ID   LZTS2_MOUSE             Reviewed;         671 AA.
AC   Q91YU6; E9QKK6; Q569X6;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Leucine zipper putative tumor suppressor 2 {ECO:0000255|HAMAP-Rule:MF_03026};
DE   AltName: Full=Protein LAPSER1 {ECO:0000255|HAMAP-Rule:MF_03026};
GN   Name=Lzts2; Synonyms=Kiaa1813, Lapser1;
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=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
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   SUBCELLULAR LOCATION.
RX   PubMed=18490357; DOI=10.1093/hmg/ddn153;
RA   Sudo H., Maru Y.;
RT   "LAPSER1/LZTS2: a pluripotent tumor suppressor linked to the inhibition of
RT   katanin-mediated microtubule severing.";
RL   Hum. Mol. Genet. 17:2524-2540(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-296, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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).
CC   -!- FUNCTION: Negative regulator of katanin-mediated microtubule severing
CC       and release from the centrosome. Required for central spindle formation
CC       and the completion of cytokinesis. May negatively regulate axonal
CC       outgrowth by preventing the formation of microtubule bundles that are
CC       necessary for transport within the elongating axon. Negative regulator
CC       of the Wnt signaling pathway. Represses beta-catenin-mediated
CC       transcriptional activation by promoting the nuclear exclusion of beta-
CC       catenin. {ECO:0000255|HAMAP-Rule:MF_03026}.
CC   -!- SUBUNIT: Interacts with KATNB1. Also interacts with CTNNB1, gamma-
CC       tubulin and KIF23. {ECO:0000255|HAMAP-Rule:MF_03026}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03026}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000255|HAMAP-Rule:MF_03026, ECO:0000269|PubMed:18490357}.
CC       Note=Localized to the centrosome throughout the cell cycle. Localized
CC       to the midbody in cells undergoing cytokinesis. {ECO:0000255|HAMAP-
CC       Rule:MF_03026}.
CC   -!- SIMILARITY: Belongs to the LZTS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03026}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98256.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129446; BAC98256.1; ALT_INIT; mRNA.
DR   EMBL; AC132957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014695; AAH14695.1; -; mRNA.
DR   EMBL; BC092263; AAH92263.1; -; mRNA.
DR   CCDS; CCDS29855.1; -.
DR   RefSeq; NP_001123997.1; NM_001130525.1.
DR   RefSeq; NP_001123998.1; NM_001130526.1.
DR   RefSeq; NP_663478.2; NM_145503.2.
DR   RefSeq; XP_006527067.1; XM_006527004.3.
DR   AlphaFoldDB; Q91YU6; -.
DR   SMR; Q91YU6; -.
DR   BioGRID; 230483; 4.
DR   IntAct; Q91YU6; 4.
DR   STRING; 10090.ENSMUSP00000045478; -.
DR   iPTMnet; Q91YU6; -.
DR   PhosphoSitePlus; Q91YU6; -.
DR   EPD; Q91YU6; -.
DR   MaxQB; Q91YU6; -.
DR   PaxDb; Q91YU6; -.
DR   PeptideAtlas; Q91YU6; -.
DR   PRIDE; Q91YU6; -.
DR   ProteomicsDB; 292159; -.
DR   Antibodypedia; 31240; 157 antibodies from 27 providers.
DR   DNASU; 226154; -.
DR   Ensembl; ENSMUST00000039016; ENSMUSP00000045478; ENSMUSG00000035342.
DR   Ensembl; ENSMUST00000178087; ENSMUSP00000136405; ENSMUSG00000035342.
DR   Ensembl; ENSMUST00000179108; ENSMUSP00000137571; ENSMUSG00000035342.
DR   GeneID; 226154; -.
DR   KEGG; mmu:226154; -.
DR   UCSC; uc008hql.2; mouse.
DR   CTD; 84445; -.
DR   MGI; MGI:2385095; Lzts2.
DR   VEuPathDB; HostDB:ENSMUSG00000035342; -.
DR   eggNOG; ENOG502QWFS; Eukaryota.
DR   GeneTree; ENSGT00940000154078; -.
DR   HOGENOM; CLU_026379_2_0_1; -.
DR   InParanoid; Q91YU6; -.
DR   OMA; EDCTAQA; -.
DR   OrthoDB; 1014871at2759; -.
DR   PhylomeDB; Q91YU6; -.
DR   TreeFam; TF331420; -.
DR   BioGRID-ORCS; 226154; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Lzts2; mouse.
DR   PRO; PR:Q91YU6; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q91YU6; protein.
DR   Bgee; ENSMUSG00000035342; Expressed in lip and 245 other tissues.
DR   ExpressionAtlas; Q91YU6; baseline and differential.
DR   Genevisible; Q91YU6; MM.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:MGI.
DR   GO; GO:0051168; P:nuclear export; IEA:UniProtKB-UniRule.
DR   GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR   GO; GO:0060682; P:primary ureteric bud growth; IMP:MGI.
DR   GO; GO:0051255; P:spindle midzone assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0072197; P:ureter morphogenesis; IMP:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR   HAMAP; MF_03026; LZTS2; 1.
DR   InterPro; IPR045329; LZTS.
DR   InterPro; IPR028597; LZTS2.
DR   PANTHER; PTHR19354; PTHR19354; 1.
DR   PANTHER; PTHR19354:SF4; PTHR19354:SF4; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Phosphoprotein; Reference proteome;
KW   Wnt signaling pathway.
FT   CHAIN           1..671
FT                   /note="Leucine zipper putative tumor suppressor 2"
FT                   /id="PRO_0000182975"
FT   REGION          1..333
FT                   /note="Required for centrosomal localization"
FT                   /evidence="ECO:0000250"
FT   REGION          1..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..671
FT                   /note="Sufficient for interaction with CTNNB1"
FT                   /evidence="ECO:0000250"
FT   REGION          452..671
FT                   /note="Sufficient for interaction with KATNB1 and for
FT                   inhibition of katanin-mediated microtubule severing"
FT                   /evidence="ECO:0000250"
FT   COILED          329..651
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
FT   MOTIF           633..642
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
FT   COMPBIAS        90..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..323
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRK4"
FT   CONFLICT        64
FT                   /note="P -> R (in Ref. 1; BAC98256 and 3; AAH14695/
FT                   AAH92263)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="H -> Q (in Ref. 3; AAH14695/AAH92263)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   671 AA;  72578 MW;  5F78644A14B1F1E6 CRC64;
     MAIVHTLPVP LEPARETATA PKTPAMGSVS SLISGRPCPG GPAPQRHHGV PGPTFFRQQD
     GLLPGGYEAQ EPLCPAVPPR KAVPGNSFTY VNEDFRTESP PSPSSDVEDP REHQAHNAHL
     RGPPPKLIPV SGKLEKNMEK ILIRPTAFKP VLPKPRGAPS LPGFLGPRAA GLSGSQGSLT
     QLFGGPASSS SSSSSSSAAD KPLALSGWAS GCPSGTLSDS GRNSLSSLPT YSTGGAEPTT
     NSPGGHLPSH GPGRGALPGP ARGVPTGPSH SDSGRSSSSK STGSLGGRVA GGLLGSGARA
     SPGSSSGGDR SPPPPPPPPP SDEALLHCVL EGKLRDREAE LQQLRDSMDE SEATVCQAFG
     ARQRRWPRER GEDCAAQAQQ ATQRVQRAQQ LLQLQVFQLQ QEKRQLQDDF AQLLQEREQL
     ERRCATFERE QRELGPRLEE TKWEVCQKSG EISLLKQQLK ESQAELVQKG SELVALRVAL
     REARATLRVS EGRARGLQEA ARAREQELEA CSQELQRYRQ EAERLREKAG HLDAEASGLR
     DPPVPPATTD PFLLAESDEA KVQRAAAGAG GSLRAQVERL RQELQREQRR GDEQRDSFEG
     ERLAWQAEKE QVIRYQKQLQ HNYIQMYRRN RQLEQELQQL SLELEARELA DLGLAESAPC
     ICLEEITATE I