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LST2_DROGR
ID   LST2_DROGR              Reviewed;        1115 AA.
AC   B4JHI7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
GN   ORFNames=GH18624;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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; CH916369; EDV92814.1; -; Genomic_DNA.
DR   RefSeq; XP_001989752.1; XM_001989716.1.
DR   AlphaFoldDB; B4JHI7; -.
DR   SMR; B4JHI7; -.
DR   STRING; 7222.FBpp0152530; -.
DR   EnsemblMetazoa; FBtr0154038; FBpp0152530; FBgn0126091.
DR   GeneID; 6563666; -.
DR   KEGG; dgr:6563666; -.
DR   eggNOG; KOG1819; Eukaryota.
DR   HOGENOM; CLU_007360_1_1_1; -.
DR   InParanoid; B4JHI7; -.
DR   OMA; DAPRCMA; -.
DR   OrthoDB; 451347at2759; -.
DR   PhylomeDB; B4JHI7; -.
DR   Proteomes; UP000001070; 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..1115
FT                   /note="Lateral signaling target protein 2 homolog"
FT                   /id="PRO_0000378964"
FT   ZN_FING         1025..1085
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          308..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..488
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..656
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..702
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..903
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1031
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1034
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1047
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1050
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1055
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1058
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1077
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1080
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         604
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         908
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1115 AA;  122723 MW;  181E530ABF63B6D1 CRC64;
     MDTFRKWLNK PKADDKSLLA RFYHADRSLT AVASELDSFD GRAEPDRCTR LVSRLRQNQD
     KVLAITNMIM EELLGEDRDP RAFRAKFPEE VLQENLAGQL WFGAECLAAG SSILNRESES
     KEMRPLAQAV TKSLGHVRVL LRDQCLRNNV PNSKTLHLDF NDSNTEQLYE SLKIFDHLFA
     EFELSYVSAM VQVKSRHEYE MQQWIGVLFS ETLQRSLKVG LLDQDMVDAF DPGLMFSIPR
     LAIVAGLVVY AKGPLNMDMP GDQLSEMFRP FRTILIKIRD LLRNLSKQEL YQLEKLLCTN
     EDINTKVPLG SSSIEAPSPE HNNSSSTTNT SNNNNNNTNN NNSSSGSDCT NNDKTGTTTN
     THKPVERLVD HRNNNTTNSQ QTSSCSVNAA ATTPATSSRT RTPPSILSPS AGSTPTASPA
     PSPTPSHSIA STSSAATTST NSPAHWSDYD DDDEDDDDDD VHADVEEDED ESGILDSDEH
     DLNDDSDSEV DEFFEAQLKA IVAAVDCAPG YLIPDCASGY LISNTNLGNL LQPQQVPLTD
     NFVASEDDEL GNPTAVDQQQ QPQQQLEHHQ QQLQQQQHTE DEPSTSAAML AARRTLQRLR
     LPSSSSDNEP SSNNQQMTIK SPSEQTTTRS SSNRHRHHSH HHHHHHHSHH HHHHQPTAAV
     AVAAAQDEQH NNNQPHSHSH SSSHHHHHNH QSHSHPHRAN RSTRKRCSQE HCETITTTKT
     TSGGEQQTED SLDSSTASSL SDDVSLAMRN TTARLKFKST ENLLHRLFVC IAGVADQLQT
     NFASDLRQIL RSVFLMNMSS AQEDIDIPEK TKESELFEFR ASENDVIQES AGSNQSIYSA
     EEVNPELDNV FNTNTGTNGA RHSAGATMQR NNTIDLATVQ SSNSGNSSSS NSSSSSSAAR
     SHVARSRSLG DHDQASTSSS QQQQRELQLQ LQQQQQQQAQ MQQQLQRHRN NSVGSNSPSS
     ASSTSSNSEH NSPVSTRSGS RRRLPSNTTT TLSTSIGTAA TTPTGATTTG VTTTTTMSPP
     AWIPDGKAPR CMSCQTPFTV VRRRHHCRNC GGVFCGVCSN ASAPLPKYGL TKAVRVCREC
     FMREVRQSHS HGQSQSQIHS PTQQAGGRPQ AASAS
 
 
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