KTNB1_STRPU
ID KTNB1_STRPU Reviewed; 690 AA.
AC O61585;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022};
DE Short=Katanin p80 subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022};
DE AltName: Full=p80 katanin {ECO:0000255|HAMAP-Rule:MF_03022};
GN Name=KATNB1 {ECO:0000255|HAMAP-Rule:MF_03022};
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-6; 8-23; 27-34; 41-56;
RP 66-77; 84-97; 105-117; 122-127; 129-141; 182-199; 207-215; 300-311;
RP 336-349; 354-364; 410-433; 439-461; 486-512; 517-529; 531-567; 636-650 AND
RP 653-668, FUNCTION, AND INTERACTION WITH KATNA1.
RX PubMed=9568719; DOI=10.1016/s0092-8674(00)81578-0;
RA Hartman J.J., Mahr J., McNally K., Okawa K., Iwamatsu A., Thomas S.,
RA Cheesman S., Heuser J., Vale R.D., McNally F.J.;
RT "Katanin, a microtubule-severing protein, is a novel AAA ATPase that
RT targets to the centrosome using a WD40-containing subunit.";
RL Cell 93:277-287(1998).
RN [2]
RP FUNCTION.
RX PubMed=8221885; DOI=10.1016/0092-8674(93)90377-3;
RA McNally F.J., Vale R.D.;
RT "Identification of katanin, an ATPase that severs and disassembles stable
RT microtubules.";
RL Cell 75:419-429(1993).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=8907702; DOI=10.1242/jcs.109.3.561;
RA McNally F.J., Okawa K., Iwamatsu A., Vale R.D.;
RT "Katanin, the microtubule-severing ATPase, is concentrated at
RT centrosomes.";
RL J. Cell Sci. 109:561-567(1996).
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:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:8221885,
CC ECO:0000269|PubMed:9568719}.
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:0000255|HAMAP-Rule:MF_03022,
CC ECO:0000269|PubMed:9568719}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03022,
CC ECO:0000269|PubMed:8907702}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03022,
CC ECO:0000269|PubMed:8907702}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:8907702}.
CC Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022,
CC ECO:0000269|PubMed:8907702}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9BVA0}. Note=Predominantly cytoplasmic.
CC Localized to the interphase centrosome and mitotic spindle poles.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03022}.
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DR EMBL; AF052433; AAC09329.1; -; mRNA.
DR RefSeq; NP_999734.1; NM_214569.1.
DR AlphaFoldDB; O61585; -.
DR SMR; O61585; -.
DR STRING; 7668.SPU_014392-tr; -.
DR GeneID; 762546; -.
DR eggNOG; KOG0267; Eukaryota.
DR InParanoid; O61585; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008352; C:katanin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
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:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Mitosis; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..690
FT /note="Katanin p80 WD40 repeat-containing subunit B1"
FT /id="PRO_0000051053"
FT REPEAT 14..54
FT /note="WD 1"
FT REPEAT 57..96
FT /note="WD 2"
FT REPEAT 99..138
FT /note="WD 3"
FT REPEAT 141..182
FT /note="WD 4"
FT REPEAT 184..222
FT /note="WD 5"
FT REPEAT 225..265
FT /note="WD 6"
FT REGION 304..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 75814 MW; F4404CD6206971DD CRC64;
MATKRAWKLQ ELVAHSSNVN CLALGPMSGR VMVTGGEDKK VNLWAVGKQN CIISLSGHTS
PVDSVKFNSS EELVVAGSQS GTMKIYDLEP AKIVRTLTGH RNSIRCMDFH PFGEFVASGS
TDTNVKLWDV RRKGCIYTYK GHSDQVNMIK FSPDGKWLVT ASEDTTIKLW DLTMGKLFQE
FKNHTGGVTG IEFHPNEFLL ASGSSDRTVQ FWDLETFQLV SSTSPGASAV RSISFHPDGS
YLFCSSQDML HAFGWEPIRC FDTFSVGWGK VADTVIASTQ LIGASFNATN VSVYVADLSR
MSTTGIAQEP QSQPSKTPSG GAEEVPSKPL TASGRKNFVR ERPHTTSSKQ RQPDVKSEPE
RQSPTQDEGV KDDDATDIKD PDSYAKIFSP KTRVDHSPER NAQPFPAPLD VPGAQEPEPF
KHPPKPAAAA AVAPVSRAPA PSASDWQPAQ ANPAPNRVPA ATKPVPAQEV APSRKPDPIS
TIIPSDRNKP ANLDMDAFLP PAHAQQAPRV NAPASRKQSD SERIEGLRKG HDSMCQVLSS
RHRNLDVVRA IWTAGDAKTS VESVVNMKDQ AILVDILNIM LLKKSLWNLD MCVVVLPRLK
ELLSSKYENY VHTSCACLKL ILKNFTSLFN QNIKCPPSGI DITREERYNK CSKCYSYLIA
TRGYVEEKQH VSGKLGSSFR ELHLLLDQLE
