KTNB1_DANRE
ID KTNB1_DANRE Reviewed; 694 AA.
AC Q7ZUV2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
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; ORFNames=zgc:56071;
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].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=25521378; DOI=10.1016/j.neuron.2014.12.014;
RA Mishra-Gorur K., Caglayan A.O., Schaffer A.E., Chabu C., Henegariu O.,
RA Vonhoff F., Akguemues G.T., Nishimura S., Han W., Tu S., Baran B.,
RA Guemues H., Dilber C., Zaki M.S., Hossni H.A., Riviere J.B., Kayserili H.,
RA Spencer E.G., Rosti R.O., Schroth J., Per H., Caglar C., Caglar C.,
RA Doelen D., Baranoski J.F., Kumandas S., Minja F.J., Erson-Omay E.Z.,
RA Mane S.M., Lifton R.P., Xu T., Keshishian H., Dobyns W.B., Chi N.C.,
RA Sestan N., Louvi A., Bilguevar K., Yasuno K., Gleeson J.G., Guenel M.;
RT "Mutations in KATNB1 cause complex cerebral malformations by disrupting
RT asymmetrically dividing neural progenitors.";
RL Neuron 84:1226-1239(2014).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=25521379; DOI=10.1016/j.neuron.2014.12.017;
RA Hu W.F., Pomp O., Ben-Omran T., Kodani A., Henke K., Mochida G.H., Yu T.W.,
RA Woodworth M.B., Bonnard C., Raj G.S., Tan T.T., Hamamy H., Masri A.,
RA Shboul M., Al Saffar M., Partlow J.N., Al-Dosari M., Alazami A.,
RA Alowain M., Alkuraya F.S., Reiter J.F., Harris M.P., Reversade B.,
RA Walsh C.A.;
RT "Katanin p80 regulates human cortical development by limiting centriole and
RT cilia number.";
RL Neuron 84:1240-1257(2014).
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}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03022}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton
CC {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9BVA0}. Note=Predominantly cytoplasmic.
CC Localized to the interphase centrosome and mitotic spindle poles.
CC {ECO:0000255|HAMAP-Rule:MF_03022}.
CC -!- DISRUPTION PHENOTYPE: Results in a significant reduction in midbrain
CC size. A wide spectrum of defects in gastrulation and formation of
CC anterior structures are noticed, ranging from milder microcephaly to
CC more severe anencephaly and early embryonic death.
CC {ECO:0000269|PubMed:25521378, ECO:0000269|PubMed:25521379}.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03022}.
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DR EMBL; BC047819; AAH47819.1; -; mRNA.
DR RefSeq; NP_998183.1; NM_213018.1.
DR RefSeq; XP_005166561.1; XM_005166504.3.
DR RefSeq; XP_005166562.1; XM_005166505.3.
DR AlphaFoldDB; Q7ZUV2; -.
DR SMR; Q7ZUV2; -.
DR STRING; 7955.ENSDARP00000024623; -.
DR PaxDb; Q7ZUV2; -.
DR Ensembl; ENSDART00000014632; ENSDARP00000024623; ENSDARG00000005456.
DR GeneID; 406291; -.
DR KEGG; dre:406291; -.
DR CTD; 10300; -.
DR ZFIN; ZDB-GENE-040426-1954; katnb1.
DR eggNOG; KOG0267; Eukaryota.
DR GeneTree; ENSGT00940000157918; -.
DR InParanoid; Q7ZUV2; -.
DR OrthoDB; 425951at2759; -.
DR PhylomeDB; Q7ZUV2; -.
DR TreeFam; TF332359; -.
DR PRO; PR:Q7ZUV2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000005456; Expressed in testis and 21 other tissues.
DR ExpressionAtlas; Q7ZUV2; baseline.
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:0007420; P:brain development; IMP:ZFIN.
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 GO; GO:0030901; P:midbrain development; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..694
FT /note="Katanin p80 WD40 repeat-containing subunit B1"
FT /id="PRO_0000051051"
FT REPEAT 18..58
FT /note="WD 1"
FT REPEAT 61..100
FT /note="WD 2"
FT REPEAT 103..142
FT /note="WD 3"
FT REPEAT 145..186
FT /note="WD 4"
FT REPEAT 188..226
FT /note="WD 5"
FT REPEAT 229..269
FT /note="WD 6"
FT REGION 319..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 75995 MW; 4D7A9145EA300EB4 CRC64;
MALTNTTITS WKLQEIVAHS SNVSSLVLGK SSGRLLATGG EDCRVNIWAV SKPNCIMSLT
GHTSAVGCIQ FNSSEERVVA GSLSGSLRLW DLEAAKILRT LMGHKASISS LDFHPMGEYL
ASGSVDSNIK LWDVRRKGCV FRYKGHTQAV RCLAFSPDGK WLASASDDST VKLWDLIAGK
MITEFTSHTS AVNVVQFHPN EYLLASGSAD RTVKLWDLEK FNMIGSSEGE TGVVRSVLFN
PDGSCLYSGS ENTLRVYGWE PDRCFDVVHV GWGKVSDLAI SNNQMIAVSY SHTNVSWYVV
DLNRVKKSGS VIQGLIQDKP IPAPSSALGT TLRRNYERPT TSCTGQEMKQ SSEADRRSPE
GERRSPSSED EKEDKESSAE ITNPEDYKEI FQPRSVISRT PPKTTEPFPA PLEHSFSESV
LEKPGPVVKI VTPVIDRAGQ LKGPITSSTP VQRVEPTVIA AAPRPVAVVT TSASSPSRPV
VNTTKPKPST GIILSTRNEP IGLNAGDFLS HARNAKASAM GDEEALAQIR KGHDTMCVML
SSRSKNLDSV RSVWASGDVK TSLDSAVSMN DLSIVVDVLN IINLKPSLWK LDLCTSILPQ
IEELLQSRYE SYVQTGCMSL KLILKRFWPL ISDTLNAPPS VGVDITREER HQKCKACYKQ
LKNLSNVVKN RAEQVGRHGS TFRELQLLMA PLDY