LST2_DROYA
ID LST2_DROYA Reviewed; 984 AA.
AC B4PRU6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Lateral signaling target protein 2 homolog;
GN ORFNames=GE10583;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000160; EDW98539.1; -; Genomic_DNA.
DR RefSeq; XP_002098827.1; XM_002098791.2.
DR AlphaFoldDB; B4PRU6; -.
DR SMR; B4PRU6; -.
DR STRING; 7245.FBpp0255593; -.
DR EnsemblMetazoa; FBtr0257101; FBpp0255593; FBgn0228438.
DR GeneID; 6538300; -.
DR KEGG; dya:Dyak_GE10583; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_0_1; -.
DR OMA; DAPRCMA; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; B4PRU6; -.
DR Proteomes; UP000002282; Chromosome 3R.
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; Zinc; Zinc-finger.
FT CHAIN 1..984
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378971"
FT ZN_FING 904..964
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 308..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..607
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 913
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 926
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 929
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 934
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 937
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 956
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 959
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 984 AA; 108548 MW; A8106ED0E2FBD0C4 CRC64;
MDTFKRWLNK PKADDKSLLA RFFHADRSLT AVASELDSFD GRAEPDRCTR LVSRLRQNQD
KVLAITNLIM EELLGEDRDP RAFRAKFPEE VLQENLAGQL WFGAECLAAG SSIMNRETES
KEMRPLAQAV TKSLGNVRVL LRDQCLKNNV PNSKTLHLDL NDSTTEQLYE SLKIFDRLFA
EFELSYVSAM VQVKSRHEYE MQQWIGVLFS ETLQRALKIG LLDQEMVDAF DPGLMFSIPR
LAIVAGLVVY AKGPLNMDMP GDQLSEMFRP FRTILIKIRD LLRNLNNQEL YQLEKLLCTN
EDINTKVPLG SSSIEAPSPE HSAHPTTSSS QNNNNSSNNN HSSSSSTTTT MGTTSTHRTV
ERLVDQRNNN HNSNSNSSTN PTVEGATLRS PSMLSLSPTS TPTASPAPSP TPSHSIASTS
SAATSSTNPP ADWSDGDDED EDDDDIEVDE EDLESSDDDT DEEQLLKDIV AADCASGYLI
PNTNLGNLLQ PQEVPLTDNF VASEDDEYGT TEQQGHQGLE EEEPSTSAAM LAATRTLQRL
RLPSSDTEPL AEPTTIKATE EHMQQPSGRH RESHSHRHHQ RHHHHHHHRH SHQHQHRQPH
PHRTTRSGRK RCSLEAVDPE TIQPEREQNL ASGDTSAASS LSDDVSLAMR NTTARLKFKS
TENLLHRLFV CIAGVADQLQ TNFASDLRQI LRSVFLMNMS SAQEEIDIPE KTKESELFEF
RASENDVIQE SAGSNQSIYS AEEVNPELDN VFSAGGGNQA TGQRHSAGAS MQRNNTIDLA
NQPGEGSPSG ATMATSRSHV TRSRSLGDQE AASSATSSTA HLRQQEQQQQ HQQLQIQLQR
QRNNSVGSNT PSSASSTSSS SEQNSPVSAR SGSRRRLQSN NETQMPSSAT STSATLSPPA
WIPDGKAPRC MACQTPFTAF RRRHHCRNCG GVFCGVCSNA SAPLPKYGLT KAVRVCRDCY
VREVRSGMGV QGVQRVQSVQ ASAS
