LST2_CAEEL
ID LST2_CAEEL Reviewed; 661 AA.
AC Q9TZD0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Lateral signaling target protein 2;
GN Name=lst-2; ORFNames=R160.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14752159; DOI=10.1126/science.1091639;
RA Yoo A.S., Bais C., Greenwald I.;
RT "Crosstalk between the EGFR and LIN-12/Notch pathways in C. elegans vulval
RT development.";
RL Science 303:663-666(2004).
CC -!- FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR)
CC signaling. {ECO:0000250, ECO:0000269|PubMed:14752159}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval precursor cells (VPCs).
CC {ECO:0000269|PubMed:14752159}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in all 6 vulval precursor cells
CC (VPCs). At the time of inductive signaling, expression forms a gradient
CC in response to inductive signal: expression is low in P6.p,
CC intermediate in P5.p and P7.p and undiminished in P3.p, P4.p, and P8.p.
CC Later, expression becomes strong again in P5.p and P7.p.
CC {ECO:0000269|PubMed:14752159}.
CC -!- DISRUPTION PHENOTYPE: Causes ectopic vulval induction.
CC {ECO:0000269|PubMed:14752159}.
CC -!- SIMILARITY: Belongs to the lst-2 family. {ECO:0000305}.
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DR EMBL; FO081006; CCD68425.1; -; Genomic_DNA.
DR PIR; T33568; T33568.
DR RefSeq; NP_508756.2; NM_076355.5.
DR AlphaFoldDB; Q9TZD0; -.
DR SMR; Q9TZD0; -.
DR STRING; 6239.R160.7; -.
DR EPD; Q9TZD0; -.
DR PaxDb; Q9TZD0; -.
DR PeptideAtlas; Q9TZD0; -.
DR EnsemblMetazoa; R160.7.1; R160.7.1; WBGene00003084.
DR GeneID; 180712; -.
DR KEGG; cel:CELE_R160.7; -.
DR UCSC; R160.7; c. elegans.
DR CTD; 180712; -.
DR WormBase; R160.7; CE33815; WBGene00003084; lst-2.
DR eggNOG; KOG1819; Eukaryota.
DR GeneTree; ENSGT00940000171484; -.
DR HOGENOM; CLU_007360_1_1_1; -.
DR InParanoid; Q9TZD0; -.
DR OMA; NLSEMFR; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; Q9TZD0; -.
DR PRO; PR:Q9TZD0; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003084; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:WormBase.
DR CDD; cd15731; FYVE_LST2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043269; FYVE_LST2.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..661
FT /note="Lateral signaling target protein 2"
FT /id="PRO_0000378957"
FT ZN_FING 566..626
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 294..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 661 AA; 74526 MW; 9B2CFF7FD13B0E23 CRC64;
MQSFRKIWNK PRPDDWMPLA RFYYADSALN DIASELDSFD GRRDPDRCNA LVTRLRVAQD
RVLHIITEML IHLYPREQDR ACRDFRVKFP DEILHDTLPG QLWFGAECLS AGSNIIDHET
ESDLIRPLAK DVTKQLDFLR DLLKNQSLRD PSAYNPVIKE NLLKFDKLFA EFEYQYVSAM
VPVKSVKEHD SQLDVAVLFS EVLSLALVKD LITQDLIDYC DPSVMIAIPR LGIVWGLLVY
SNGALNVDVP AENLSEMFRP FYSLLVKIRN LLRILTPTEL TKLETVLCKG ESAVPEDTSS
TLTMSDFRTN ATDEEKAKNN QRVWMCDMPS DSTSSLDSSV QDSSSETTSL ASSALASPHS
GSEENVSQIE NEEGDDEAIG TNSNSSNEVT ESPETIEEPD NVDMEESSES EVDTHIDETR
NESDDEITDD VQASDVLQVE TKKCKSSRLL EQKKFDKSVK TIIPMQTDPR SQIDPKNLRS
RFRSSEDLVH RLFVCIAGVA DQLQTNYSSE IRKVLKLILQ PSEIIPVYEV VNAQVANSQT
EGEETGVEAQ ETLPLPAFMG VRWVPDEDCE QCTACSMPFN FVRRRHHCRN CGRIFCHKCS
CNTISIPEHG YDRKVRVCNL CYVHRLNSFG CNEPMSQVNE NGATVPSVTE QQSAQTASAS
S
