LZTS1_MOUSE
ID LZTS1_MOUSE Reviewed; 599 AA.
AC P60853; B2RTI1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Leucine zipper putative tumor suppressor 1;
DE AltName: Full=F37/Esophageal cancer-related gene-coding leucine-zipper motif;
DE AltName: Full=Fez1;
GN Name=Lzts1; Synonyms=Fez1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/J;
RX PubMed=10097140; DOI=10.1073/pnas.96.7.3928;
RA Ishii H., Baffa R., Numata S., Murakumo Y., Rattan S., Inoue H., Mori M.,
RA Fidanza V., Alder H., Croce C.M.;
RT "The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein, and its
RT expression is altered in multiple human tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3928-3933(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Involved in the regulation of cell growth. May stabilize the
CC active CDC2-cyclin B1 complex and thereby contribute to the regulation
CC of the cell cycle and the prevention of uncontrolled cell
CC proliferation. May act as tumor suppressor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds EEF1G, TLK2 and CDK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Synapse {ECO:0000250}.
CC Note=Associated with the plasma membrane and with microtubules.
CC Detected in dendritic spines, especially in the postsynaptic density
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residues. Hyperphosphorylated by the
CC cAMP-dependent kinase PKA during cell-cycle progression (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LZTS family. {ECO:0000305}.
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DR EMBL; AF288601; AAQ14349.1; -; mRNA.
DR EMBL; BC139350; AAI39351.1; -; mRNA.
DR EMBL; BC139352; AAI39353.1; -; mRNA.
DR CCDS; CCDS22345.1; -.
DR RefSeq; NP_955396.2; NM_199364.2.
DR RefSeq; XP_006509669.1; XM_006509606.1.
DR RefSeq; XP_006509670.1; XM_006509607.3.
DR RefSeq; XP_006509671.1; XM_006509608.3.
DR AlphaFoldDB; P60853; -.
DR SMR; P60853; -.
DR BioGRID; 229205; 1.
DR IntAct; P60853; 2.
DR MINT; P60853; -.
DR STRING; 10090.ENSMUSP00000139117; -.
DR iPTMnet; P60853; -.
DR PhosphoSitePlus; P60853; -.
DR EPD; P60853; -.
DR MaxQB; P60853; -.
DR PaxDb; P60853; -.
DR PRIDE; P60853; -.
DR ProteomicsDB; 292062; -.
DR Antibodypedia; 1747; 249 antibodies from 27 providers.
DR DNASU; 211134; -.
DR Ensembl; ENSMUST00000037049; ENSMUSP00000039397; ENSMUSG00000036306.
DR Ensembl; ENSMUST00000185176; ENSMUSP00000139117; ENSMUSG00000036306.
DR GeneID; 211134; -.
DR KEGG; mmu:211134; -.
DR UCSC; uc009lxa.1; mouse.
DR CTD; 11178; -.
DR MGI; MGI:2684762; Lzts1.
DR VEuPathDB; HostDB:ENSMUSG00000036306; -.
DR eggNOG; ENOG502QRU7; Eukaryota.
DR GeneTree; ENSGT00940000154078; -.
DR HOGENOM; CLU_026379_2_1_1; -.
DR InParanoid; P60853; -.
DR OMA; LEPKCNS; -.
DR OrthoDB; 1014871at2759; -.
DR PhylomeDB; P60853; -.
DR TreeFam; TF331420; -.
DR BioGRID-ORCS; 211134; 5 hits in 74 CRISPR screens.
DR PRO; PR:P60853; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P60853; protein.
DR Bgee; ENSMUSG00000036306; Expressed in olfactory tubercle and 163 other tissues.
DR Genevisible; P60853; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:MGI.
DR InterPro; IPR045329; LZTS.
DR InterPro; IPR033293; LZTS1.
DR PANTHER; PTHR19354; PTHR19354; 1.
DR PANTHER; PTHR19354:SF5; PTHR19354:SF5; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Lipoprotein; Membrane; Myristate; Reference proteome; Synapse;
KW Tumor suppressor.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..599
FT /note="Leucine zipper putative tumor suppressor 1"
FT /id="PRO_0000182972"
FT REGION 135..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..572
FT /evidence="ECO:0000255"
FT COMPBIAS 171..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CONFLICT 90
FT /note="I -> M (in Ref. 1; AAQ14349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 67290 MW; 7B77A3BCF249E817 CRC64;
MGSVSSLISG HSFHSKHCRA SQYKLRKSSH LKKLNRYSDG LLRFGFSQDS GRGKSSSKMG
KSEDFFYIKV SQKARGSHRP DYTALSSGDI GGQTGVDFDP ATPPKLMPFS NQLEMSSDKG
AVRPTAFKPV LPRSGAILHS SPESTSHQLH PMPPDKPKEQ ELKPGLCSGA LSDSGRNSMS
SLPTHSTTSS YQLDPLVTPV GPTSRFGGSA HNITQGIILQ DSNMMSLKAL SFSDGGSKLA
HPGKADKGAS CVRSPLSTDE CTIQELEQKL LQRETALQKL QRSFDEKEFA SGQTFEERPR
RTRDELECLE PKSKLKPPSQ KSQRTQQVLQ LQVLQLQQEK RQLRQELESL MKEQDLLETK
LRSYEREKTN FAPALEETQW EVCQKSGEIS LLKQQLKESQ LEVNTKASEI LSLKAQLKDT
RGKLDGMELK TQDLESALRT KGLELEVCEN ELQRKKNEAE LLREKVNLLE QELMELRAQA
ALHPAPLGPP GVGLTFSEDI PALQRELDRL RAELKEERQG HDQMSSGFQH ERLVWKEEKE
KVIQYQRQLQ QSYLAMYQRN QRLEKALQQL ARGDGPGEPF EIDLEGADIP YEDIIATEI
