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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
 
 
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