KATL1_RABIT
ID KATL1_RABIT Reviewed; 490 AA.
AC B7NZ88;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 {ECO:0000255|HAMAP-Rule:MF_03024};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (DEC-2008) 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). Has microtubule-
CC severing activity in vitro (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0T4, ECO:0000250|UniProtKB:Q9BW62}.
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 -!- SUBUNIT: Interacts with KATNB1 and KATNBL1.
CC {ECO:0000250|UniProtKB:Q9BW62}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP001022; ACJ72829.1; -; Genomic_DNA.
DR RefSeq; NP_001164961.1; NM_001171490.1.
DR RefSeq; XP_008271739.1; XM_008273517.2.
DR RefSeq; XP_008271740.1; XM_008273518.2.
DR RefSeq; XP_008271741.1; XM_008273519.2.
DR AlphaFoldDB; B7NZ88; -.
DR SMR; B7NZ88; -.
DR STRING; 9986.ENSOCUP00000002938; -.
DR PRIDE; B7NZ88; -.
DR Ensembl; ENSOCUT00000046530; ENSOCUP00000027774; ENSOCUG00000003387.
DR GeneID; 100328900; -.
DR KEGG; ocu:100328900; -.
DR CTD; 84056; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156630; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; B7NZ88; -.
DR OMA; YEKWMSE; -.
DR OrthoDB; 717356at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000003387; Expressed in testis and 15 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:Ensembl.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
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:0042802; F:identical protein binding; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
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 InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..490
FT /note="Katanin p60 ATPase-containing subunit A-like 1"
FT /id="PRO_0000367125"
FT REGION 96..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW62"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK7"
SQ SEQUENCE 490 AA; 55295 MW; 9B2843DC82377A12 CRC64;
MNLAEICDNA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSIRDPAVKG KWQQVRQELL
EEYEQVKSIV STLESFKIEK PPDFPVSCQD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
RPLRKEMAGV GARGPVGRAH PISKSEKPSA SRDKDCRARG RDDKGRKNMQ DGASDGEIPK
FDGAGYDKDL VEALERDIVS RNPSIHWDDI ADLEEAKKLL REAVVLPMWM PDFFKGIRRP
WKGVLMVGPP GTGKTMLAKA VATECGTTFF NVSSSTLTSK YRGESEKLVR LLFEMARFYA
PTTIFIDEID SICSRRGTSD EHEASRRVKS ELLVQMDGVG GALENDDPSK MVMVLAATNF
PWDIDEALRR RLEKRIYIPL PTAKGRAELL KISLREVELD PDIRLEDIAE KIEGYSGADI
TNVCRDASLM AMRRRINGLS PEEIRALSKE ELQMPVTRGD FELALKKIAK SVSAADLEKY
EKWMVEFGSA
