ID G3Q029_GASAC Unreviewed; 663 AA.
AC G3Q029;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 {ECO:0000256|HAMAP-Rule:MF_03022};
DE Short=Katanin p80 subunit B1 {ECO:0000256|HAMAP-Rule:MF_03022};
DE AltName: Full=p80 katanin {ECO:0000256|HAMAP-Rule:MF_03022};
GN Name=KATNB1 {ECO:0000256|HAMAP-Rule:MF_03022};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023219.2, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000023219.2, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000023219.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Participates in a complex which severs microtubules in an
CC ATP-dependent manner. May act to target the enzymatic subunit of this
CC complex to sites of action such as the centrosome. Microtubule severing
CC may promote rapid reorganization of cellular microtubule arrays and the
CC release of microtubules from the centrosome following nucleation.
CC {ECO:0000256|HAMAP-Rule:MF_03022}.
CC -!- SUBUNIT: Interacts with KATNA1. This interaction enhances the
CC microtubule binding and severing activity of KATNA1 and also targets
CC this activity to the centrosome. {ECO:0000256|HAMAP-Rule:MF_03022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03022}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton
CC {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|HAMAP-Rule:MF_03022}. Note=Predominantly cytoplasmic.
CC Localized to the interphase centrosome and mitotic spindle poles.
CC {ECO:0000256|HAMAP-Rule:MF_03022}.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03022}.
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DR AlphaFoldDB; G3Q029; -.
DR STRING; 69293.ENSGACP00000023219; -.
DR Ensembl; ENSGACT00000023264.2; ENSGACP00000023219.2; ENSGACG00000017570.2.
DR eggNOG; KOG0267; Eukaryota.
DR GeneTree; ENSGT00940000157918; -.
DR InParanoid; G3Q029; -.
DR OMA; TYADIPN; -.
DR TreeFam; TF332359; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000017570; Expressed in mesonephros and 13 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008352; C:katanin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR HAMAP; MF_03022; Katanin_p80_B1; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR028021; Katanin_C-terminal.
DR InterPro; IPR026962; KTNB1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19845; KATANIN P80 SUBUNIT; 1.
DR PANTHER; PTHR19845:SF0; KATANIN P80 WD40 REPEAT-CONTAINING SUBUNIT B1; 1.
DR Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_03022};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_03022};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03022};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP-
KW Rule:MF_03022}; Microtubule {ECO:0000256|HAMAP-Rule:MF_03022};
KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03022};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 16..58
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 59..100
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 101..142
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 143..184
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 185..226
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 501..659
FT /note="Katanin p80 subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13925"
FT REGION 323..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 72923 MW; 95B01F90737CFF90 CRC64;
MAVANTTKIS WRLQEFEAHS SSVSCLALGR SSGRLLATGG GDCRVNIWAV SKANCIMSLT
GHKNPVECVQ FNTSEEQVVA GSQSGSIRVW DLEAAKILRT LMGHKSSITS LGFHPFGDFL
ASSSMDTNIK LWDVRRRGYV FRYKGHTEAV RSLAFSPDGK WLASASDDST VKLWDLTQGK
MITEFKSHTA PVNIIQFHPN EYLLASGSSD RTIKLWDLEK FTMIGSLEGD TTPVRSVFFS
SDGSCLYSGA TDSLRIFGWE PDRCFDVVPV GWGKVSDLAV CNQQLIGVSH QLSSVSSYVV
DLKRVKKNGG SVIRGIIQDN QPLAEPRDAK GSALRRSYER PTTTCSSQRY GSPKGPNHLP
EGERRSPSED EADEKLSSAE IHNAEDFKEI FQPKNAISRT PPKVSEPFPA PPEDVNAAAV
VSVQTVEPTV VSFAKRPTPS AVVPASPPPQ PPVSTARSKP KIILSCRNEP IGLNVADFLP
SSPNNRGGAL SDDEALSQLK KGHDTMCVML RSRHKNLETV RSVWVREDIK SALDAAVSMN
DLSIVVDILN IINLQPSLWR LDLCTTTLPQ IDQLLHSKYE SYIQTGCTSL KLIMKHFWTL
ISETLKATPS VGVDITREER HQKCRAICKQ LKNLSNLVEN KALQVGRHGS AFRELQLLMA
PLD
//
