LST2_DROVI
ID LST2_DROVI Reviewed; 1052 AA.
AC B4M140;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Lateral signaling target protein 2 homolog;
GN ORFNames=GJ23073;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR)
CC signaling. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lst-2 family. {ECO:0000305}.
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DR EMBL; CH940650; EDW67451.1; -; Genomic_DNA.
DR RefSeq; XP_002053931.1; XM_002053895.2.
DR AlphaFoldDB; B4M140; -.
DR SMR; B4M140; -.
DR STRING; 7244.FBpp0237490; -.
DR EnsemblMetazoa; FBtr0238998; FBpp0237490; FBgn0210175.
DR GeneID; 6630849; -.
DR KEGG; dvi:6630849; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_0_1; -.
DR InParanoid; B4M140; -.
DR OMA; DAPRCMA; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; B4M140; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1052
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378969"
FT ZN_FING 972..1032
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 311..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..614
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 994
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 997
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1002
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1005
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1052 AA; 115891 MW; 324DCD3CC03D7EAD CRC64;
MDTFRKWLNK PKADDKSLLA RFYHADRSLT AVASELDSFD GRAEPDRCTR LVSRLRQNQD
KVLAITNLIM EELLGEERDP RAFRAKFPEE VLQENLAGQL WFGAECLAAG SSILNRESES
KEMRPLAQAV TKSLSNVRVL LRDQCLRNNV PNSKTLHLDF NDSTTEQLYE SLKIFDHLFA
EFELSYVSAM VQVKSRHEYE MQQWIGVLFS ETLQRALKIG LLDQDMVDAF DPGLMFSIPR
LAIVAGLVIY AKGPLNMDMP GDELSEMFRP FRTILIKIRD LLRNLSKQEL YQLEKLLCTN
EEINTKVPLG YSSIEAPSPE PNSSNNHNNN NSNSSDSGSA KTSTTSPHKA VERLVDHRNN
NNSSSCSASA ATQAVARSPS MLSLSAGSTP TASPAPSPTP SHSIASTSSA ATTSTNPPAN
WSEDDDDDDE EREDDEEECG MLDSDEQDLN DDSDSDVDEY IEAQLKAIVA AADCASGYLI
PNTNLGNLLQ PQTAPLTDNF VASEDDEFGA EQEQEQQQRQ REEQLQPSSE QQEEPSTSAA
MLAARRTLQR LRLPSSSSEN EQTTGSNQQS TIKTPNGGGQ PMRSGSQRQR HHSHHHHHRH
HHHHHHHRQH HHQQQHQPAQ AEQHSHHHHH QTHPHRTSRS ARKRCSQEHW ESTTAEQQQT
IDHGHGLASA DTSNASSFSD DVSLAMRNTT ARLKFKSTEN LLHRLFVCIA GVADQLQTNF
ASDLRQILRS VFLINMSSSQ EDIDIPEKTK ESELFEFRAS ENDVIQESAG SNQSIYSAEE
VNPELDNVFN MGNGNGGGTN AARHSAGAAM QRNNTIDLSG GGYNNNNNNN NNSGSSSSSN
SSTVARSHVA RSRSLGDQEA ATSGTLQEEQ RQQQQQQQAQ LQLQMQRQRN NSVGSNSPSS
SSSSSSSSEH NSPISTRSGS RRRLHSNSAS MPSIGSTATT AAATAAATAT TTTSATTTTT
TTTMSPPAWI PDGKAPRCMS CQTPFTAFRR RHHCRNCGGV FCGVCSNASA PLPKYGLTKA
VRVCRECYVR EVRSSRTQAH SQASRPQAAS AS
