ID   A0A3B3SQK3_9TELE        Unreviewed;       674 AA.
AC   A0A3B3SQK3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Leucine zipper putative tumor suppressor 2 homolog {ECO:0000256|HAMAP-Rule:MF_03026};
DE   AltName: Full=Protein LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026};
GN   Name=LZTS2 {ECO:0000256|HAMAP-Rule:MF_03026,
GN   ECO:0000313|Ensembl:ENSPKIP00000032605.1};
GN   Synonyms=LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000032605.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000032605.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03026}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03026}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000256|HAMAP-Rule:MF_03026}.
CC   -!- SIMILARITY: Belongs to the LZTS2 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03026}.
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DR   AlphaFoldDB; A0A3B3SQK3; -.
DR   Ensembl; ENSPKIT00000013475.1; ENSPKIP00000032605.1; ENSPKIG00000012642.1.
DR   GeneTree; ENSGT00940000154078; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
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:0030178; P:negative regulation of Wnt signaling pathway; IEA:UniProtKB-UniRule.
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; ZIPPER PUTATIVE TUMOR SUPPRESSOR 2 HOMOLOG-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR19354:SF4; ZIPPER PUTATIVE TUMOR SUPPRESSOR 2-RELATED; 1.
DR   Pfam; PF06818; Fez1; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_03026};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_03026}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_03026};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03026};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP-
KW   Rule:MF_03026};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|HAMAP-
KW   Rule:MF_03026};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|HAMAP-Rule:MF_03026};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|HAMAP-
KW   Rule:MF_03026}.
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          438..528
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT   COILED          577..657
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT   COMPBIAS        178..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  73397 MW;  EF9845C4C5758200 CRC64;
     MALVQALPVP SDPCSSAISA QCPPSPPAPS PPAGAMGSVS SLIAGRSYQE RHSRPGDLGA
     RVRKPTPGTG CFRGGSSTEH LVGHEPPPPG RRQPPPATSD VSSYAYLNED FVGDWNDNLV
     STGGPASDAE DAGDMRVLNG NIGGPPPKLV PVSGKLEKNM EKTVIRPTAF KPVLPKNRNS
     VQYLSPRPGG TLSESQGSLN LLLPVSGGSP GCGEKRGSYS GGRGGGGGGG SQSCATSDSG
     RNSLSSLPTY SSTGYGLGVG EPSVGPPEPV RAAPGHSTSD SGRSSSSKST GSMGGRCRPL
     SDGSSSGVRS PVPAEGYEGV VRDLEDKLRE RELELQQLRE NLDENEAAIC QVYEEKQKRC
     EQELEELRQS CASRMRQASQ RAQRAQQEKK KLQEDFGQLL QEHELLESRC ASIQRQQTQL
     GPRLEETKWE VCQKTGEISL LKQQLKDLQA DLAQRTGEIV TLKAQLREAR AELQAGEARA
     QEARAAARAR TLELEVCENE LQRRKSEAEL LREKASRLEE ETVRLREALG QCSAASPPPG
     RAPVLSPTHR EADERLLACE SDEVKAQRQG CGPGGGTQVL RQQVERLRAE LMLERRRGEE
     QLSTFEGERR VWQEEKEKVI RYQEQLQQNY VQMYRRNREL ERVMRELSLA LESRQLEHAA
     VSKIHFEEIA ATEI
//