ID A0A1S3T1G2_SALSA Unreviewed; 801 AA.
AC A0A1S3T1G2;
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 homolog {ECO:0000256|HAMAP-Rule:MF_03026};
DE AltName: Full=Protein LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026};
GN Name=LOC106613059 {ECO:0000313|RefSeq:XP_014070417.1,
GN ECO:0000313|RefSeq:XP_014070425.1};
GN Synonyms=LAPSER1 {ECO:0000256|HAMAP-Rule:MF_03026}, LZTS2
GN {ECO:0000256|HAMAP-Rule:MF_03026};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014070417.1};
RN [1] {ECO:0000313|RefSeq:XP_014070417.1, ECO:0000313|RefSeq:XP_014070425.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014070417.1,
RC ECO:0000313|RefSeq:XP_014070425.1};
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. 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 RefSeq; XP_014070417.1; XM_014214942.1.
DR RefSeq; XP_014070425.1; XM_014214950.1.
DR STRING; 8030.ENSSSAP00000000216; -.
DR PaxDb; 8030-ENSSSAP00000000216; -.
DR GeneID; 106613059; -.
DR KEGG; sasa:106613059; -.
DR OrthoDB; 5394101at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
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 Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|HAMAP-
KW Rule:MF_03026}.
FT REGION 110..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 409..627
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03026"
FT COMPBIAS 279..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 87225 MW; 772A5E402DB67ECB CRC64;
MALVQTLPVS TTDHPKPPTS LNIVSLSPVV GGPCGPCGPG ATMGSVSSLI SGRTYQEQRH
CRAASEFSTK TRHNTPTTSC FRLQGDSNTL HSASSLEQLL VINNQTQIQT TQLQPPPLPT
KKQPRSGNSA GGTGCAAGGG VGAGNGNYGF VTEVVTVGDW NDNHVVAIGS PCSDSEEQRD
NRGLNGNIGG PPPKLIPVSG KLEKNMEKFL IRPTAFKPVV PKNRHSVQYL SPRPGGSLSE
SQGSLNLLLP LPINGNNGNT VVNSPGSYGN VVSLLCSSSD SKRNSYSGGR NARSSQSCSM
SDSGRNSLSS LPTHSSTGYS LAHSEASGSG GSGVGLEPGA GRTTTTNGGG SVTHGVHSHS
TSHGHSNSDS GRSSSSKSTG SLSGRGQPLS DSGSCGHSPP PLEGCEGVMR ELEEKLRERD
LELQQLRENL DENEAAICQV YEEKQRRCER ELEEMRQSCS SKMKQATQKA QRVQQALQLQ
VFQLQQEKKK LQEDFSSLLQ DREVLERRCA SIQREQIQLG PRLEETKWEV CQKSGEISLL
KQQLKEIQSE LSQKGGELVV LKSQLREART DLQNSQARSQ EAGSALRTRS LELEVCENEL
QRRKSEAELL REKVIRLEEE LAQLRGALAN QGGGYLPGGQ APANKGQCMS LPLPQGRGGV
EGGKGGPSPS TGYREAEEGR LVWGGESDEA KTQRLSAEAV LGLRQQVERL RAELMYERRS
SEEQLGGFEE ERRVWQEEKE KVIRYQKQLQ QNYIQMYRRN RDLERVMREL SLELENRDIE
DYDIQSGSND IHFEEMTATE I
//
