KATL1_MOUSE
ID KATL1_MOUSE Reviewed; 488 AA.
AC Q8K0T4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF LEU-286.
RX PubMed=22654668; DOI=10.1371/journal.pgen.1002697;
RA Smith L.B., Milne L., Nelson N., Eddie S., Brown P., Atanassova N.,
RA O'Bryan M.K., O'Donnell L., Rhodes D., Wells S., Napper D., Nolan P.,
RA Lalanne Z., Cheeseman M., Peters J.;
RT "KATNAL1 regulation of Sertoli cell microtubule dynamics is essential for
RT spermiogenesis and male fertility.";
RL PLoS Genet. 8:E1002697-E1002697(2012).
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 (PubMed:22654668). Has microtubule-
CC severing activity in vitro (By similarity).
CC {ECO:0000250|UniProtKB:Q9BW62, ECO:0000269|PubMed:22654668}.
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, ECO:0000269|PubMed:22654668}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9BW62}. Note=Colocalizes with microtubules
CC throughout the basal and adluminal compartments of Sertoli cells
CC (PubMed:22654668). Localizes within the cytoplasm, partially
CC overlapping with microtubules, in interphase and to the mitotic spindle
CC and spindle poles during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9BW62, ECO:0000269|PubMed:22654668}.
CC -!- TISSUE SPECIFICITY: Widely expressed, including in testis, brain,
CC heart, lung, kidney, liver, spleen, seminal vesicles and ovary. In
CC testis, restricted to Sertoli cells within the seminiferous epithelium
CC (at protein level). {ECO:0000269|PubMed:22654668}.
CC -!- DEVELOPMENTAL STAGE: Expressed in Sertoli cells from 15.5 dpc onwards
CC (at protein level). {ECO:0000269|PubMed:22654668}.
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; BC030434; AAH30434.1; -; mRNA.
DR CCDS; CCDS39404.1; -.
DR RefSeq; NP_705800.1; NM_153572.2.
DR RefSeq; XP_006504891.1; XM_006504828.3.
DR RefSeq; XP_006504892.1; XM_006504829.3.
DR AlphaFoldDB; Q8K0T4; -.
DR SMR; Q8K0T4; -.
DR BioGRID; 231194; 1.
DR STRING; 10090.ENSMUSP00000043210; -.
DR iPTMnet; Q8K0T4; -.
DR PhosphoSitePlus; Q8K0T4; -.
DR EPD; Q8K0T4; -.
DR MaxQB; Q8K0T4; -.
DR PaxDb; Q8K0T4; -.
DR PeptideAtlas; Q8K0T4; -.
DR PRIDE; Q8K0T4; -.
DR ProteomicsDB; 301742; -.
DR Antibodypedia; 49047; 198 antibodies from 20 providers.
DR DNASU; 231912; -.
DR Ensembl; ENSMUST00000047257; ENSMUSP00000043210; ENSMUSG00000041298.
DR GeneID; 231912; -.
DR KEGG; mmu:231912; -.
DR UCSC; uc009aow.2; mouse.
DR CTD; 84056; -.
DR MGI; MGI:2387638; Katnal1.
DR VEuPathDB; HostDB:ENSMUSG00000041298; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156630; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; Q8K0T4; -.
DR OMA; YEKWMSE; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; Q8K0T4; -.
DR TreeFam; TF323170; -.
DR BioGRID-ORCS; 231912; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8K0T4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K0T4; protein.
DR Bgee; ENSMUSG00000041298; Expressed in spermatid and 192 other tissues.
DR ExpressionAtlas; Q8K0T4; baseline and differential.
DR Genevisible; Q8K0T4; MM.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008352; C:katanin complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
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; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0051013; P:microtubule severing; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..488
FT /note="Katanin p60 ATPase-containing subunit A-like 1"
FT /id="PRO_0000084602"
FT REGION 95..179
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 143..171
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW62"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK7"
FT MUTAGEN 286
FT /note="L->V: Males are infertile and show a significant
FT reduction in the number of spermatids in testis, due to
FT premature exfoliation of spermatids from the seminiferous
FT epithelium. Sertoli cells contain reduced numbers of stable
FT microtubules. The protein localizes exclusively to the
FT basal compartment of Sertoli cells."
FT /evidence="ECO:0000269|PubMed:22654668"
SQ SEQUENCE 488 AA; 55165 MW; A9BFF34DF2F44BAC CRC64;
MNLAEICENA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSLRDPATKA KWQQVRQELL
EEYEQVKSIV STLESFKMDK PPDFPVSCRD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
RPLRKDVGAG ARGLVGRAHQ ISKSDKPASR DKDYRARGRD DKARKNVQDG ASDSEIPKFD
GAGYDKDLVE ALERDIVSRN PSIHWDDIAD LEEAKKLLRE AVVLPMWMPD FFKGIRRPWK
GVLMVGPPGT GKTMLAKAVA TECGTTFFNV SSSTLTSKYR GESEKLVRLL FEMARFYAPT
TIFIDEIDSI CSRRGTSDEH EASRRVKSEL LIQMDGVGGA LENDDPSKMV MVLAATNFPW
DIDEALRRRL EKRIYIPLPT AKGRAELLKI SLREVELDPD VHLEDIADKT EGYSGADITN
ICRDASLMAM RRRINGLSPE EIRALSKEEL QMPVTRGDLE LALKKIAKSV SAADLEKYEK
WMVEFGSA
