION:
CC Q9ERZ6; Q9DBR0: Akap8; NbExp=4; IntAct=EBI-11111349, EBI-4285802;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16751186}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Note=Localizes to centrosomes throughout mitosis and to
CC the spindle midzone during telophase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERZ6-2; Sequence=VSP_020731;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11017077}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the embryo at 8.5 dpc.
CC Oocyst, optic cup and pelvic anlage show strongest expression. At 10.5
CC dpc, expression concentrated in epithelial cells of the dorso-lateral,
CC posterior and anterior otocyst wall. Expression in the eye is found
CC fairly evenly throughout the retinal neural epithelium, with some
CC enrichment in the inner retina where cells begin their differentiation
CC to form retinal ganglion cells. Some expression is seen in the lens pit
CC and in the cell layer that will become the pigment epithelium. At 11.5
CC dpc, when the superior semicircular canal has begun to form from the
CC posterior otocyst, much of the expression is concentrated there,
CC although there is also expression in the part of the otocyst that will
CC form the lateral or horizontal canal. Strong expression was also seen
CC in the acoustic ganglia and cochlea. In the eye the expression pattern
CC is similar to that found in 10.5 dpc except that expression is
CC concentrated in the retinal ganglion layer. As the lens vesicle forms
CC and matures at 13 dpc, expression is also seen in the anterior wall of
CC the lens, but persists throughout the neural retina, especially in the
CC peripheral retina where cells are still differentiating.
CC {ECO:0000269|PubMed:11017077}.
CC -!- DISEASE: Note=Defects in Fign are characterized by a side-to-side head-
CC shaking and circling behavior, due to reduced or absent semicircular
CC canals. Diseased mice also have small eyes, associated with cell-cycle
CC delay and insufficient growth of the retinal neural epithelium, and
CC lower penetrance skeletal abnormalities, including pelvic girdle
CC dysgenesis, skull bone fusions and polydactyly.
CC {ECO:0000269|PubMed:11017077}.
CC -!- DISRUPTION PHENOTYPE: FIGN and AKAP8 double mutant mice die soon after
CC birth due to cleft palate. {ECO:0000269|PubMed:16751186}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF263913; AAG17289.1; -; mRNA.
DR EMBL; AK143787; BAE25540.1; -; mRNA.
DR EMBL; AK163474; BAE37359.1; -; mRNA.
DR EMBL; AK164536; BAE37827.1; -; mRNA.
DR EMBL; BC059266; AAH59266.1; -; mRNA.
DR CCDS; CCDS16070.1; -. [Q9ERZ6-1]
DR RefSeq; NP_001254775.1; NM_001267846.1. [Q9ERZ6-2]
DR RefSeq; NP_001254776.1; NM_001267847.1. [Q9ERZ6-2]
DR RefSeq; NP_068362.1; NM_021716.5. [Q9ERZ6-1]
DR AlphaFoldDB; Q9ERZ6; -.
DR SMR; Q9ERZ6; -.
DR BioGRID; 208552; 7.
DR IntAct; Q9ERZ6; 8.
DR STRING; 10090.ENSMUSP00000122855; -.
DR iPTMnet; Q9ERZ6; -.
DR PhosphoSitePlus; Q9ERZ6; -.
DR PaxDb; Q9ERZ6; -.
DR PRIDE; Q9ERZ6; -.
DR ProteomicsDB; 267586; -. [Q9ERZ6-1]
DR ProteomicsDB; 267587; -. [Q9ERZ6-2]
DR Antibodypedia; 47964; 137 antibodies from 18 providers.
DR DNASU; 60344; -.
DR Ensembl; ENSMUST00000131615; ENSMUSP00000122855; ENSMUSG00000075324. [Q9ERZ6-1]
DR GeneID; 60344; -.
DR KEGG; mmu:60344; -.
DR UCSC; uc008jvv.3; mouse. [Q9ERZ6-1]
DR CTD; 55137; -.
DR MGI; MGI:1890647; Fign.
DR VEuPathDB; HostDB:ENSMUSG00000075324; -.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000157526; -.
DR HOGENOM; CLU_000688_21_10_1; -.
DR InParanoid; Q9ERZ6; -.
DR OMA; GNFSYNQ; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q9ERZ6; -.
DR TreeFam; TF105015; -.
DR BioGRID-ORCS; 60344; 2 hits in 110 CRISPR screens.
DR ChiTaRS; Fign; mouse.
DR PRO; PR:Q9ERZ6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ERZ6; protein.
DR Bgee; ENSMUSG00000075324; Expressed in optic fissure and 186 other tissues.
DR ExpressionAtlas; Q9ERZ6; baseline and differential.
DR Genevisible; Q9ERZ6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; 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:0008568; F:microtubule severing ATPase activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 Alternative splicing; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..759
FT /note="Fidgetin"
FT /id="PRO_0000250749"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 529..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5HY92"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11017077,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020731"
FT CONFLICT 200..201
FT /note="SQ -> IP (in Ref. 3; AAH59266)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="A -> V (in Ref. 2; BAE25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="H -> R (in Ref. 2; BAE25540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 82098 MW; A139A1EFE47E12E9 CRC64;
MISSTSVYGL KMQWTPEHAQ WPEQHFDITS TTRSPAHKVE AYRGHLQRTY QYAWANDDIS
ALTASNLLKK YAEKYSGILE GPVDRPVLSN YSDTPSGLVN GRKNDSEPWQ PSLNSEAVYP
MNCVPDVITA SKAGVSSALP PVDVSASIGS SPGVASNLTE PSYSSSTCGS HTVPSLHAGL
PSQEYAPGYN GSYLHSTYSS QATPALPSPH PSPLHSSGLL QPPPPPPPPP ALVPGYNGTS
NLSSYSYPSA SYPPQTAVGS GYSPGGAPPP PSAYLPSGIP APTPLPPTTV PGYTYQGHGL
TPIAPSALTN NSASSLKRKA FYMAGQGDMD SSYGNYSYGQ QRSTQSPMYR MPDNSISNSN
RGNGFDRNAE TSSLAFKPTK QLMPSEQQRK FSSQSSRALT PPSYSTAKNS LGSRSSESFG
KYTSPVMSEH GDDHRQLLAH PIQGPGLRAA TSSNHSVDEQ LKNTDTHLID LVTNEIITQG
PPVDWSDIAG LDLVKAVIKE EVLWPVLRSD AFSGLTALPR SILLFGPRGT GKTLLGRCIA
SQLGATFFKI AGSGLVAKWI GEAEKIIHAS FLVARCRQPS VIFVSDIDML LSSQVSEEHS
PVSRMRTEFL MQLDTVLTSA EDQIVVICAT SKPEEIDESL RRYFMKRLLI PLPDSTARHQ
IIVQLLTQHN YCLNDKEFAL LVQRTEGFSG LDVAHLCQEA AVGPLHAMPA TDLSAIMPSQ
LRPVTYQDFE NAFCKIQPSI SQKELDMYVE WNKMFGCSQ
