KATL1_OTOGA
ID KATL1_OTOGA Reviewed; 490 AA.
AC B4USW8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii(Bushbaby).";
RL Submitted (MAR-2011) 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}.
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DR EMBL; DP000875; ACG64309.1; -; Genomic_DNA.
DR RefSeq; XP_003797655.1; XM_003797607.2.
DR AlphaFoldDB; B4USW8; -.
DR SMR; B4USW8; -.
DR STRING; 30611.ENSOGAP00000010127; -.
DR GeneID; 100944651; -.
DR KEGG; oga:100944651; -.
DR CTD; 84056; -.
DR eggNOG; KOG0738; Eukaryota.
DR InParanoid; B4USW8; -.
DR OrthoDB; 717356at2759; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
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: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; 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_0000367123"
FT REGION 87..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; 55207 MW; 3A0C1AF450DE55A1 CRC64;
MNLAEICDNA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSVRDPAVKG KWQQVRQELL
EEYEQVKSIV STLESFKIDK PPDFPVSCQD EPVRDPAVWP PPVPAEHRAP PQIRRSNREV
RPLRKDMAGV GARGPVGRAH PISKSEKPST SRDKDNRARG KDDKGRKNMQ DGASDGEIPK
FDGAGYDKDL IEALERDIVS RNPSIHWDDI ADLEEAKKLL REAVVLPMWM PDFFKGIRRP
WKGVLMVGPP GTGKTMLAKA VATECGTTFF NVSSSTLTSK YRGESEKLVR LLFEMARFYA
PTTIFIDEID SICSRRGTSD EHEASRRVKS ELLIQMDGVG GALENDDPSK MVMVLAATNF
PWDIDEALRR RLEKRIYIPL PTAKGRAELL KINLREVELD PDIQLEDIAE KIEGYSGADI
TNVCRDASLM AMRRRINGLS PEEIRALSKE ELQMPVTKGD FELALKKIAK SVSAADLEKY
EKWMVEFGSA
