ID   SDE2_XENLA              Reviewed;         454 AA.
AC   Q6NRI5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=sde2;
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 [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in both DNA replication and cell cycle control.
CC       Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction
CC       with PCNA prevents monoubiquitination of the latter thereby inhibiting
CC       translesion DNA synthesis. The binding of SDE2 to PCNA also leads to
CC       processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving
CC       off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is
CC       degraded by the DCX(DTL) complex in a cell cycle- and DNA damage
CC       dependent manner. Binding of SDE2 to PCNA is necessary to counteract
CC       damage due to ultraviolet light induced replication stress. The
CC       complete degradation of SDE2 is necessary to allow S-phase progression.
CC       {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates both the
CC       interaction with PCNA and cleavage of the SDE2 precursor by a
CC       deubiquitinating enzyme. {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- DOMAIN: The SAP domain is necessary for specific binding to DNA.
CC       {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- DOMAIN: The propeptide displays a ubiquitin-like fold.
CC       {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- PTM: The protein is cleaved at Gly-71 by a deubiquitinating enzyme to
CC       form the active SDE2. {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- SIMILARITY: Belongs to the SDE2 family. {ECO:0000305}.
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DR   EMBL; BC070765; AAH70765.1; -; mRNA.
DR   RefSeq; NP_001084858.1; NM_001091389.1.
DR   AlphaFoldDB; Q6NRI5; -.
DR   SMR; Q6NRI5; -.
DR   BioGRID; 101272; 1.
DR   IntAct; Q6NRI5; 1.
DR   DNASU; 431906; -.
DR   GeneID; 431906; -.
DR   KEGG; xla:431906; -.
DR   CTD; 431906; -.
DR   Xenbase; XB-GENE-6079013; sde2.S.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 431906; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR024974; Sde2_N.
DR   Pfam; PF13019; Sde2_N_Ubi; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Coiled coil; DNA replication; DNA-binding;
KW   Mitosis; Nucleus; Reference proteome.
FT   PROPEP          1..71
FT                   /note="UBL"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT                   /id="PRO_0000442526"
FT   CHAIN           72..454
FT                   /note="Replication stress response regulator SDE2"
FT                   /id="PRO_0000286089"
FT   DOMAIN          399..433
FT                   /note="SAP"
FT                   /evidence="ECO:0000255"
FT   REGION          170..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          109..143
FT                   /evidence="ECO:0000255"
FT   MOTIF           33..46
FT                   /note="PIP-box"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   COMPBIAS        179..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            71..72
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
SQ   SEQUENCE   454 AA;  49363 MW;  C540EE4E97B17644 CRC64;
     MASVWVRDAL SGRLQLVRVA PGAVALDLLY QEGTAIPLTD FYVKCNGHLA DLEEKLQDGH
     TYSIEPRLCG GKGGFGSMLR ALGAQIEKTT NREACRDLSG RRLRDVNHEK AMAEWTKKQA
     DREAEKEQRR LERLQRKLAE PKHYFTDPEY HKQCHDMSER LEEAVIKGLQ ASSSDVVSAE
     SDDTRKRKKD MYASKGTSSK KKCFWTGLEG LEASSSSDSS SDSDLDESPC SSSSGSKHHE
     YIKERLGSPE SSSSSDGLEE ASSAGSHQML KGQTSGSESD NILEGPSSSA GSLHVPQLQS
     SSKGTEHIQE PQTCPAESEQ NTETPNISDG SEENPTTVTN SECKSVTSAA NTGQNEQILD
     DGHKFASPTL LEPKSELQQS SNTEPSSIDL VAYKTVAELE ALGLEKLKLE LVALGLKCGG
     TLQERAARLF SVRGLARDQI DPSLFAKPAK AKKK