ID   KATL1_DANRE             Reviewed;         488 AA.
AC   Q5U3S1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Katanin p60 ATPase-containing subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE            Short=Katanin p60 subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE            EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE   AltName: Full=p60 katanin-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
GN   Name=katnal1; ORFNames=zgc:101696;
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=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process
CC       that is essential for spermiogenesis and male fertility. Severs
CC       microtubules in an ATP-dependent manner, promoting rapid reorganization
CC       of cellular microtubule arrays (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC         alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03024};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03024}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW62}. Note=Colocalizes
CC       with microtubules throughout the basal and adluminal compartments of
CC       Sertoli cells (By similarity). Localizes within the cytoplasm,
CC       partially overlapping with microtubules, in interphase and to the
CC       mitotic spindle and spindle poles during mitosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K0T4, ECO:0000250|UniProtKB:Q9BW62}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC       subfamily. A-like 1 sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03024}.
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DR   EMBL; BC085416; AAH85416.1; -; mRNA.
DR   RefSeq; NP_001007432.1; NM_001007431.1.
DR   AlphaFoldDB; Q5U3S1; -.
DR   SMR; Q5U3S1; -.
DR   STRING; 7955.ENSDARP00000005849; -.
DR   PaxDb; Q5U3S1; -.
DR   GeneID; 492790; -.
DR   KEGG; dre:492790; -.
DR   CTD; 84056; -.
DR   ZFIN; ZDB-GENE-041114-141; katnal1.
DR   eggNOG; KOG0738; Eukaryota.
DR   InParanoid; Q5U3S1; -.
DR   OrthoDB; 717356at2759; -.
DR   PhylomeDB; Q5U3S1; -.
DR   PRO; PR:Q5U3S1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051013; P:microtubule severing; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03023; Katanin_p60_A1; 1.
DR   HAMAP; MF_03024; Katanin_p60_AL1; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR028596; KATNA1.
DR   InterPro; IPR028594; Katnal1_chordates.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Katanin p60 ATPase-containing subunit A-like 1"
FT                   /id="PRO_0000358714"
FT   REGION          84..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..107
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03024"
SQ   SEQUENCE   488 AA;  54891 MW;  9C474EA3808FFC8C CRC64;
     MNLTEICDNA KKGREYALLG NYDSSMVYYQ GVIQQIHKHC QSLRDPAQKV KWQQVRQELA
     EEYEQVKSIV STLESFKVDK AVDFPNPVPE EGPRDPDVWP PPTPAEHRGP VQVKKPVPLS
     KPQRKESPGM QHRGAVGRGQ ANIKPDRPNT RDGRGNKAKE EKSKRNAQEG AADVEQKKFD
     GTGYDSDLVD ALERDIVSRN PNIHWDDIAD LEDAKKLLRE AVVLPMWMPD FFKGIRRPWK
     GVLMVGPPGT GKTMLAKAVA TECGTTFFNV SSSTLTSKYR GESEKLVRLL FEMARFYAPT
     TIFIDEIDSI CGRRGTSDEH EASRRVKSEL LVQMDGVGGA QESEDPSKMV MVLAATNFPW
     DIDEALRRRL EKRIYIPLPT AKGRAELLKI NLREVDVASD VDLTVFAEKI EGYSGADITN
     VCRDASMMAM RRRIQGLSPE EIRALSKDEL QMPVTMEDFE LALKKISKSV SAADLEKYES
     WMSEFGSV