LST2_DROAN
ID LST2_DROAN Reviewed; 985 AA.
AC B3MT31;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Lateral signaling target protein 2 homolog;
GN ORFNames=GF22946;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902623; EDV30421.1; -; Genomic_DNA.
DR RefSeq; XP_001964625.2; XM_001964589.2.
DR AlphaFoldDB; B3MT31; -.
DR SMR; B3MT31; -.
DR STRING; 7217.FBpp0126138; -.
DR EnsemblMetazoa; FBtr0383557; FBpp0343678; FBgn0099940.
DR GeneID; 6505595; -.
DR KEGG; dan:6505595; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_0_1; -.
DR InParanoid; B3MT31; -.
DR OMA; DAPRCMA; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; B3MT31; -.
DR Proteomes; UP000007801; 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..985
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378962"
FT ZN_FING 904..964
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 310..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..603
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..892
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 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 985 AA; 108300 MW; 740F75E5E2734F67 CRC64;
MNGSGGRQMQ CGKKADDKSL LARFFHADRS LTAVASELDS FDGRAEPDRC TRLVSKLRLN
QDKVLAITNL IMEELLGEDR DPRAFRAKFP EEVLQENLAG QLWFGAECLA AGSSIMNREA
ESKEMRPLAQ AVTKSLGNVR VLLRDQCLRN NVPNSKTLQL DLNDSTTEQL YESLKIFDRL
FAEFELSYVS AMVQVKSRHE YEMQQWIGVL FSETLQRALK IGLLDQDMVD AFDPGLMFSI
PRLAIVAGLV VYAKGPLNMD MPGDQLSEMF RPFRTILIKI RDLLRNLNHE ELYQLEKVLC
TNEDINAKAP LGSSSIEAPS PEHSSHHPTT SSNNNNNNGD TTGTTNTHRT VERLVDQRNN
NNNNNTSSAP ALDKAANRSP SMLSLSPNST PTASPAPSPT PSHSIASTSS SATGSTHPPA
DWSDGDDEDE EDDDDDIEVE EEELDSTDDE TDEEQLLKDI VAADCASGYL IPNTNLGNLL
QPQEVPLTDN FVASEDDEYG AGEQQRQRHR DGQEDEPSTS AAMLAASRTL QRLRLPSSDA
EPLAEQSTIK TPEQEQDQPH QSVYRHRHSH RHHHRHHHHH HQRHHHHQHQ QPPQPHPHRT
TRSGRKRCSL DSTESEATQP ERDREPSQAS GDTSAASSLS DDVSLAMRNT TARLKFKSTE
NLLHRLFVCI AGVADQLQTN FASDLRQILR SVFLMNMSSA QEEIDIPEKT KESELFEFRA
SENDVIQESA GSNQSIYSAE EVNPELDNVF SAGSGGGSPG NGNQANASAQ RHSAGGSIQR
NNTVDDGSPT GGGALLATSR SHVMRSRSLG DQESASTSTS SSQLHQEQQQ LQIQVQRQRN
NSVGSNTPSS ASSTSSSSEQ NSPVSARSGS RRRLQSNNET QMPSSATVTT TATATLAPPA
WIPDGKAPRC MSCQTPFTAF RRRHHCRNCG GVFCGVCSNA SAPLPKYGLT KAVRVCRECY
VREVRSGMSV QGVPSVQERL TATAS
