ID   SRRT_CRIGR              Reviewed;         306 AA.
AC   Q60436;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 3.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Serrate RNA effector molecule homolog;
DE   AltName: Full=Arsenite-resistance protein 2;
DE   Flags: Fragment;
GN   Name=SRRT; Synonyms=ARS2, ASR2;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PRELIMINARY FUNCTION.
RC   TISSUE=Lung;
RX   PubMed=10069470; DOI=10.1093/carcin/20.2.311;
RA   Rossman T.G., Wang Z.;
RT   "Expression cloning for arsenite-resistance resulted in isolation of tumor-
RT   suppressor fau cDNA: possible involvement of the ubiquitin system in
RT   arsenic carcinogenesis.";
RL   Carcinogenesis 20:311-316(1999).
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 (By similarity). Does not directly confer
CC       arsenite resistance but rather modulates arsenic sensitivity.
CC       Independently of its activity on miRNAs, necessary and sufficient to
CC       promote neural stem cell self-renewal. Does so by directly binding SOX2
CC       promoter and positively regulating its transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CASP8AP2, ERBB4, NCBP1/CBP80 and DROSHA.
CC       Interacts with LUZP4. Interacts with NCBP2/CBP20 and NCBP3.
CC       {ECO:0000250|UniProtKB:Q99MR6, 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA83777.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U41500; AAA83777.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001233648.1; NM_001246719.1.
DR   AlphaFoldDB; Q60436; -.
DR   SMR; Q60436; -.
DR   STRING; 10029.NP_001233648.1; -.
DR   GeneID; 100689205; -.
DR   KEGG; cge:100689205; -.
DR   CTD; 51593; -.
DR   OrthoDB; 525905at2759; -.
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; IPR039727; SE/Ars2.
DR   InterPro; IPR007042; SERRATE/Ars2_C.
DR   PANTHER; PTHR13165; PTHR13165; 1.
DR   Pfam; PF04959; ARS2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation.
FT   CHAIN           <1..306
FT                   /note="Serrate RNA effector molecule homolog"
FT                   /id="PRO_0000220964"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         101
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT   MOD_RES         263
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT   MOD_RES         270
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT   MOD_RES         280
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT   NON_TER         1
SQ   SEQUENCE   306 AA;  34267 MW;  552C89175C005F94 CRC64;
     HKEEELLGSS GGPPPEEPPK EGNPAEINVE RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY
     PNEDEMPNRC GIIHVRGPMP PNRISHGEVL EWQKTFEEKL TPLLSVRESL SEEEAQKMGR
     KDTEQEVEKF VTSNTQELGK DKWLCPLSGK KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF
     NNFLTDAKRP ALPEMKPAQP PGPAQILPPG LTPGLPYPHQ TPQGLMPYGQ PALPIFGYGA
     GAVRPAVPTG GPPYPHGPYG AGRGNYDAFR GQGGYPGKPR NRMVRGDPRA IVEYRDLDAP
     DDVDFF