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LST2_CULQU
ID   LST2_CULQU              Reviewed;         907 AA.
AC   B0WAQ0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
GN   ORFNames=CPIJ004116;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB;
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS231874; EDS41691.1; -; Genomic_DNA.
DR   RefSeq; XP_001845784.1; XM_001845732.1.
DR   AlphaFoldDB; B0WAQ0; -.
DR   SMR; B0WAQ0; -.
DR   STRING; 7176.CPIJ004116-PA; -.
DR   GeneID; 6035645; -.
DR   KEGG; cqu:CpipJ_CPIJ004116; -.
DR   VEuPathDB; VectorBase:CPIJ004116; -.
DR   VEuPathDB; VectorBase:CQUJHB012925; -.
DR   eggNOG; KOG1818; Eukaryota.
DR   eggNOG; KOG1819; Eukaryota.
DR   HOGENOM; CLU_007360_1_0_1; -.
DR   InParanoid; B0WAQ0; -.
DR   OMA; DAPRCMA; -.
DR   OrthoDB; 451347at2759; -.
DR   PhylomeDB; B0WAQ0; -.
DR   Proteomes; UP000002320; Partially assembled 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; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..907
FT                   /note="Lateral signaling target protein 2 homolog"
FT                   /id="PRO_0000378961"
FT   ZN_FING         845..905
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          339..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..393
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..516
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..548
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         851
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         854
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         867
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         870
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         875
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         878
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ   SEQUENCE   907 AA;  98062 MW;  FFED7BBD2C70F629 CRC64;
     MLVGADDKSL LARFYHADRA LTAVASELDS FDGRAEPVRC TRLVGRLRQG QDRVLAITNQ
     IMDELLGEDR AARAFRAKFP EEVLQESLAG QLWFGAECLA AGSSIMNREV ESATMRPLAK
     AVTKSLDNVR NLLREQCLRN NTPNSLTLRL DVNDAATEQL YESLKIFDRL FAEFELLYVS
     AMVQVKSKQE YEMQELICVL FSETLQRALK VGLLEQEQVD SYDPALMFSI PRLAIVAGLV
     IFKEGPLNMD QPADDISEMF RPFRKLLIKM RDLLRTLTKH ELYQLEKLLC TNEEISLKEQ
     QIICDGNEIV GGGQSPSAAP NPARDDTVVI VTTSATVNSS DNLRGQEPQE DISSFYTSNN
     RRTVDSEPNE DDDVSESNDE DEDEGEEVDE DDPANILKDA LVTSDCASGY LIPNTNFGNL
     LQTNEAPLTD SFIATDEELK LASGAASSHA RIEQILSESN QKLTDSGLGT ANPSLDHSPE
     LETERPVTSS HPIAQSSSSS SEEEGEVDEY DEDDSESTLC EPKPHHTKHQ RRHRHHHHHH
     RKHYSKHRSS AAGSAGTSGT TCSAAERQIS SCDTSPSSGG LPSECGSSTS GGSSGNSSGG
     SGDADAAQEV AMAIRAAGRI KFKTTENLLH RLFVCIAGVA DQLQTNFAAD LRQMLKSVFV
     INSSPPEPED PPEPAANSTD KPKEPDPADL FEFRASEQDV ITNSGGSSQS IYSAEEVNAE
     DPHDSVFGSP PGGASPVRAS SAPRTMMTTA ASSENGSVTV NVSVSVVTAG SGGSGSGSSR
     SSQERSVSLS ETSIVVDGSG GNTEGTALLV PRESTPKSVQ SEQSGQRGMM EERRMPEAPP
     RWIPDGDAPR CMACASSFTP FRRRHHCRNC GGVFCGGCSS ASAPLPKYGL TKAVRVCREC
     FVREVGV
 
 
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