LST2_DROMO
ID LST2_DROMO Reviewed; 1051 AA.
AC B4K982;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Lateral signaling target protein 2 homolog;
GN ORFNames=GI24295;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW14495.1; -; Genomic_DNA.
DR RefSeq; XP_001999034.2; XM_001998998.2.
DR AlphaFoldDB; B4K982; -.
DR SMR; B4K982; -.
DR STRING; 7230.FBpp0173512; -.
DR KEGG; dmo:Dmoj_GI24295; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_0_1; -.
DR InParanoid; B4K982; -.
DR OMA; DAPRCMA; -.
DR PhylomeDB; B4K982; -.
DR Proteomes; UP000009192; 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..1051
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378966"
FT ZN_FING 965..1025
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 305..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..637
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..668
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 974
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 987
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 990
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 995
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 998
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1051 AA; 115850 MW; 41B085D3C5A5C93C CRC64;
MFVFIYCLQA DDKSLLARFY HADRSLTAVA SELDSFDGRA EPDRCTRLVS RLRQNQDKVL
AITNLIMEEL LGDERDPRAF RAKFPEEVLQ DNLAGQLWFG AECLAAGSSI LNRESESKEM
RPLAQAVTKS LGNVRVLLRD QCLRNNVPNS KTLHLDFNDS TTEQLYESLK IFDHLFAEFE
LSYVSAMVPV KSRHEYEMQQ WIGVLFSETL QRALKIGLLE QEMVDAFDPG LMFSIPRLAI
VAGLVVFTKG PLNMDMPGDE LSEMFRPFRT ILIKIRDLLR NLSKQELHQL EKLLCTNEEI
NTNVPLGSSS IEAPSPEHNN TSSSTSNNNN NNNNNSSSSS SSSSGSGSNT AKTSTSSTHK
AVERLVDHRN NNSSTVAGAT QPSTARSPSM LSLSAGSTPT ASPAPSPTPS HSIASTSSAA
TTSTNPPANW SDYDEDDEDL EEEVGMLDSD EDDLNDDSDD DIEVDEYIEA QLKAIVAAAD
CASGYLIPNT NLGNLFQAQQ LPLTDNFVAS EDDEFGSNAA TERQQQQQHM DELQPGDQQQ
QQQQLQDEPS TSAAMLAAQR TLQRLHLPSS SSENEQAPSS NQQTTIKTPN GNQSMPNSSS
SSSNHNNNRH RHSHSHSHSS HHHHHHHRHH HHTHPHHQQQ QEQRLQAADH HHHHHHHHQS
HPHRINRSAR KRCSQEHWES TANAEQPAPE QTPGSADTSN ASSFSDEVSL AMRSTTARLK
FKSTENLLHR LFVCIAGVAD QLQTNFASDL RQILRSVFLI NMSSSQDEDI DIPEKTKESE
LFEFRASEND VIQESAGSNQ SIYSAEEVNP ELDNVFNNTN AAVRHSAGAA MQRNNTIDLA
SGNNNGNSNA AARNHVARSR SLGDQEAAGS GTRQDEQRQQ QQQQQQQLQQ QLQMQRQRNN
SVGSNSPSSA SSSSSSSEHN SPISTRSGSR RRLHSNSSIG TTSTITPSTA AATATTMSPP
AWIPDGKAPR CMSCQTPFTA FRRRHHCRNC GGVFCGVCSN ASAPLPKYGL TKAVRVCREC
YVREVRSSRQ APAQPSQAHG QASRPQAASA S