ID   SUH_XENLA               Reviewed;         501 AA.
AC   Q91880; Q91881;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Suppressor of hairless protein homolog;
DE   AltName: Full=X-Su(H);
GN   Name=rbpj; Synonyms=rbpsuh, suh;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=9043084; DOI=10.1242/dev.124.3.693;
RA   Wettstein D.A., Turner D.L., Kintner C.;
RT   "The Xenopus homolog of Drosophila suppressor of hairless mediates Notch
RT   signaling during primary neurogenesis.";
RL   Development 124:693-702(1997).
RN   [2]
RP   SUBUNIT.
RX   PubMed=11485984; DOI=10.1101/gad.908101;
RA   Lamar E., Deblandre G., Wettstein D., Gawantka V., Pollet N., Niehrs C.,
RA   Kintner C.;
RT   "Nrarp is a novel intracellular component of the Notch signaling pathway.";
RL   Genes Dev. 15:1885-1899(2001).
RN   [3]
RP   INTERACTION WITH RITA1, AND SUBCELLULAR LOCATION.
RX   PubMed=21102556; DOI=10.1038/emboj.2010.289;
RA   Wacker S.A., Alvarado C., von Wichert G., Knippschild U., Wiedenmann J.,
RA   Clauss K., Nienhaus G.U., Hameister H., Baumann B., Borggrefe T.,
RA   Knochel W., Oswald F.;
RT   "RITA, a novel modulator of Notch signalling, acts via nuclear export of
RT   RBP-J.";
RL   EMBO J. 30:43-56(2011).
CC   -!- FUNCTION: Transcriptional regulator that plays a central role in Notch
CC       signaling, a signaling pathway involved in cell-cell communication that
CC       regulates a broad spectrum of cell-fate determinations. Acts as a
CC       transcriptional repressor when it is not associated with Notch
CC       proteins. When associated with some NICD product of Notch proteins
CC       (Notch intracellular domain), it acts as a transcriptional activator
CC       that activates transcription of Notch target genes (By similarity).
CC       Required for the transcriptional activation of ESR1, suggesting that it
CC       is required during primary neurogenesis in embryos. Binds to the oxygen
CC       responsive element of COX4I2 and activates its transcription under
CC       hypoxia conditions (4% oxygen) (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q06330, ECO:0000269|PubMed:9043084}.
CC   -!- SUBUNIT: Interacts with activated Notch proteins (By similarity). Forms
CC       a ternary complex with nrarp and the intracellular domain (NICD) of
CC       notch1. Interacts with rita1, leading to nuclear export, prevent the
CC       interaction between rbpj and NICD product and subsequent down-
CC       regulation of the Notch signaling pathway. {ECO:0000250,
CC       ECO:0000269|PubMed:11485984, ECO:0000269|PubMed:21102556}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:21102556}. Cytoplasm
CC       {ECO:0000250}. Note=Mainly nuclear, upon interaction with rita1,
CC       translocates to the cytoplasm, down-regulating the Notch signaling
CC       pathway. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=X-Su(H)1;
CC         IsoId=Q91880-1; Sequence=Displayed;
CC       Name=2; Synonyms=X-Su(H)2;
CC         IsoId=Q91880-2; Sequence=VSP_008394, VSP_008395;
CC   -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
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DR   EMBL; U60093; AAB05478.1; -; mRNA.
DR   EMBL; U60094; AAB05479.1; -; Genomic_DNA.
DR   RefSeq; NP_001084347.1; NM_001090878.1. [Q91880-1]
DR   AlphaFoldDB; Q91880; -.
DR   SMR; Q91880; -.
DR   ELM; Q91880; -.
DR   IntAct; Q91880; 2.
DR   MINT; Q91880; -.
DR   GeneID; 399453; -.
DR   KEGG; xla:399453; -.
DR   CTD; 399453; -.
DR   Xenbase; XB-GENE-865998; rbpj.S.
DR   OrthoDB; 444988at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 399453; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
DR   GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; ISS:UniProtKB.
DR   CDD; cd01176; IPT_RBP-Jkappa; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1450; -; 1.
DR   InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR   InterPro; IPR036358; BTD_sf.
DR   InterPro; IPR040159; CLS_fam.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR   InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR   InterPro; IPR038007; RBP-Jkappa_IPT.
DR   PANTHER; PTHR10665; PTHR10665; 2.
DR   Pfam; PF09270; BTD; 1.
DR   Pfam; PF09271; LAG1-DNAbind; 1.
DR   Pfam; PF20144; TIG_SUH; 1.
DR   SMART; SM01268; BTD; 1.
DR   SMART; SM01267; LAG1_DNAbind; 1.
DR   SUPFAM; SSF110217; SSF110217; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW   DNA-binding; Notch signaling pathway; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..501
FT                   /note="Suppressor of hairless protein homolog"
FT                   /id="PRO_0000208569"
FT   DOMAIN          356..446
FT                   /note="IPT/TIG"
FT   REGION          58..68
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q06330"
FT   REGION          166..171
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q06330"
FT   REGION          193..198
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q06330"
FT   VAR_SEQ         1..20
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9043084"
FT                   /id="VSP_008394"
FT   VAR_SEQ         21
FT                   /note="G -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9043084"
FT                   /id="VSP_008395"
SQ   SEQUENCE   501 AA;  55864 MW;  2B2A271F38E843C2 CRC64;
     MQPGIPKYTP SAIQLAPVVT GKFGERPQPK RLTREAMRNY LKERGDQTVL ILHAKVAQKS
     YGNEKRFFCP PPCVYLMGSG WKKKKEQMER DGCSEQESQP CAFIGIGNSE QEMQQLNLEG
     KNYCTAKTLY ISDSDKRKHF MLSVKMFYGN SDDIGVFLSK RIKVISKPSK KKQSLKNADL
     CIASGTKVAL FNRLRSQTVS TRYLHVEGGN FHASSQQWGA FYIHLLDDEE SEGEEFTVRD
     GYIHYGQTVK LVCSVTGMAL PRLIIRKVDK QTALLDADDP VSQLHKCAFY LKDTERMYLC
     LSQERIIQFQ ATPCPKEPNK EMINDGASWT IISTDKAEYT FYEGMGPINA PVTPVPVVES
     LQLNGGGDVA MLELTGQNFT PNLRVWFGDV EAETMYRCAE SMLCVVPDIS AFREGWRWVR
     QPVQVPVTLV RNDGVIYSTS LTFTYTPEPG PRPHCSAAGA ILRANSSLLA SNEPNTNSEG
     SYTNISTNSA NVTSSTAAVV S