ID   SDE2_PONAB              Reviewed;         451 AA.
AC   Q5RET9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=SDE2;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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-77 by a deubiquitinating enzyme to
CC       form the active SDE2. {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- PTM: Both SDE2-UBL and the mature SDE2 are polyubiquitinated.
CC       {ECO:0000250|UniProtKB:Q6IQ49}.
CC   -!- SIMILARITY: Belongs to the SDE2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR857420; CAH89711.1; -; mRNA.
DR   EMBL; CR857427; CAH89718.1; -; mRNA.
DR   RefSeq; NP_001124780.1; NM_001131308.1.
DR   AlphaFoldDB; Q5RET9; -.
DR   STRING; 9601.ENSPPYP00000000167; -.
DR   GeneID; 100171633; -.
DR   KEGG; pon:100171633; -.
DR   CTD; 163859; -.
DR   eggNOG; KOG2827; Eukaryota.
DR   InParanoid; Q5RET9; -.
DR   Proteomes; UP000001595; Unplaced.
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; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   PROPEP          1..77
FT                   /note="UBL"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT                   /id="PRO_0000442523"
FT   CHAIN           78..451
FT                   /note="Replication stress response regulator SDE2"
FT                   /id="PRO_0000286086"
FT   DOMAIN          396..430
FT                   /note="SAP"
FT                   /evidence="ECO:0000255"
FT   REGION          182..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          109..149
FT                   /evidence="ECO:0000255"
FT   MOTIF           39..52
FT                   /note="PIP-box"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   COMPBIAS        186..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            77..78
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1J5"
FT   MOD_RES         274
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   MOD_RES         319
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BJN8"
SQ   SEQUENCE   451 AA;  49821 MW;  B73AC83B041047FF CRC64;
     MAEAAALVWI RGPGFGCKAV RCASARCTVR DFIHRHCQDQ NVPVENFFVK CNGALIYTSD
     TVQHGAVYSL EPRLCGGKGG FGSMLRALGA QIEKTTNREA CRDLSGRRLR DVNHEKAMAE
     WVKQQAEREA EKEQKRLERL QRKLVEPKHC FTSPDYQQQC HEMAERLEDS VLKGMQAASS
     KMVSAEISEN RKRQWPTKSQ TDREASAGKR RYFWLGMEGL ETAEGSSSES SDDDSEEAPS
     TSGMGFHAPK IGGSGVEMAA KFPSGSQRAR VVNTDPGSPE QLQIPVTDSG RHISEDSCAE
     LGESKEHMES RMVTETEETQ EKKAESREPI EEEPTGAGLN KDKETEERTD GERVAEVACE
     ERENVAVAKL QESQPGNAVI DKETIDLLAF TSVAELELLG LEKLKCELMA LGLKCGGTLQ
     ERAARLFSVR GLAKEQIDPA LFAKPLKGKK K