ID   SRRTB_XENLA             Reviewed;         844 AA.
AC   Q6INH5; Q8AVP5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Serrate RNA effector molecule homolog B;
DE   AltName: Full=Arsenite-resistance protein 2-B;
GN   Name=srrt-b; Synonyms=ars2-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and
CC       the primary microRNAs (miRNAs) processing machinery during cell
CC       proliferation. Contributes to the stability and delivery of capped
CC       primary miRNA transcripts to the primary miRNA processing complex,
CC       thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts ncbp1/cbp80. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=Predominantly nuclear. Shuttles between the nucleus
CC       and the cytoplasm (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH41542.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC041542; AAH41542.1; ALT_SEQ; mRNA.
DR   EMBL; BC072306; AAH72306.1; -; mRNA.
DR   RefSeq; NP_001082532.1; NM_001089063.1.
DR   AlphaFoldDB; Q6INH5; -.
DR   SMR; Q6INH5; -.
DR   PRIDE; Q6INH5; -.
DR   DNASU; 398542; -.
DR   GeneID; 398542; -.
DR   KEGG; xla:398542; -.
DR   CTD; 398542; -.
DR   Xenbase; XB-GENE-5825723; srrt.L.
DR   OrthoDB; 525905at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 398542; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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; PTHR13165; 1.
DR   Pfam; PF04959; ARS2; 1.
DR   Pfam; PF12066; SERRATE_Ars2_N; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..844
FT                   /note="Serrate RNA effector molecule homolog B"
FT                   /id="PRO_0000385213"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  97871 MW;  062C2E44FC487843 CRC64;
     MADSDDEHDR RRRDKFRRER SDYDRSRERE ERRRDDWSDR EWDRGRERRS RGEYRDYESR
     SRRDRFSPQR HDISPPQKRM RRDWDDHGSD PYHSGYEMPY SSSAGPAYGP PQPWGHPEMH
     VMQHHGIPIQ ARLGNLHDVD LGTPAPTMKT FKEFLLSLED SVDETEAVKR YNDYKIDFRR
     QQMQEFFLAH KDEEWFRSKY HPDEVGKHKQ ESRASLHNRL NAFMFLMENS WLNEVQLDIA
     QSTAIIKVLD AAVIKMEGGT EIDLKILDEE EEEAKREAAK KEEARVTETE KVITEEKEAP
     AKPEKDKEPE SEEKPVKPEE EEEKKVEKEE PERETRKPGT RKRKRSGDSD DGSDSESDTE
     TASPKPETPN QNGCEDTPKK EEETEKPKEK PKEDTVKPRP LHKTCSIFMR NIPPNISKAE
     ITALCKRYPG FMRVALSEPQ PERRFLRKAY VTFDRSVNIK EICWSVQNIR LRECELSPGV
     NRDLTYRVRN INGITLHRPI VRNDIKLAAR LIHALDERAQ LWEGEQGDQV VSAQNPILKN
     ITDYLIDEVN AEEEELLSSA GRTPETEAPK EGNPTEITVE RDEKLIKVLD KLLFYLRIVH
     SVDYYNTCEY PNEDEMPTRC GMMHVRGPLP PNRVSHGEVT EWQKTIEEKL APLFAVRETL
     SEDEAMKMGK KDPEQEAEKF VTANTQELGK EKWLCPLSGK KFKGPEFVRK HIFNKHAEKI
     EEVKKEVEFF NNYLTDSKRP ALPEVKPLQP PGGAAGQALA AGLLYPPQGP QALLPYGQPR
     PPVLGYGGAP QFPPNPYGAG RGNYDSFRGQ GMYPGKPRNR MMRGDPRSII EYRDLDAPDD
     VDFF