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LST2_DROSE
ID   LST2_DROSE              Reviewed;         975 AA.
AC   B4IC49;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
GN   ORFNames=GM10129;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480828; EDW45207.1; -; Genomic_DNA.
DR   RefSeq; XP_002041469.1; XM_002041433.1.
DR   AlphaFoldDB; B4IC49; -.
DR   SMR; B4IC49; -.
DR   STRING; 7238.B4IC49; -.
DR   EnsemblMetazoa; FBtr0193114; FBpp0191606; FBgn0165080.
DR   HOGENOM; CLU_007360_1_0_1; -.
DR   OMA; DAPRCMA; -.
DR   PhylomeDB; B4IC49; -.
DR   Proteomes; UP000001292; 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..975
FT                   /note="Lateral signaling target protein 2 homolog"
FT                   /id="PRO_0000378968"
FT   ZN_FING         895..955
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          299..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..455
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..598
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..889
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         901
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         904
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         917
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         920
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         925
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         928
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         947
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         950
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         796
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   975 AA;  106909 MW;  240390DBDE6984D1 CRC64;
     MQSADDKSLL ARFFHADRSL TAVASELDSF DGRAEPDRCT RLVSRLRQNQ DKVLAITNLI
     MEELLGEDRD PRAFRAKFPE EVLQENLAGQ LWFGAECLAA GSSIMNRESE SKEMRPLAQA
     VTKSLGNVRV LLRDQCLKNN VPNSKTLHLD LNDSTTEQLY ESLKIFDRLF AEFELSYVSA
     MVQVKSRHEY EMQQWIGVLF SETLQRALKI GLLDQEMVDA FDPGLMFSIP RLAIVAGLVV
     YAKGPLNMDM PGDQLSEMFR PFRTILIKIR DLLRNLNNQE LYQLEKLLCT NEDINTKVPL
     GSSSIEAPSP EHSSHPTTSS TQNNNNSSNN NHSSSSTNTT STTITTAGTT NTHRTVERLV
     DQRNNNHNSN SNSSSNPTVE GATLRSPSML SLSTTSTPTA SPTPSPTPSH SIASTSSAAT
     SSTNPPADWS DGDDEDEDDD DIDVDEEDPE SSDDGTDEEQ LLKDIVAADC ASGYLIPNTN
     LGNLLQPQEV PLTDNFVASE DDEYGTAEQQ GHQGLEEEEP STSAAMLAAT RTLQRLRLPS
     SDNEPLAEPT TIKASEEHMQ QPSGRHHRHH QSHHHHHHHR HSHQHQHRQP HPHRTTRSGR
     KRCSLEAADP ETIQPEREQN LASGDTSAAS SLSDDVSLAM RNTTARLKFK STENLLHRLF
     VCIAGVADQL QTNFASDLRQ ILRSVFLMNM SAAQEDIDIP EKTKESELFE FRASENDVIQ
     ESAGSNQSIY SAEEVNPELD NVFSAGGGNQ ATGQRHSAGA SMQRNNTIDL ASQPGEGSPS
     GATTTTSRSH VTRSRSLGDQ EAASSATSST AQLRQLEQQQ QQQQLQIQLQ RQRNNSVGSN
     TPSSASSTSS SSEQNSPVSA RSGSRRRLQS NNETQMPSSA TSTSATLSPP AWIPDGKAPR
     CMACQTPFTA FRRRHHCRNC GGVFCGVCSN ASAPLPKYGL TKAVRVCRDC YVREVRSGMG
     VQGVQSVQSV QASAS
 
 
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