ID   SDE2_XENTR              Reviewed;         468 AA.
AC   Q07G43;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=sde2; ORFNames=TEgg019d03.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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; CR762124; CAL49366.1; -; mRNA.
DR   RefSeq; NP_001120528.1; NM_001127056.1.
DR   AlphaFoldDB; Q07G43; -.
DR   SMR; Q07G43; -.
DR   PaxDb; Q07G43; -.
DR   GeneID; 100145674; -.
DR   KEGG; xtr:100145674; -.
DR   CTD; 163859; -.
DR   Xenbase; XB-GENE-5807809; sde2.
DR   eggNOG; KOG2827; Eukaryota.
DR   InParanoid; Q07G43; -.
DR   OrthoDB; 1446978at2759; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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_0000442527"
FT   CHAIN           72..468
FT                   /note="Replication stress response regulator SDE2"
FT                   /id="PRO_0000286090"
FT   DOMAIN          413..447
FT                   /note="SAP"
FT                   /evidence="ECO:0000255"
FT   REGION          169..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          112..143
FT                   /evidence="ECO:0000255"
FT   MOTIF           33..46
FT                   /note="PIP-box"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   COMPBIAS        180..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..378
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   468 AA;  50788 MW;  6767AC4FE9B16A33 CRC64;
     MASVWVRDAL SSRLQLVRVA PGAAALDLLS QAGTAIPLTD FYITCNGHLA DLEEKLQDGR
     TYSIVPRLCG GKGGFGSMLR ALGAQIEKTT NREACRDLSG RRLRDVNHEK AMAEWIKKQA
     DREAEKEQRR LERLQRKLAE PKHYFTDPEY HKQCHDMSER LEEAVIKGLQ ASSSSMASAE
     SDDTRKRKKD MYSSKGTPGK KKCFWTGLEG LETSSSSDSA SDSDLDESPC SSSSSSSDSK
     YYENIKERLQ SPESQSSPEE LGQGSSDGSH QMLEGHSSSD RSHQMLEGQA SCSGSDQMLE
     GPSSSAGAQW QSSSKGTELV QESQSIPVES EQNMESQNSS DESKQTAFNN SGINVECENV
     TSPGSTGQDG QTPNDGVRPA SPSIPISKQE LQQPSNAETS PIDLLAFKTA AELEALGLEK
     LKLELGALAL KCGGTLQERA ARLFSVRGLP RDQIDPSLFA KPAKGKKK