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SRRT_DROAN
ID   SRRT_DROAN              Reviewed;         948 AA.
AC   B3MJ69;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Serrate RNA effector molecule homolog;
DE   AltName: Full=Arsenite-resistance protein 2 homolog;
GN   Name=Ars2; ORFNames=GF13819;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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: Acts as a mediator between the cap-binding complex (CBC) and
CC       RNA-mediated gene silencing (RNAi). Involved in innate immunity via the
CC       short interfering RNAs (siRNAs) processing machinery by restricting the
CC       viral RNA production. Also involved microRNA (miRNA)-mediated silencing
CC       by contributing to the stability and delivery of primary miRNA
CC       transcripts to the primary miRNA processing complex containing drosha
CC       and pasha (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
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DR   EMBL; CH902619; EDV38163.1; -; Genomic_DNA.
DR   RefSeq; XP_001961341.1; XM_001961305.2.
DR   AlphaFoldDB; B3MJ69; -.
DR   SMR; B3MJ69; -.
DR   STRING; 7217.FBpp0117011; -.
DR   PRIDE; B3MJ69; -.
DR   EnsemblMetazoa; FBtr0118519; FBpp0117011; FBgn0090846.
DR   GeneID; 6496655; -.
DR   KEGG; dan:6496655; -.
DR   eggNOG; KOG2295; Eukaryota.
DR   HOGENOM; CLU_008560_0_0_1; -.
DR   InParanoid; B3MJ69; -.
DR   OMA; HLRMCEE; -.
DR   OrthoDB; 525905at2759; -.
DR   PhylomeDB; B3MJ69; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IEA:EnsemblMetazoa.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; ISS:UniProtKB.
DR   GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR   GO; GO:0030422; P:siRNA processing; IEA:EnsemblMetazoa.
DR   InterPro; IPR039727; SE/Ars2.
DR   InterPro; IPR007042; SERRATE/Ars2_C.
DR   InterPro; IPR021933; SERRATE/Ars2_N.
DR   PANTHER; PTHR13165; PTHR13165; 1.
DR   Pfam; PF04959; ARS2; 1.
DR   Pfam; PF12066; SERRATE_Ars2_N; 1.
PE   3: Inferred from homology;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..948
FT                   /note="Serrate RNA effector molecule homolog"
FT                   /id="PRO_0000385216"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          856..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..876
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         82
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         431
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   948 AA;  107630 MW;  6132FC6780ECFBC7 CRC64;
     MADSDDEYDR KRRDKFRGER SDSYRTERRD DRRPLGGSGS ARDEWSDRNP FRGGASAGGG
     GGGARHRPDY SDYRGPGPRA RYGSPGRDLP PAKRMRPDWG DGDVRPNPRF GGYDPYLMQA
     WNDHYQSIHS AYSHGSHMPP VRESGGSGGD SLTQPAMLNL KQFLDTQDEN ISDSEVMRKY
     TEYKTDFKRQ QLNEFFVAHK DEEWFKNKYH PEDSVRRAEE QRGFLKRRTD VFVELLENGT
     IGSVKVDSVQ GDALIRVLDT CVIKLEGGTD EDLKALDEKP KETPVYERKH DPAPVKAVDE
     VKSPKKETEK EASPVIVSPQ RKSVKPLNSD DENWDEEVAA PPKKDVEEEP KALESGSEDK
     SRRKKSAKRK RVNSGDDSSS ESDSSSSSDD EDEEKLKKKY DVEDGLRSEQ KAEAEKDKEM
     QDAKVIEAPE SPKEATENSA EEVKASDAAE TPAEEAEQEK PEVAEEVNRP KQDQENGDKI
     TTEDGETKSD SEENKVMETE TIDLDKVRDG QPRALHRTSS IFLRNLAPSI TKAEIEAVCT
     RFSGYLRVAI ADPLVERRWY RRGWITFTRD VNIKEICWSL NNQRLRDCEM GAIVNRDLSR
     RVRPANGITA HKQVVRSDIK LCAKIILNLD ERFRLWPEPT SDDSIPFDRA GESSANGNTS
     TYGIKSKNPV LQNITDYLIE EASAEEEELL GLTGENKDAE GEPIERDEHL LAVLDRLVLY
     LRIVHSVDYY NHCEYPYEDE MPNRCGIIHA RGPAPSRVTS NDIHEYVKTY ESKLQQFLTK
     TALLSDEETK DLGAKDAETE VEKFVQANTQ ELAKDKWLCP LSGKKFKGPE FIRKHIFNKH
     EEKVDEVRKE VQYFNNYLRD PKRPQLPEHP GSSKRPESES GRGGGSGYRP PMYPPFSGMP
     YGFSPSMMGG GRGGRNFPPV RRELPLEHQR RLIGYHDLDA PANSDMFD
 
 
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