FIGN_DANRE
ID FIGN_DANRE Reviewed; 736 AA.
AC Q503S1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Fidgetin;
GN Name=fign; ORFNames=zgc:110229;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes
CC to centrosomes throughout mitosis and to the spindle midzone during
CC telophase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; BC095207; AAH95207.1; -; mRNA.
DR RefSeq; NP_001018411.1; NM_001020575.1.
DR AlphaFoldDB; Q503S1; -.
DR SMR; Q503S1; -.
DR STRING; 7955.ENSDARP00000006334; -.
DR PaxDb; Q503S1; -.
DR GeneID; 553599; -.
DR KEGG; dre:553599; -.
DR CTD; 55137; -.
DR ZFIN; ZDB-GENE-050522-339; fign.
DR eggNOG; KOG0740; Eukaryota.
DR InParanoid; Q503S1; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q503S1; -.
DR PRO; PR:Q503S1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; IEA:UniProtKB-SubCell.
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: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; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..736
FT /note="Fidgetin"
FT /id="PRO_0000250750"
FT REGION 118..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 507..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
SQ SEQUENCE 736 AA; 79202 MW; ECB1AF5AC83C64AE CRC64;
MQWTPEHAQW AEQHFDISST TRSLAHKAEA YRGHLQRTYQ YAWANDDISA LTASNLLKKY
AEKYSGILEG PSERALLCSY SESAPGLLNG RKSESDAWQE GIYPMSCAAD VISASKTGMT
PALPPPDVTA SVGSSTGVAS SLSEPSYSSS NCGNHASALH SGIPSQEFAS SYNGSYLHST
YSGGQSTPAL PSPHPSPLHS AGLLQPPPPP PPTLVPSYNT SSPNLSSYNY PPAGYPPQTP
VAPGYSPGGA PPPSAYLPSG IAAPTPLPPS TIPGYSYQSH NHAPIAPTPL NGSSANTLKR
KAFYMTGQGD MDSSYGNFNY SQQRSAQSPM YRMPDNSLVD STRGNGFDRN ADTSSLAFKP
TKQSMPTDQQ RKFGSQAGRA LTPPSYGSSK GSLGSMRSGE SFGKFGSPVM SDHGDDSRQH
LPHSIDTATS SSHPAEEQLK NSDANLVEMV TTEILQQTSP VDWSDIAGLE MAKATIKDEV
LWPILRPDMF SGLATLPRSI LLFGPQGTGR TLLGRCMASQ LGAAFLLLSG SALVTKWLGE
GEKIVQASFL IARCRQPSVV FISDVDLLLS SQLSEESPVN RIKSELLLQL DGVLSSPEEH
VLVVCSTSKP EEIDESLRRY FVKRLLVPLP DATARHQIIS QLLSQHNYCL SDKEVTLLVQ
RTDGFSGLDV VRLCQEALVG PLHGMPGADL SGMIPGQMRP VSYQDFENVF CKIQPSISQK
ELDTYTEWNK MFGCSQ
