ID H9Z0S2_MACMU Unreviewed; 669 AA.
AC H9Z0S2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
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|EMBL:AFH29538.1};
GN Synonyms=LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH29538.1};
RN [1] {ECO:0000313|EMBL:AFH29538.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFH29538.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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; JU472734; AFH29538.1; -; mRNA.
DR AlphaFoldDB; H9Z0S2; -.
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 2: Evidence at transcript level;
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..78
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..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..470
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COILED 499..533
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COILED 572..648
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT MOTIF 631..640
FT /note="Nuclear export signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..247
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..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 72789 MW; 21FE92D83E65713D CRC64;
MAIVQTLPVP LEPAPEAATA PQAPAMGSVS SLISGRPCPG GPAPPRHHGP PGPTFFRQQD
GLLRGGYEAQ EPLCPAVPPR KAVPVTSFTY INEDFRTESP PSPSSDVEDA REQRAHNAHL
RGPPPKLIPV SGKLEKNMEK ILIRPTAFKP VLPKPRGAPS LPSFMGPRAT GLSGSQGSLT
QLFGGPASSS SSSSSSSAAD KPLAFSGWAS GCPSGTLSDS GRNSLSSLPT YSTGGAEPTT
SSPGGHLPSH GSGRGALPGP ARGVPTGPSH SDSGRSSSSK STGSLGGRVA AGLLGSGTRA
SPDSSSCGER SPPPPPPPPS DEALLHCVLE GKLREREAEL QQLRDSLDEN EATMCQAYEE
RQRHWQRERE ALREDCAAQA QRAQRAQQLL QLQVFQLQQE KRQLQDDFAQ LLQEREQLER
RCATLEREQR ELGPRLEETK WEVCQKSGEI SLLKQQLKES QAELVQKGSE LVALRVALRE
ARATLRVSEG RARGLQEAAR ARELELEACS QELQRHRQEA ERLREKAGQL DAEAAGLREP
AVPPATADPF LLAESDEAKV QRAAAGIGGS LRAQVERLRV ELQRERRRGE EQRDSFEGER
LAWQAEKEQV IRYQKQLQHN YIQMYRRNRQ LEQELQQLSL ELEARELAEL GLAEQAPCIC
LEEITATEI
//
