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KTNB1_XENLA
ID   KTNB1_XENLA             Reviewed;         655 AA.
AC   Q4V7Y7; O93320; Q6DE69;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 305-655, FUNCTION, INTERACTION WITH KATNA1,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Ovary;
RX   PubMed=9658175; DOI=10.1091/mbc.9.7.1847;
RA   McNally F.J., Thomas S.;
RT   "Katanin is responsible for the M-phase microtubule-severing activity in
RT   Xenopus eggs.";
RL   Mol. Biol. Cell 9:1847-1861(1998).
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:9658175}.
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       ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03022,
CC       ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:9658175}.
CC       Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022,
CC       ECO:0000269|PubMed:9658175}. 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH77273.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC077273; AAH77273.1; ALT_SEQ; mRNA.
DR   EMBL; BC097654; AAH97654.1; -; mRNA.
DR   EMBL; AF056021; AAC25113.1; -; mRNA.
DR   RefSeq; NP_001081754.1; NM_001088285.1.
DR   AlphaFoldDB; Q4V7Y7; -.
DR   SMR; Q4V7Y7; -.
DR   BioGRID; 99367; 1.
DR   DNASU; 398032; -.
DR   GeneID; 398032; -.
DR   KEGG; xla:398032; -.
DR   CTD; 398032; -.
DR   Xenbase; XB-GENE-998277; katnb1.L.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 398032; Expressed in ovary and 19 other tissues.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008352; C:katanin complex; IEA:InterPro.
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: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; 5.
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; Microtubule; Mitosis;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..655
FT                   /note="Katanin p80 WD40 repeat-containing subunit B1"
FT                   /id="PRO_0000270748"
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..184
FT                   /note="WD 4"
FT   REPEAT          187..226
FT                   /note="WD 5"
FT   REPEAT          229..269
FT                   /note="WD 6"
FT   REGION          338..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        402
FT                   /note="V -> I (in Ref. 2; AAC25113)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   655 AA;  71593 MW;  EA24B2D6920509E3 CRC64;
     MAAPSPTKTT WKLQEIVAHG CSVSSVVLGR SSGRLVATGG DDCRVHLWSV NKPNCIMSLT
     GHTTPVESVR FNNSEELIVA GSQSGSLRIW DLEAAKILRT LMGHKANVSS LDFHPYGEFV
     ASGSLDTNIK LWDVRRKGCV FRYKGHTQAV RCLRFSPDGK WLASASDDHS VKLWDLTAGK
     MMAELSEHKG PVNIIEFHPN EYLLASGSAD RTVRFWDLEK FQLVGCTEGE TIPVRAILFS
     NDGGCIFCGG KDSLRVYGWE PDQCFDTVPV GWGKVSDLAI CNNQLIGVSS AQSNISSFVV
     DLTRVKMTGC APQGPVPAEI PISQPAPTGT SLRRIYERPS TTCSKPNRVS PTSDDEEKES
     RAEIQNPEDY KEIFQPKNAI SRTPPRNSEP FPAPPEDDIS IVKEAVAPTP DVVTPATSNK
     KNTEQLQRPP VAASTPIVCQ EPSPVPAPQS KPPVISAARN EPIGLKAADF LPAVKSSSPT
     EVVDDEAVSQ IRKGHDTMCM VLTSRMRNLD TVRAVWSSGD IKTSIDSAVA INDLSVVVDL
     LNIINQKASL WKLDLCMTVL PQIEKMLQSK YESYVQTGCI SLKLILQRFL PLITDILAAP
     PSVGVDISRE ERLSKCKLCY KQLRILSPLV KSKASQSGRY GSAFRELHLL MSGLE
 
 
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