SRRT_BOVIN
ID SRRT_BOVIN Reviewed; 876 AA.
AC A4IFB1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2;
GN Name=SRRT; Synonyms=ARS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) 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 containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated
CC gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped
CC RNA); however interaction is probably mediated via its interaction with
CC NCBP1/CBP80 component of the CBC complex. Involved in cell cycle
CC progression at S phase. Does not directly confer arsenite resistance
CC but rather modulates arsenic sensitivity. Independently of its activity
CC on miRNAs, necessary and sufficient to promote neural stem cell self-
CC renewal. Does so by directly binding SOX2 promoter and positively
CC regulating its transcription (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CASP8AP2, ERBB4, NCBP1/CBP80 and DROSHA.
CC Interacts with LUZP4. Interacts with NCBP2/CBP20 and NCBP3. Interacts
CC with MTREX (By similarity). {ECO:0000250|UniProtKB:Q99MR6,
CC ECO:0000250|UniProtKB:Q9BXP5}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Predominantly nuclear. Shuttles between the nucleus
CC and the cytoplasm in a CRM1-dependent way (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
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DR EMBL; BC134491; AAI34492.1; -; mRNA.
DR RefSeq; NP_001077177.1; NM_001083708.1.
DR AlphaFoldDB; A4IFB1; -.
DR SMR; A4IFB1; -.
DR STRING; 9913.ENSBTAP00000001507; -.
DR PaxDb; A4IFB1; -.
DR PRIDE; A4IFB1; -.
DR Ensembl; ENSBTAT00000001507; ENSBTAP00000001507; ENSBTAG00000001134.
DR Ensembl; ENSBTAT00000001510; ENSBTAP00000001510; ENSBTAG00000001134.
DR GeneID; 527938; -.
DR KEGG; bta:527938; -.
DR CTD; 51593; -.
DR VEuPathDB; HostDB:ENSBTAG00000001134; -.
DR VGNC; VGNC:35296; SRRT.
DR eggNOG; KOG2295; Eukaryota.
DR GeneTree; ENSGT00390000005492; -.
DR InParanoid; A4IFB1; -.
DR OMA; QVGFNWF; -.
DR OrthoDB; 525905at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000001134; Expressed in thymus and 106 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:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0140262; F:mRNA cap binding complex binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 2.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT CHAIN 2..876
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000325959"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 8
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 544
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 833
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 840
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 850
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
SQ SEQUENCE 876 AA; 100566 MW; 9B577B5B619585CD CRC64;
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR
NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYEMPY AGGGGGPAYG PPQPWGHPDV
HIVQHPVLPI QARLGSIAEI DLGVPPPVMK TFKEFLLSLD DAVDETEAVK RYNDYKLDFR
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LRVFLSLMES GWFDNLLLDI
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPNKKEESR VGPGLGDGER
KANEKDDKKE DGKQAENESS SDDKIKKSEG DGDKEEKKED SEKEAKKSSK KRNRKHSGDD
SFDEGSVSES ESESESGQAE EEKEEADETL KEKEKPKEEE REKPKDAPGL ECKPRPLHKT
CSLFMRNIAP NISRAEIISL CKRYPGFMRV ALSEPQPERR FFRRGWVTFD RSVNIKEICW
NLQNIRLREC ELSPGVNRDL TRRVRNINGI TQHKQIVRND IKLAAKLVHT LDDRTQLWAP
EPGTPALPAS LPSQNPILKN ITDYLIEEVS AEEEELLGSS GGAPPEEPPK EGNPAEINVE
RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY PNEDEMPNRC GIIHVRGPMP PNRISHGEVL
EWQKTFEEKL TPLLSVRESL SEEEAQKMGR KDPEQEVEKF VTSNTQELGK DKWLCPLSGK
KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF NNFLTDAKRP ALPEIKPAQP PGPAQILPPG
LTPGLPYPHQ TPQGLMPYGQ PRPPILGYGA GAVRPAVPTG GPPYPHAPYG AGRGNYDAFR
GQGGYPGKPR NRMVRGDPRA IVEYRDLDAP DDVDFF
