ID   PTTG1_GORGO             Reviewed;         202 AA.
AC   A1YF19;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Securin;
DE   AltName: Full=Pituitary tumor-transforming gene 1 protein;
GN   Name=PTTG1;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory protein, which plays a central role in chromosome
CC       stability, in the p53/TP53 pathway, and DNA repair. Probably acts by
CC       blocking the action of key proteins. During the mitosis, it blocks
CC       Separase/ESPL1 function, preventing the proteolysis of the cohesin
CC       complex and the subsequent segregation of the chromosomes. At the onset
CC       of anaphase, it is ubiquitinated, conducting to its destruction and to
CC       the liberation of ESPL1. Its function is however not limited to a
CC       blocking activity, since it is required to activate ESPL1. Negatively
CC       regulates the transcriptional activity and related apoptosis activity
CC       of TP53. The negative regulation of TP53 may explain the strong
CC       transforming capability of the protein when it is overexpressed. May
CC       also play a role in DNA repair via its interaction with Ku, possibly by
CC       connecting DNA damage-response pathways with sister chromatid
CC       separation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RPS10 and DNAJA1 (By similarity). Interacts
CC       with the caspase-like ESPL1, and prevents its protease activity
CC       probably by covering its active site. Interacts with TP53 and blocks
CC       its activity probably by blocking its binding to DNA. Interacts with
CC       the Ku 70 kDa subunit of ds-DNA kinase. Interacts with PTTG1IP (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal destruction box (D-box) acts as a recognition
CC       signal for degradation via the ubiquitin-proteasome pathway.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The TEK-boxes are required for 'Lys-11'-linked ubiquitination
CC       and facilitate the transfer of the first ubiquitin and ubiquitin chain
CC       nucleation. TEK-boxes may direct a catalytically competent orientation
CC       of the UBE2C/UBCH10-ubiquitin thioester with the acceptor lysine
CC       residue (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-165 by CDK1 during mitosis. {ECO:0000250}.
CC   -!- PTM: Phosphorylated in vitro by ds-DNA kinase. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by
CC       the anaphase promoting complex (APC) at the onset of anaphase,
CC       conducting to its degradation. 'Lys-11'-linked ubiquitination is
CC       mediated by the E2 ligase UBE2C/UBCH10 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the securin 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; DQ976507; ABM46737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YF19; -.
DR   STRING; 9593.ENSGGOP00000016528; -.
DR   eggNOG; ENOG502S2GG; Eukaryota.
DR   InParanoid; A1YF19; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR   GO; GO:2000816; P:negative regulation of mitotic sister chromatid separation; IBA:GO_Central.
DR   InterPro; IPR006940; Securin_separation_inhibitor.
DR   PANTHER; PTHR10418; PTHR10418; 1.
DR   Pfam; PF04856; Securin; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Repeat; SH3-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95997"
FT   CHAIN           2..202
FT                   /note="Securin"
FT                   /id="PRO_0000285529"
FT   REGION          35..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           61..64
FT                   /note="D-box"
FT   MOTIF           71..73
FT                   /note="TEK-box 1"
FT   MOTIF           94..96
FT                   /note="TEK-box 2"
FT   MOTIF           163..173
FT                   /note="SH3-binding"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95997"
FT   MOD_RES         165
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:O95997"
SQ   SEQUENCE   202 AA;  22038 MW;  E1B2301F6F508A03 CRC64;
     MATLIYVDKE NGEPGTRVAA KDGLKLGSAP SIKALDGRSQ VSTPRFGKTF DAPPALPKAT
     RKALGTVNRA TEKSVKTKGP LKQKQPSFSA KKMTEKTVKA KSSVPASDDA YPEIEKFFPF
     NPLDFESFDL PEEHQIAHLP LSGVPLMILD EERELEKLFQ LGPPSPVRMP SPPWESNLLQ
     SPSSILSTLD VELPPVCCDI DI