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KATL2_HUMAN
ID   KATL2_HUMAN             Reviewed;         538 AA.
AC   Q8IYT4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 3.
DT   03-AUG-2022, entry version 170.
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 {ECO:0000255|HAMAP-Rule:MF_03025};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-160.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-215 (ISOFORM 1), AND VARIANT ASN-160.
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-146 (ISOFORM 1).
RA   Arakawa T., Carninci P., Fukuda S., Hasegawa A., Hayashida K., Hori F.,
RA   Kai C., Kawai J., Kojima M., Murata M., Nakamura M., Nishiyori H.,
RA   Nomura K., Ohno M., Sasaki D., Shibazaki E., Tagami M., Tagami Y.,
RA   Hayashizaki Y.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26929214; DOI=10.1074/mcp.m115.056465;
RA   Cheung K., Senese S., Kuang J., Bui N., Ongpipattanakul C., Gholkar A.,
RA   Cohn W., Capri J., Whitelegge J.P., Torres J.Z.;
RT   "Proteomic analysis of the mammalian Katanin family of microtubule-severing
RT   enzymes defines Katanin p80 subunit B-like 1 (KATNBL1) as a regulator of
RT   mammalian Katanin microtubule-severing.";
RL   Mol. Cell. Proteomics 15:1658-1669(2016).
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   -!- INTERACTION:
CC       Q8IYT4; P35609: ACTN2; NbExp=3; IntAct=EBI-1044332, EBI-77797;
CC       Q8IYT4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1044332, EBI-739832;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03025}. Cytoplasm {ECO:0000269|PubMed:26929214}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000269|PubMed:26929214}.
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:0000269|PubMed:26929214}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IYT4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IYT4-2; Sequence=VSP_033523;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BI560635; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC012254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471096; EAW62904.1; -; Genomic_DNA.
DR   EMBL; BC034999; AAH34999.2; -; mRNA.
DR   EMBL; BI560635; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; DB461284; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS32828.1; -. [Q8IYT4-2]
DR   RefSeq; NP_112593.2; NM_031303.2. [Q8IYT4-2]
DR   RefSeq; XP_006722617.1; XM_006722554.3. [Q8IYT4-1]
DR   AlphaFoldDB; Q8IYT4; -.
DR   SMR; Q8IYT4; -.
DR   BioGRID; 123661; 10.
DR   ComplexPortal; CPX-6367; Katanin complex, KATNAL2-KATNB1 variant.
DR   ComplexPortal; CPX-6383; Katanin complex, KATNAL2-KATNBL1 variant.
DR   IntAct; Q8IYT4; 57.
DR   STRING; 9606.ENSP00000245121; -.
DR   iPTMnet; Q8IYT4; -.
DR   PhosphoSitePlus; Q8IYT4; -.
DR   BioMuta; KATNAL2; -.
DR   DMDM; 189028467; -.
DR   EPD; Q8IYT4; -.
DR   jPOST; Q8IYT4; -.
DR   MassIVE; Q8IYT4; -.
DR   MaxQB; Q8IYT4; -.
DR   PaxDb; Q8IYT4; -.
DR   PeptideAtlas; Q8IYT4; -.
DR   PRIDE; Q8IYT4; -.
DR   ProteomicsDB; 71235; -. [Q8IYT4-1]
DR   ProteomicsDB; 71236; -. [Q8IYT4-2]
DR   Antibodypedia; 22528; 66 antibodies from 16 providers.
DR   DNASU; 83473; -.
DR   Ensembl; ENST00000245121.10; ENSP00000245121.4; ENSG00000167216.19. [Q8IYT4-2]
DR   Ensembl; ENST00000356157.12; ENSP00000348478.6; ENSG00000167216.19. [Q8IYT4-1]
DR   Ensembl; ENST00000683218.1; ENSP00000508137.1; ENSG00000167216.19. [Q8IYT4-1]
DR   GeneID; 83473; -.
DR   KEGG; hsa:83473; -.
DR   MANE-Select; ENST00000683218.1; ENSP00000508137.1; NM_001387690.1; NP_001374619.1.
DR   UCSC; uc002lco.3; human. [Q8IYT4-1]
DR   CTD; 83473; -.
DR   DisGeNET; 83473; -.
DR   GeneCards; KATNAL2; -.
DR   HGNC; HGNC:25387; KATNAL2.
DR   HPA; ENSG00000167216; Low tissue specificity.
DR   MIM; 614697; gene.
DR   neXtProt; NX_Q8IYT4; -.
DR   OpenTargets; ENSG00000167216; -.
DR   PharmGKB; PA134921461; -.
DR   VEuPathDB; HostDB:ENSG00000167216; -.
DR   eggNOG; KOG0738; Eukaryota.
DR   GeneTree; ENSGT00940000157302; -.
DR   InParanoid; Q8IYT4; -.
DR   OMA; MKTQGKY; -.
DR   OrthoDB; 787710at2759; -.
DR   PhylomeDB; Q8IYT4; -.
DR   TreeFam; TF329610; -.
DR   PathwayCommons; Q8IYT4; -.
DR   SignaLink; Q8IYT4; -.
DR   SIGNOR; Q8IYT4; -.
DR   BioGRID-ORCS; 83473; 11 hits in 1067 CRISPR screens.
DR   ChiTaRS; KATNAL2; human.
DR   GenomeRNAi; 83473; -.
DR   Pharos; Q8IYT4; Tbio.
DR   PRO; PR:Q8IYT4; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q8IYT4; protein.
DR   Bgee; ENSG00000167216; Expressed in right uterine tube and 105 other tissues.
DR   ExpressionAtlas; Q8IYT4; baseline and differential.
DR   Genevisible; Q8IYT4; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IC:ComplexPortal.
DR   GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; IDA: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:0031122; P:cytoplasmic microtubule organization; IC:ComplexPortal.
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   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Isomerase;
KW   Microtubule; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..538
FT                   /note="Katanin p60 ATPase-containing subunit A-like 2"
FT                   /id="PRO_0000333792"
FT   DOMAIN          25..57
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
FT   REGION          94..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         294..301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033523"
FT   VARIANT         160
FT                   /note="S -> N (in dbSNP:rs7233515)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT                   /id="VAR_043160"
FT   CONFLICT        179..180
FT                   /note="AH -> GQ (in Ref. 3; BI560635)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="N -> S (in Ref. 3; BI560635)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   538 AA;  61253 MW;  F966747821008D3F CRC64;
     MELSYQTLKF THQAREACEM RTEARRKNLL ILISHYLTQE GYIDTANALE QETKLGLRRF
     EVCDNIDLET ILMEYESYYF VKFQKYPKIV KKSSDTAENN LPQRSRGKTR RMMNDSCQNL
     PKINQQRPRS KTTAGKTGDT KSLNKEHPNQ EVVDNTRLES ANFGLHISRI RKDSGEENAH
     PRRGQIIDFQ GLLTDAIKGA TSELALNTFD HNPDPSERLL KPLSAFIGMN SEMRELAAVV
     SRDIYLHNPN IKWNDIIGLD AAKQLVKEAV VYPIRYPQLF TGILSPWKGL LLYGPPGTGK
     TLLAKAVATE CKTTFFNISA STIVSKWRGD SEKLVRVLFE LARYHAPSTI FLDELESVMS
     QRGTASGGEH EGSLRMKTEL LVQMDGLARS EDLVFVLAAS NLPWELDCAM LRRLEKRILV
     DLPSREARQA MIYHWLPPVS KSRALELHTE LEYSVLSQET EGYSGSDIKL VCREAAMRPV
     RKIFDALENH QSESSDLPRI QLDIVTTADF LDVLTHTKPS AKNLAQRYSD WQREFESV
 
 
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