ID   LZTS2_XENTR             Reviewed;         683 AA.
AC   Q6DIS8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Leucine zipper putative tumor suppressor 2 homolog {ECO:0000255|HAMAP-Rule:MF_03026};
DE   AltName: Full=Protein lapser1 {ECO:0000255|HAMAP-Rule:MF_03026};
GN   Name=lzts2; Synonyms=lapser1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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. Negative regulator of the Wnt
CC       signaling pathway. Represses beta-catenin-mediated transcriptional
CC       activation by promoting the nuclear exclusion of beta-catenin.
CC       {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}.
CC   -!- SIMILARITY: Belongs to the LZTS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03026}.
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DR   EMBL; BC075457; AAH75457.1; -; mRNA.
DR   RefSeq; NP_001006721.1; NM_001006720.1.
DR   RefSeq; XP_012821843.1; XM_012966389.2.
DR   RefSeq; XP_012821845.1; XM_012966391.1.
DR   AlphaFoldDB; Q6DIS8; -.
DR   SMR; Q6DIS8; -.
DR   PaxDb; Q6DIS8; -.
DR   DNASU; 448373; -.
DR   Ensembl; ENSXETT00000033260; ENSXETP00000033260; ENSXETG00000015201.
DR   GeneID; 448373; -.
DR   KEGG; xtr:448373; -.
DR   CTD; 84445; -.
DR   Xenbase; XB-GENE-1216151; lzts2.
DR   eggNOG; ENOG502QWFS; Eukaryota.
DR   HOGENOM; CLU_026379_2_0_1; -.
DR   InParanoid; Q6DIS8; -.
DR   OMA; VTENTMG; -.
DR   OrthoDB; 1014871at2759; -.
DR   PhylomeDB; Q6DIS8; -.
DR   TreeFam; TF331420; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000015201; Expressed in skeletal muscle tissue and 14 other tissues.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-UniRule.
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; IBA:GO_Central.
DR   GO; GO:0051168; P:nuclear export; IEA:UniProtKB-UniRule.
DR   GO; GO:0051255; P:spindle midzone assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..683
FT                   /note="Leucine zipper putative tumor suppressor 2 homolog"
FT                   /id="PRO_0000367898"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          324..665
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
FT   COMPBIAS        11..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  77782 MW;  FF067B134CC9622A CRC64;
     MAALQALPLS IDQNAEVSGS QSHTNTRSPV TENTMGSVSS LISGRTYHDK QCKASELSNK
     CRKPTNMPNC FKQQEGLIKS NYSSQDPLFN GLPTKKPSTT TSGNNGNYVY VNEDFKEEWH
     EPRVPISPSS DAEDIREERA LNGNIRGPPP KLIPVSGKLE KNVEKTLIKP TAFKPVVPKK
     RNSSLQYLVQ RNGGPGLSES QSSLNLLFNG NAAGIPEKHN LLSCRNSTHS GTMSDSGRTS
     LSSLPTYSTN CSHQMDPVSV SMGHINLDNH TNINGYSDRA PRGRTRPTNS DSGRSSSSKS
     TGSLSGRGNP SSDSGSCDRS PILSDEILIR ELEEKLKDRE MELQQLKENL DENEAAICQV
     YEEKQKRCEQ EMEELRQSCA LKMKQAAQKA QRLQQVLQLQ IFQLQQEKKK LQEDFSQLLQ
     ERELLEKRCA SFEREQTEFG PRLEETKWEV CQKSGEISLL KQQLKDSQAE LAQKSNEILL
     LRAQVREARS DLQISEEQVQ ELQDTAHTKT LELEVCENEL QRKKNEAELL REKASKLDQE
     VAGLREAAVA NLRHGLCLCH EKEDPFLLYE SDEAKAQRQN ADNLQGLQQY VERLREALTS
     ERRRYQEQAD SFEDERRIWQ EEKEKVIRYQ KQLQHNYIQM YQQNRELERD IKQLSLELEA
     RELDEFDLHG AEIQFEEITA TEI