LST2_DROER
ID LST2_DROER Reviewed; 981 AA.
AC B3P851;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Lateral signaling target protein 2 homolog;
GN ORFNames=GG12136;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954182; EDV53455.1; -; Genomic_DNA.
DR RefSeq; XP_001981585.1; XM_001981549.2.
DR AlphaFoldDB; B3P851; -.
DR SMR; B3P851; -.
DR STRING; 7220.FBpp0130682; -.
DR EnsemblMetazoa; FBtr0132190; FBpp0130682; FBgn0104428.
DR GeneID; 6554807; -.
DR KEGG; der:6554807; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_0_1; -.
DR OMA; DAPRCMA; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; B3P851; -.
DR Proteomes; UP000008711; 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; Zinc; Zinc-finger.
FT CHAIN 1..981
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378963"
FT ZN_FING 901..961
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 561..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..897
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..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 573..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..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
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 923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 931
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 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 981 AA; 108102 MW; A835D3306CD0E86C 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 HSSSSTTTTT MGTTNTHRTV
ERLVDQRNNN HNSNSNSSTN PTVEGATLRS PSMLSLSATS TPTASPAPSP TPSHSIDSTS
SAATSSTNPP ADWSDGDDED EDDDDIEVDE EDLESSDDDT DEEQLLKDIV AADCASGYLI
PNTNLGNLLQ PQEVPLTDNF VASEDDEYGT AEQQGHQGLE EEEPSTSAAM LAATRTLQRL
RLPSSDTEPL AEPTTIKATE EQMQQPNGRH QESHSHSHRH HQRHHHHHHH RHSHQHRQPH
PHRTTRSGRK RCSLEVADPE TIQPEREQNL ASGDTSAASS LSDDVSLAMR NTTARLKFKS
TENLLHRLFV CIAGVADQLQ TNFASDLRQI LRSVFLMNMS SAQEEIDIPE KTKESELFEF
RASENDVIQE SAGSNQSIYS AEEVNPELDN VFSAGGGNQA TGQRHSAGAS MQRNNTIDLA
SQSGEGSPSG ATMSTSRSHV TRSRSLGDQE AASSATSSTA QLRQQEQQQQ LQIQLQRQRN
NSVGSNTPSS ASSTSSSSEQ NSPVSARSGS RRRLQSNNET QMPSSATSTS ATLSPPAWIP
DGKAPRCMAC QTPFTAFRRR HHCRNCGGVF CGVCSNASAP LPKYGLTKAV RVCRDCYVRE
VRSGMGVQGV QRVQSVQASA S
