KATL1_PAPAN
ID KATL1_PAPAN Reviewed; 490 AA.
AC A9RA82;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (DEC-2007) 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; DP000511; ABX89264.1; -; Genomic_DNA.
DR RefSeq; NP_001162539.1; NM_001169068.1.
DR AlphaFoldDB; A9RA82; -.
DR SMR; A9RA82; -.
DR STRING; 9555.ENSPANP00000009005; -.
DR PRIDE; A9RA82; -.
DR Ensembl; ENSPANT00000078021; ENSPANP00000051502; ENSPANG00000023364.
DR GeneID; 100137574; -.
DR KEGG; panu:100137574; -.
DR CTD; 84056; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156630; -.
DR OrthoDB; 717356at2759; -.
DR Proteomes; UP000028761; Chromosome 15.
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_0000367124"
FT REGION 95..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Pro residues"
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; 55312 MW; 034DAB7601DE345A CRC64;
MNLAEICDNA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSVRDPAIKG KWQQVRQELL
EEYEQVKSIV STLESFKIDR PPDFPVSCQD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
RPLRKEMAGV GARGPVGRAH PISKSEKPST SRDKDCRARG RDDKGRKNMQ DGASDGEMPK
FDGAGYDKDL VEALERDIVS RNPSIHWDDI ADLEEAKKLL REAVVLPMWM PDFFKGIRRP
WKGVLMVGPP GTGKTMLAKA VATECGTTFF NVSSSTLTSK YRGESEKLVR LLFEMARFYA
PTTIFIDEID SICSRRGTSD EHEASRRVKS ELLIQMDGVG GALENDDPSK MVMVLAATNF
PWDIDEALRR RLEKRIYIPL PTAKGRAELL KINLREVELD PDIQLEDIAE KIEGYSGADI
TNVCRDASLM AMRRRINGLG PEEIRALSKE ELQMPVTKGD FELALKKIAK SVSAADLEKY
EKWMVEFGSA
