LST2_DROWI
ID LST2_DROWI Reviewed; 993 AA.
AC B4NFJ7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Lateral signaling target protein 2 homolog;
GN ORFNames=GK22512;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH964251; EDW83064.1; -; Genomic_DNA.
DR RefSeq; XP_002072078.2; XM_002072042.2.
DR AlphaFoldDB; B4NFJ7; -.
DR SMR; B4NFJ7; -.
DR STRING; 7260.FBpp0251655; -.
DR EnsemblMetazoa; FBtr0420570; FBpp0378686; FBgn0224489.
DR GeneID; 6649397; -.
DR KEGG; dwi:6649397; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_0_1; -.
DR InParanoid; B4NFJ7; -.
DR OMA; DAPRCMA; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; B4NFJ7; -.
DR Proteomes; UP000007798; 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..993
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378970"
FT ZN_FING 905..965
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 340..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..604
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 927
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 930
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 935
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 938
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 957
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 993 AA; 108641 MW; FC944CFC08F923F7 CRC64;
MCDDGAVCAA TAAANADDKS LLARFYHADR SLTAVASELD SFDGRAEPDR CSRLVSRLRQ
NQDKVLAITN LIMEELLGED RDPRAFRAKF PEEVLQENLA GQLWFGAECL AAGSSILNRE
TESKEMRPLA QAVTKSLGNV RVLLRDQCLR NNVPNSKTLH LDFNDCTTEQ LYESLKIFDR
LFAEFELSYV SAMVQVKSRH EYEMQQWIGV LFSETLQRAL KMGLLDQEMV DAFDPGLMFS
IPRLAIVAGL VVYNKGPLNM DMPGDQLSEM FRPFRTILIK IRDLLRNLNQ QELYQLEKLL
CTNEDINTKA PLGSSSIEAP SQQDYSTANT HRTLERLTVD QRNNNNNINN NSSSSSNSNS
GAPSVQEDAN HRSPSMLSLS TASPTPSHSI GSTFSAATSS TNPPVNWSDG DDADDDDDGD
DDDEDDDDDV DDDLVGNDDS DDDDDDTTDE HLLDDIVAAD CASGYLIPNT NLGNLLQPQQ
VTLTDNFVAS DDDDGYGQVA AGAGNDEEPS TSAATRHMQR LHLPSSDSYG DADGSHNNTT
TIKSPDSDGQ QQHQQHTSSR QRHSHHHHRH HHHHHRHSSH SSHSHHHQHQ QHHSQPHPHR
TTRSGRKRCS LESPTDVDVT VVQPEPEPEL VSASADNSTA SSLSDDISLA MRNTTARLKF
KSTENLLHRL FVCIAGVADQ LQTNFASDLR QILRSVFLMN VSSSQEEIDD IPEKTKESEL
FEFRASENDV IQESAGSNQS IYSAEEVNPE LDNVFSASGA RHSAGASMQR NHTTIDNNNS
TSSSPPDATI TTTTTTTTTR SHVTRSRSLG DQEVVASAAA AAAAAVNEER EMQRQRNNSV
GSNTPSSASS SATSSSSEQN SPVSMRSGTG RRRHQSNNET QMPTTATTTT TTGTGTLAPP
AWIPDGKAPR CMSCQTPFTA FRRRHHCRNC GGVFCGVCSN ASAPLPKYGL TKAVRVCRDC
YAREIRSSGG GGGGVVQMQR QQAANRPQTA SAS
