LZTS2_BOVIN
ID LZTS2_BOVIN Reviewed; 667 AA.
AC A5PKL7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 {ECO:0000255|HAMAP-Rule:MF_03026};
GN Synonyms=LAPSER1 {ECO:0000255|HAMAP-Rule:MF_03026};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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. 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}.
CC -!- SUBUNIT: Interacts with KATNB1. Also interacts with CTNNB1, gamma-
CC tubulin and KIF23. {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}. Note=Localized to the centrosome
CC throughout the cell cycle. Localized to the midbody in cells undergoing
CC cytokinesis. {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; BC142533; AAI42534.1; -; mRNA.
DR RefSeq; NP_001092332.1; NM_001098862.2.
DR AlphaFoldDB; A5PKL7; -.
DR SMR; A5PKL7; -.
DR STRING; 9913.ENSBTAP00000004268; -.
DR PaxDb; A5PKL7; -.
DR PRIDE; A5PKL7; -.
DR GeneID; 504411; -.
DR KEGG; bta:504411; -.
DR CTD; 84445; -.
DR eggNOG; ENOG502QWFS; Eukaryota.
DR InParanoid; A5PKL7; -.
DR OrthoDB; 1014871at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..667
FT /note="Leucine zipper putative tumor suppressor 2"
FT /id="PRO_0000367895"
FT REGION 1..333
FT /note="Required for centrosomal localization"
FT /evidence="ECO:0000250"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..667
FT /note="Sufficient for interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 448..667
FT /note="Sufficient for interaction with KATNB1 and for
FT inhibition of katanin-mediated microtubule severing"
FT /evidence="ECO:0000250"
FT REGION 516..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 329..647
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
FT MOTIF 629..638
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03026"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YU6"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YU6"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK4"
SQ SEQUENCE 667 AA; 72466 MW; 3BB7C3B4CEE85564 CRC64;
MAIVQTLPVP LEPAPEAATA QQAPAMGSVS SLISGRPCPG GPAPPRHHGP PGPTFFRQQD
GLLRGGYEAQ EPLCPAVPPR KAVPGTNFTY INEDFRTESP PSPSSDLEDA REQRARNAHL
RGPPPKLIPV SGKLEKNMEK IVIRPTAFKP VLPKPRGVPS LPSFLGPRAT GPSGSQGSLT
QLFGGPASSS SSSSSSAADK PLILSGWASG CPSGTLSDSG RNSLSSLPTY STGGAEPATN
SPGGHLPSHG PGRGALPGPA RGAPTGPSHS DSGRSSSSKS TGSLGGRLAG GLLGSGPRAS
PDSSSCGERS PPPPPPPPPP SDEALLHCVL EGKLRDREAE LQQLRDSLDE SEVTMCQVYE
ERQRHWPRER EALREDGVAR AQRAQQLLQL QVFQLQQEKR QLQDDFAQLL QEREQLERRC
AAFEREQREL GPRLEETKWE VCQKSGEISL LKQQLKESQS ELVQKGSELV ALRVALREAR
AALRVSEGRA RGLQEAARTR ELELEACSQE LQRHRQEAER LREKAGQLDS EAAGLREPPV
PPATADPFLL AESDEAKAQR AAAGVGGSLR AQVERLRAEL QRERRQGEEQ RDSFEGERLA
WQAEKEQVIR YQKQLQHNYI QMYRRNRQLE QELQQLSLEL EARELADLGL AEPAPCICLE
EITATEI
