SRRT_PONAB
ID SRRT_PONAB Reviewed; 871 AA.
AC Q5R539;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2;
GN Name=SRRT; Synonyms=ARS2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-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 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; CR861036; CAH93127.1; -; mRNA.
DR RefSeq; NP_001126849.1; NM_001133377.1.
DR AlphaFoldDB; Q5R539; -.
DR SMR; Q5R539; -.
DR PRIDE; Q5R539; -.
DR GeneID; 100173857; -.
DR KEGG; pon:100173857; -.
DR CTD; 51593; -.
DR InParanoid; Q5R539; -.
DR OrthoDB; 525905at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
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..871
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000325960"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..849
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..382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..411
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 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 828
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 835
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 845
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 871 AA; 100030 MW; ED600032CCE62A3E CRC64;
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDHGRERR SRGEYRDYDR
NRRERFSPPR HELSPPQKRM RRDWDGHSSD PYHSGYEMPY AGGGGGPTYG PPQPWGHPGV
HIMQHHVLPI QARLGSIAEI DLGVPPPVMK TFKEFLLSLD DSVDETEAVK RYNDYKLDFR
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LRVFLSLMET GWFDNLLLDI
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPGKKEEGR AGAGLGDGER
KTNDKDEKKE DSKQAENDSS NDDKTKKSEG DGDKEEKKED SEKEAKKSSK KRNRKHSGDD
SFDEGSMSES ESESESGQAE EEKEEAEALK EKEKPKEEEW EKPKDAAGLE CKPRPLHKTC
SLFMRNIAPN ISRAEIISLC KRYPGFMRVA LSEPQPERRF FRRGWVTFDR SVNIKEICWN
LQNIRLRECE LSPGVNRDLT RRVRNINGIT QHKQIVRNDI KLAAKLIHTL DDRTQLWASE
PGTPPLPTSL PSQNPILKNI TDYLIEEVSA EEEELLGSSG GAPPEEPPKE GNPAEINVER
DEKLIKVLDK LLLYLRIVHS LDYYNTCEYP NEDEMPNRCG IIHVRGPMPP NRISHGEVLE
WQKTFEEKLT PLLSVRESLS EEEAQKMGRK DPEQEVEKFV TSNTQELGKD KWLCPLSGKK
FKGPEFVRKH IFNKHAEKIE EVKKEVAFFN NFLTDAKRPA LPEIKPAQPP GPAQSLTPGL
PYPHQTPQGL MPYGQPRPPI LGYGAGAVRP AVPTGGPPYP HAPYGAGRGN YDAFRGQGGY
PGKPRNRMVR GDPRAIVEYR DLDAPDDVDF F
