KATL2_MOUSE
ID KATL2_MOUSE Reviewed; 539 AA.
AC Q9D3R6; Q6NSQ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Katanin p60 ATPase-containing subunit A-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
DE Short=Katanin p60 subunit A-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03025};
DE AltName: Full=p60 katanin-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
GN Name=Katnal2;
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] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Jaw;
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).
CC -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This
CC activity may promote rapid reorganization of cellular microtubule
CC arrays. {ECO:0000255|HAMAP-Rule:MF_03025}.
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_03025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03025}. Cytoplasm {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8IYT4}.
CC Note=Localizes within the cytoplasm, partially overlapping with
CC microtubules in interphase and to the mitotic spindle and spindle poles
CC during mitosis. {ECO:0000250|UniProtKB:Q8IYT4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D3R6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D3R6-2; Sequence=VSP_033524, VSP_033525, VSP_033526;
CC Name=3;
CC IsoId=Q9D3R6-3; Sequence=VSP_033527, VSP_033528;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. A-like 2 sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03025}.
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DR EMBL; AK017114; BAB30604.1; -; mRNA.
DR EMBL; AC132608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069977; AAH69977.1; -; mRNA.
DR CCDS; CCDS37865.1; -. [Q9D3R6-3]
DR CCDS; CCDS89281.1; -. [Q9D3R6-1]
DR RefSeq; NP_081997.1; NM_027721.2. [Q9D3R6-3]
DR RefSeq; XP_006526500.1; XM_006526437.3.
DR AlphaFoldDB; Q9D3R6; -.
DR SMR; Q9D3R6; -.
DR STRING; 10090.ENSMUSP00000026486; -.
DR iPTMnet; Q9D3R6; -.
DR PhosphoSitePlus; Q9D3R6; -.
DR EPD; Q9D3R6; -.
DR jPOST; Q9D3R6; -.
DR MaxQB; Q9D3R6; -.
DR PaxDb; Q9D3R6; -.
DR PRIDE; Q9D3R6; -.
DR ProteomicsDB; 301743; -. [Q9D3R6-1]
DR ProteomicsDB; 301744; -. [Q9D3R6-2]
DR ProteomicsDB; 301745; -. [Q9D3R6-3]
DR Antibodypedia; 22528; 66 antibodies from 16 providers.
DR DNASU; 71206; -.
DR Ensembl; ENSMUST00000026486; ENSMUSP00000026486; ENSMUSG00000025420. [Q9D3R6-3]
DR Ensembl; ENSMUST00000126153; ENSMUSP00000122079; ENSMUSG00000025420. [Q9D3R6-1]
DR Ensembl; ENSMUST00000154665; ENSMUSP00000119066; ENSMUSG00000025420. [Q9D3R6-2]
DR GeneID; 71206; -.
DR UCSC; uc008fqx.1; mouse. [Q9D3R6-3]
DR UCSC; uc008fqz.1; mouse. [Q9D3R6-2]
DR CTD; 83473; -.
DR MGI; MGI:1924234; Katnal2.
DR VEuPathDB; HostDB:ENSMUSG00000025420; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000157302; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; Q9D3R6; -.
DR OMA; MKTQGKY; -.
DR OrthoDB; 787710at2759; -.
DR PhylomeDB; Q9D3R6; -.
DR TreeFam; TF329610; -.
DR BioGRID-ORCS; 71206; 0 hits in 57 CRISPR screens.
DR ChiTaRS; Katnal2; mouse.
DR PRO; PR:Q9D3R6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D3R6; protein.
DR Bgee; ENSMUSG00000025420; Expressed in spermatid and 117 other tissues.
DR ExpressionAtlas; Q9D3R6; baseline and differential.
DR Genevisible; Q9D3R6; MM.
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; IEA:UniProtKB-EC.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03025; Katanin_p60_AL2; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027497; Katanin_p60_AL2.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF08513; LisH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50896; LISH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Isomerase;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..539
FT /note="Katanin p60 ATPase-containing subunit A-like 2"
FT /id="PRO_0000333793"
FT DOMAIN 25..57
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
FT REGION 93..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 295..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
FT VAR_SEQ 150..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033524"
FT VAR_SEQ 185..219
FT /note="GQIIDFRGLLSDAIKGATSEFALNTFECNPDPSER -> VSGAQGPRMERGT
FT CLKKKENKAYSCCQTGKRRQKH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033525"
FT VAR_SEQ 220..539
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033526"
FT VAR_SEQ 407..409
FT /note="LDC -> GDA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033527"
FT VAR_SEQ 410..539
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033528"
SQ SEQUENCE 539 AA; 61153 MW; 199E141AEF2F402C CRC64;
MELSYQTLKL THQAREAYEM RTEARRKNLL ILILHYLTQE GYMDAAKALE EETKLGLRRF
EVCDNVDLET ILMEYESYYF VKFQKYPKVV KKAPDPVENN LPSRSGGKNK RLTNDSCQNL
PKICHQKSRP KTSAVKTGDT KSVKEHLKQV KESVTDTQAE STDFGLNISK IHKDQPEEKA
QPRRGQIIDF RGLLSDAIKG ATSEFALNTF ECNPDPSERL LKPLSAFIGM NSEMRELAAV
VSRDIYLHNP NIKWNDIIGL DAAKQLVKEA VVYPIRYPQL FTGILSPWKG LLLYGPPGTG
KTLLAKAVAT ECKTTFFNIS ASTIVSKWRG DSEKLVRVLF ELARYHAPST IFLDELESVM
SQRGMVPGGE HEGSLRMKTE LLVQMDGLAR SEDLVFVLAA SNLPWELDCA MLRRLEKRIL
VDLPSQEARQ AMIYHWLPPV SKNHALELHT QLEYSVLSQE TEGYSGSDIK LVCREAAMRP
VRKIFSVLEN NQSESNNLPG IQLDTVTTQD FLDVLAHTKP SAKNLTERYL AWQEKFESV
