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LST2_CAEBR
ID   LST2_CAEBR              Reviewed;         651 AA.
AC   A8XJZ8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Lateral signaling target protein 2;
GN   Name=lst-2; ORFNames=CBG14460;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE600983; CAP32974.1; -; Genomic_DNA.
DR   RefSeq; XP_002644535.1; XM_002644489.1.
DR   AlphaFoldDB; A8XJZ8; -.
DR   SMR; A8XJZ8; -.
DR   STRING; 6238.CBG14460; -.
DR   GeneID; 8586531; -.
DR   KEGG; cbr:CBG_14460; -.
DR   CTD; 8586531; -.
DR   WormBase; CBG14460; CBP41975; WBGene00034944; Cbr-lst-2.
DR   eggNOG; KOG1819; Eukaryota.
DR   HOGENOM; CLU_007360_1_1_1; -.
DR   InParanoid; A8XJZ8; -.
DR   OMA; NLSEMFR; -.
DR   OrthoDB; 451347at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
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..651
FT                   /note="Lateral signaling target protein 2"
FT                   /id="PRO_0000378956"
FT   ZN_FING         557..617
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          294..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         563
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         566
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         579
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         582
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         587
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         590
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         609
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         612
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ   SEQUENCE   651 AA;  73333 MW;  831DBFAA219A4646 CRC64;
     MQSFRKIWNK PRPDDWMPLA RFYYADSALN DIASELDSFD GRRDPDRCNA LVTRLRVAQD
     RVLHIITEML IHLYPREQDR ACRDFRIKFP DEILHDTLPG QLWFGAECLS AGSNIIDHET
     ESDLIRPLAK EVTKQLDILR DLLKNQSLRD PSAYNPVIKE NLLKFDKLFA EFEYQYVSAM
     VPVKSVKEHD SQLDVAVLFS EVLSLALEKD LITQDLIDYC DPSVMIAIPR LGIVWGLLVY
     SEGALNVDVP AENLSEMFRP FYSLLVKIRN LLRILTPVEL TRLETVLCKG ETAVPEDSSS
     KLTMSDFRTN ATDEEKAKNN QRVWMCDMPS DSTSSLDSDL RDSASEATSL ASSGLTSPSS
     GSEDNLNRMV DKSDEELDDD VIETASSEEN ESDSNNENVE MVASSGDSSE TESNSKENEE
     DVDEQATLQA LAHETAEQLV AIKKKHEKHS KIIIPMQNEP RTLIDPKNLR SRFRSSEDLV
     HRLFVCIAGV ADQLQTNYSS EIRKVLKIIL QPSEVIPVYE VVNAQVANNS TEGEETGVEA
     QETLPLPAFM GVRWVPDEDC EQCTACSMPF NFVRRRHHCR NCGRIFCHKC SCNSISIPEH
     GYDRKVRVCN LCYVHRLNPF GCNEQSQASE NNTGISSVAE QSSAQATSAS S
 
 
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