ID M3YZS2_MUSPF Unreviewed; 670 AA.
AC M3YZS2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Leucine zipper putative tumor suppressor 2 {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:ENSMPUP00000016833.1};
GN Synonyms=LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000016833.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000016833.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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. 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:0000256|HAMAP-Rule:MF_03026}.
CC -!- SUBUNIT: Interacts with KATNB1. Also interacts with CTNNB1, gamma-
CC tubulin and KIF23. {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}. Note=Localized to the centrosome
CC throughout the cell cycle. Localized to the midbody in cells undergoing
CC cytokinesis. {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 EMBL; AEYP01026094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YZS2; -.
DR STRING; 9669.ENSMPUP00000016833; -.
DR Ensembl; ENSMPUT00000017082.1; ENSMPUP00000016833.1; ENSMPUG00000016937.1.
DR eggNOG; ENOG502QWFS; Eukaryota.
DR GeneTree; ENSGT00940000154078; -.
DR HOGENOM; CLU_026379_2_0_1; -.
DR InParanoid; M3YZS2; -.
DR OMA; LQHSYIQ; -.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0051168; P:nuclear export; IEA:UniProtKB-UniRule.
DR GO; GO:0060682; P:primary ureteric bud growth; IEA:Ensembl.
DR GO; GO:0051255; P:spindle midzone assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0072197; P:ureter morphogenesis; IEA:Ensembl.
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..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 382..472
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COILED 570..650
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT MOTIF 633..642
FT /note="Nuclear export signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 72636 MW; 253958B1A62B093D CRC64;
SVAMAIVQTL PVPLEPAPEA TTAPQAAAMG SVSSLISGRP CPGGPAPPRH HGPPGPTFFR
QQDGLLRGGY EAQEPLCPAV PPRKAVPATS FTYINEDFWA ESPPSPSSDI EDAREQRARS
AHLRGPPPKL IPVSGKLEKN MEKILIRPTA FKPVLPKPRG APSLPSFLGP RAAGLSGSQG
SLTQLFGGPA SSSSSSSSSA ADKPLALSGW ASGCPSGTLS DSGRNSLSSL PTYSTGGAEP
ASHSPGGHLP SHGPGRGALP GPARGAPTGP SHSDSGRSSS SKSTGSLGGR VAGGLLGSGT
RASPDSSSCG ERSPPPPPPP PSDEALLHSV LEGKLHDREA ELQQLRDSLD ESEVTMCQAY
EERQRHWPRE RETLRDDSTA QAQRAQRAQQ LLQLQVFQLQ QEKRQLQDDF AQLLQEREQL
ERRCATFERE QRELGPRLEE TKWEVCQKSG EISLLKQQLK ESQAELVQKG SELVALRVAL
REARAALRVS EGRARGLQEA ARARELELEA CSQELQRHRQ EAERLREKAG QLDTEAAGLR
EPPGPPTTTD PFLLAESDEA KAQRAASGVG GSLRAQVERL RAELQRERRR GEEQRDSFEG
ERLAWQAEKE QVIRYQKQLQ HNYVQMYRRN RQLEQELQQL SLELEARELA DLGLAEPAPC
ICLEEITATE
//
