ID W8AP59_CERCA Unreviewed; 867 AA.
AC W8AP59;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Serrate RNA effector molecule homolog {ECO:0000256|ARBA:ARBA00017364};
DE AltName: Full=Arsenite-resistance protein 2 homolog {ECO:0000256|ARBA:ARBA00030701};
DE Flags: Fragment;
GN Name=SRRT {ECO:0000313|EMBL:JAB90560.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB90560.1};
RN [1] {ECO:0000313|EMBL:JAB90560.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB90560.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
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. {ECO:0000256|ARBA:ARBA00025002}.
CC -!- SUBUNIT: Interacts with cbp20, Dcr-2 and pasha.
CC {ECO:0000256|ARBA:ARBA00011796}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARS2 family.
CC {ECO:0000256|ARBA:ARBA00005407}.
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DR EMBL; GAMC01015995; JAB90560.1; -; mRNA.
DR AlphaFoldDB; W8AP59; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd00590; RRM_SF; 1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR PANTHER; PTHR13165; ARSENITE-RESISTANCE PROTEIN 2; 1.
DR PANTHER; PTHR13165:SF0; SERRATE RNA EFFECTOR MOLECULE HOMOLOG; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
PE 2: Evidence at transcript level;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 28..137
FT /note="SERRATE/Ars2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12066"
FT DOMAIN 673..840
FT /note="SERRATE/Ars2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04959"
FT REGION 171..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB90560.1"
SQ SEQUENCE 867 AA; 98996 MW; 05C0CC7411CDED05 CRC64;
GHNHAPHASR EAPSSGDLQT QPAMLTLKQF LDTQDDGISD SEVLRKYSEY KIEFKRQQLN
EFFVAHKDEE WFKNKYHPAD SVKRKEEQLN FLKKRVDVFN ELLVNGQVKA VSIDTSQTDP
LLRLLDTVVI KLEGGTDDDL KILDEKPREY TFPERSFDKK PQHDDDVIIT SVGKKRNEDD
EPKVVSPRPI RRAPLSDDEE NWDDDDAGDN KVTTDKGDVK KDHSDEEDKS DEEEKGRDKK
SLKRKRTSSE SSSSSSSDSD SSSSSSSDEE DDEKVKDKYD LGRVKEEKDA EKNVADDVKE
KEDVDKTIDA PQDKEVASVE NNLNGESEKE SQLSQNGMIL NEKAENSSEQ KDGEAEAEGE
KDDSEKIAEP VPRDDDMKEA TFNNNNPKSE DAKEDKPDSN ERDEKEVDLE KKEINEPEDQ
PETIDLDKVK DGPQPRALHR TSSIFLRNLA PSITKAEIET LCQRFDGYLR VAIADPLVDR
RWYRRGWVTF KRDVNIKEIC WNLNNTRLRD CEMGAIVNRD LSRRVRPVNG MTAHKTIVRS
DIKLCAKIAM NLDERFKLWD KNNQKNTEQT AENSKGNGDA AASYGFKSNN PVLQNITDYL
IEEASAEEDE LLGISGENKE SEGEMIERDV QLISVLDSLI LYLRIVHSVD FYNHCEYPYE
DEMPNRCGII HARGPPPSKV QANDIQDYIK NFESKMQTFL TKTTPIDDEE LKNLGSKDAE
AEVEKFVQAN TQELAKDKWL CPLSGKKFKG PEFIRKHIFN KHTEKVDEVR KEVEFFNNYL
RDPKRPQLPE HASSSKRTTS ESGGLGYRPS VYPPAFMPPY AAYAPPMMVP GRGGRGFGPG
RRPPNKYRQL TQYRDLDAPQ EPVDIFN
//