SDE2_DANRE
ID SDE2_DANRE Reviewed; 467 AA.
AC Q7T293;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE Flags: Precursor;
GN Name=sde2; ORFNames=zgc:112095;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54640.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC054640; AAH54640.1; ALT_INIT; mRNA.
DR RefSeq; NP_001017752.2; NM_001017752.2.
DR AlphaFoldDB; Q7T293; -.
DR STRING; 7955.ENSDARP00000043773; -.
DR PaxDb; Q7T293; -.
DR Ensembl; ENSDART00000183044; ENSDARP00000149480; ENSDARG00000109881.
DR GeneID; 550448; -.
DR KEGG; dre:550448; -.
DR CTD; 163859; -.
DR ZFIN; ZDB-GENE-050417-270; sde2.
DR eggNOG; KOG2827; Eukaryota.
DR InParanoid; Q7T293; -.
DR OrthoDB; 1446978at2759; -.
DR PhylomeDB; Q7T293; -.
DR PRO; PR:Q7T293; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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_0000442525"
FT CHAIN 72..467
FT /note="Replication stress response regulator SDE2"
FT /id="PRO_0000286088"
FT DOMAIN 412..446
FT /note="SAP"
FT /evidence="ECO:0000255"
FT REGION 173..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..143
FT /evidence="ECO:0000255"
FT COILED 341..381
FT /evidence="ECO:0000255"
FT MOTIF 33..46
FT /note="PIP-box"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT COMPBIAS 219..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..392
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 467 AA; 51381 MW; 69E746E980CEBAD2 CRC64;
MELFVISPDL KFNNLTVAPD STVSDLIDHF TVKNGVSLTD FYVSSNGRLS RSNDLLQSGV
VYRLEPRLCG GKGGFGSMLR ALGAQIEKTT NREACRDLSG RRLRDVNHEK EMAEWLKKQA
DREAEKEQRR LERIQRKLAE PKHYFTDTNY EQQCHDLSER LEDSVLKGMQ ASSSGLVQAD
EGPSLKRANP TDSKKKAKKK CYWTGMAGLE EMASSSEGSD DSDSEVSPST SGASCSSGFP
KPVVSAHKAD PQEQPSSSSP AQRKHNQEEL QKRDKEECTS EISSSSSSPA ANNEKLNQEE
TNEISSSSSS PAPKPTEVNQ QEMETEMECT AQISSSSSSP AEHSEEEVQQ TAERVEKMAE
EVQKTAEEVQ KKTEESTAEI SPSSSIPEEK SQVLSQVEDP LDLLSVSGPE QLEALGLERL
KKELMERGMK CGGTLQERAA RLFSVKGLTP DQIDPSLLAK PSKGKKK
