LZTS2_RAT
ID LZTS2_RAT Reviewed; 670 AA.
AC Q3LUD4; Q24K74;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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=Lapser1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GAMMA-TUBULIN, KIF23
RP AND KATNB1, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar;
RX PubMed=17351128; DOI=10.1096/fj.06-7254com;
RA Sudo H., Maru Y.;
RT "LAPSER1 is a putative cytokinetic tumor suppressor that shows the same
RT centrosome and midbody subcellular localization pattern as p80 katanin.";
RL FASEB J. 21:2086-2100(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.-H., Proepper C.,
RA Sobue K., Gundelfinger E.D., Kreutz M.R., Boeckers T.M.;
RT "ProSAPiP1, a novel PSD protein that links spar to the PDZ domain of
RT ProSAP2/Shank3.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH KATNB1, AND 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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, ECO:0000269|PubMed:17351128,
CC ECO:0000269|PubMed:18490357}.
CC -!- SUBUNIT: Interacts with CTNNB1 (By similarity). Interacts with KATNB1.
CC Also interacts with gamma-tubulin and KIF23. {ECO:0000250,
CC ECO:0000269|PubMed:17351128, ECO:0000269|PubMed:18490357}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Preferentially localized to the
CC mother centriole. Also localized to the midbody in cells undergoing
CC cytokinesis. Within neurons, enriched in cell bodies and localized to
CC branch points and the tips of axonal branches.
CC -!- SIMILARITY: Belongs to the LZTS2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03026}.
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DR EMBL; AY928801; AAX28869.1; -; mRNA.
DR EMBL; DQ176638; ABA06435.2; -; mRNA.
DR RefSeq; NP_001014269.2; NM_001014247.2.
DR AlphaFoldDB; Q3LUD4; -.
DR SMR; Q3LUD4; -.
DR STRING; 10116.ENSRNOP00000042095; -.
DR iPTMnet; Q3LUD4; -.
DR PhosphoSitePlus; Q3LUD4; -.
DR PaxDb; Q3LUD4; -.
DR PRIDE; Q3LUD4; -.
DR GeneID; 365468; -.
DR KEGG; rno:365468; -.
DR CTD; 84445; -.
DR RGD; 1359249; Lzts2.
DR eggNOG; ENOG502QWFS; Eukaryota.
DR InParanoid; Q3LUD4; -.
DR PhylomeDB; Q3LUD4; -.
DR PRO; PR:Q3LUD4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0051168; P:nuclear export; IEA:UniProtKB-UniRule.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
DR GO; GO:0060682; P:primary ureteric bud growth; ISO:RGD.
DR GO; GO:0051255; P:spindle midzone assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0072197; P:ureter morphogenesis; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
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..670
FT /note="Leucine zipper putative tumor suppressor 2"
FT /id="PRO_0000367896"
FT REGION 1..333
FT /note="Required for centrosomal localization"
FT /evidence="ECO:0000250"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..670
FT /note="Sufficient for interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 451..670
FT /note="Sufficient for interaction with KATNB1 and for
FT inhibition of katanin-mediated microtubule severing"
FT /evidence="ECO:0000250"
FT COILED 329..650
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
FT MOTIF 632..641
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
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..239
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:0000250|UniProtKB:Q91YU6"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK4"
SQ SEQUENCE 670 AA; 72493 MW; 9637FAA7B631E9A2 CRC64;
MAIVQTLPVP LEPARETATA PQTPAMGSVS SLISGRPCPG GPAPQRHHGV PGPTFFRQQD
GLLRGGYEAQ EPLCPAVPPR KTVPGNSFTY VNEDFRTESP PSPSSDVEDP REHQAHNAHL
RGPPPKLIPV SGKLEKNMEK ILIRPTAFKP VLPKPRGAPS LPGFLGPRAA GLSGSQGSLT
QLFGGPASSS SSSSSSSAAD KPLALSGWAS GCPSGTLSDS GRNSLSSLPT YSTGGAEPTA
NSPGGHLPSH GPGRGPLPGP ARGVPTGPSH SDSGRSSSSK STGSLGARVA GGLLGSGARA
SPGSSSGGDR SPPPPPPPPP SDEALLHCVL EGKLRDREAE LQQLRDSVDE SEAAVCQAFG
ARQRRWPGER EDCASHAQQA TQRVQRAQQL LQLQVFQLQQ EKRQLQDDFA QLLQEREQLE
RRCATFEREQ QELGPRLEET KWEVCQKSGE ISLLKQQLKE SQAELVQKGS ELVALRVALR
EARAALRVSE GHARGLQEAA RARELELEAC SQELQRYRQE AEQLREKARH LDAEAAGLRE
PPVPPATTDP FLLAESDEAK VQRAAAGTGG SLRAQVERLR QELQREQRRG DEQRNSFEGE
RLAWQAEKEQ VIRYQKQLQH NYVQMYRRNR QLEQELQQLS LELEARELAD LGLSEPAPCI
CLEEITATEI
