SRRT_DANRE
ID SRRT_DANRE Reviewed; 896 AA.
AC Q66I22; Q8JHH2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2;
GN Name=srrt; Synonyms=ars2; ORFNames=ch211-283g2.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=12006978; DOI=10.1038/ng896;
RA Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA Hopkins N.;
RT "Insertional mutagenesis in zebrafish rapidly identifies genes essential
RT for early vertebrate development.";
RL Nat. Genet. 31:135-140(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-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). Independently of its activity on miRNAs, necessary and
CC sufficient to promote neural stem cell self-renewal. Does so by
CC directly binding SOX2 promoter and positively regulating its
CC transcription (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}.
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DR EMBL; AF506224; AAM34668.1; -; mRNA.
DR EMBL; CR407559; CAM14209.1; -; Genomic_DNA.
DR EMBL; BC081580; AAH81580.1; -; mRNA.
DR RefSeq; NP_775345.2; NM_173238.2.
DR AlphaFoldDB; Q66I22; -.
DR SMR; Q66I22; -.
DR STRING; 7955.ENSDARP00000005886; -.
DR PaxDb; Q66I22; -.
DR PRIDE; Q66I22; -.
DR Ensembl; ENSDART00000018895; ENSDARP00000005886; ENSDARG00000017762.
DR GeneID; 192311; -.
DR KEGG; dre:192311; -.
DR CTD; 51593; -.
DR ZFIN; ZDB-GENE-020419-13; srrt.
DR eggNOG; KOG2295; Eukaryota.
DR GeneTree; ENSGT00390000005492; -.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; Q66I22; -.
DR OMA; QVGFNWF; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; Q66I22; -.
DR TreeFam; TF317609; -.
DR Reactome; R-DRE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q66I22; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000017762; Expressed in mature ovarian follicle and 22 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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; 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 2: Evidence at transcript level;
KW Activator; Cytoplasm; Nucleus; Reference proteome;
KW RNA-mediated gene silencing; Transcription; Transcription regulation.
FT CHAIN 1..896
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000385211"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 215
FT /note="A -> V (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="K -> R (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..459
FT /note="SI -> EF (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="D -> E (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="A -> E (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="L -> M (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="L -> I (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="L -> V (in Ref. 1; AAM34668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 103274 MW; 5B8DD1E66B1E84CC CRC64;
MGDSDDEYDR RRRDKFRRER SDYDRSRERE DRRRDDWNDR RPSAREWDRG RERRSRGEYR
DYDRGRRERF SPPRHDMSPQ QKRMRRDWDD HGGDPYHGGY DLGYGGGGGP SYAPPQPWGH
PDMHLMQPHH GIPIQARLGN IHDMDLGPPP PVMKTFKEFL ISLDDSVDET ESVKRYNEYK
IDFRRQQMQD FFLAHKDEEW FRSKYHPDEA GRRKAEAHSA LQNRLGVYMY LMDNNWFESV
SLDIERAPQI TKILDAAVIK MEGGAENDLR ILEQPSEEEE ERERLSSGGT PSEPSKRDEP
KPADTENKPS EEKDKMEEGE ESAEKDGEKA SAGGSEGEEK TEKEAPAEPI PEPKKLSKKR
KRKHSGDSED EASASESESD SDSDSNSHCS EKPSEREREP EEVEEKEEEE EEEGEAADGK
EQTDEQTERE KEKEKKVKDD QPPRPRPLHR TCSLFMRSIA PTISKAEIVA LCRRYPGFMR
VCLSEPQPER RFFRRCWVTF DRGVNIKEIC WNLQNIRLRD CELAPGVNRD LARRVRNVNG
ITQHKQVLRN DIKLAAKLIH ALDDREKLWS QKPREETPTL ELPAQNPILK NITDYLIEEV
SAEEEELLGS AGGGDSEDGS KEGNPTEITV ERDEKLVKVL DRLLFYLRIV HSIDYYNTCE
YPSEDEMPNR CGIIHVRGPI PPNRITLREV SDWQKTFEEK MGPLFSVKEN LSEDEAAKMG
RKDPEQEVEK FVVANTQELG KDKWLCPLSG KKFKGPEFVR KHILNKHGDK IEEVKKEVVF
FNNFLMDAKR PCIPEMKPPP HPGPGQGVLS PGGLPFPPQG PQGLMGFGQP RPPLMGYGGG
PPYPPNQYGG GRGNYDNFRG QGGYPGKPRN SRVMRGDPRN IIEYRDLDAP DDVDFF
