ID A0A1S3A6W7_ERIEU Unreviewed; 672 AA.
AC A0A1S3A6W7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_007530348.1, ECO:0000313|RefSeq:XP_007530349.1,
GN ECO:0000313|RefSeq:XP_007530350.1};
GN Synonyms=LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007530348.1};
RN [1] {ECO:0000313|RefSeq:XP_007530348.1, ECO:0000313|RefSeq:XP_007530349.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007530348.1; XM_007530286.2.
DR RefSeq; XP_007530349.1; XM_007530287.2.
DR RefSeq; XP_007530350.1; XM_007530288.2.
DR STRING; 9365.ENSEEUP00000010386; -.
DR GeneID; 103119947; -.
DR CTD; 84445; -.
DR eggNOG; ENOG502QWFS; Eukaryota.
DR OrthoDB; 5394101at2759; -.
DR Proteomes; UP000079721; 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.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 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 Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|HAMAP-
KW Rule:MF_03026}.
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..473
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COILED 509..536
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COILED 575..651
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT MOTIF 634..643
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..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..246
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 308..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 73087 MW; 3610A84F4079BB05 CRC64;
MAIVQTLPVP LEPTPEAATA PQAPAMGSVS SLISGRPCPG GSASTRHHGP PGPTFFRQQD
GLLRGGYEAQ EPLCPAVPPR KAVPGTSFTY INEDFRTETP PSPGSDMEDP REQRARNAHL
RGPPPKLIPV SGKLEKNMEK ILIRPTAFKP VLPKPRGAPS LPSFLGPRAT GLSGSQGSLT
QLFGGPASSS SSSSSSATDK PLALSAWANG CPSGTLSDSG RNSLSSLPTY STGGAEPATN
SPGGHLSSHG PGRGVLPGPA RGAPTGPSHS DSGRSSSSKS TGSLGGRVAG GLLGSGPQTS
PDSSSCGERS PLPPPPPPPP PPSDEALLHC VLEGKLRDRE AELQQLRDSL DESEVPVCQV
YEERQLHWQR EREALREDST AQAQRAQRAQ QLLQLQVFQL QQEKRQLQDD FAQLLQEREQ
LERRCATFER EQQELGPRLE ETKWEVCQKS GEISLLKQQL KESQAELVQK GSELVALRVA
LREARAALRV SEGRARGLQE AARTRELELE TCSHELQRHR QEAERLREKA GQLDQEAAGL
REPARAVAAA DPFLLAESDE AKAQRAAAGV GGSLRAQVER LRMELQCERR RGEEQRDSFE
GERLAWQAEK EQVIRYQKQL QHNYIQMYRR NRQLEQELQQ LSLELEAREL ADLGLAEPAP
CICLEEITAT EI
//
