ID   PTTG1_PIG               Reviewed;         121 AA.
AC   Q9BDP6;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Securin;
DE   AltName: Full=Pituitary tumor-transforming gene 1 protein;
DE   Flags: Fragment;
GN   Name=PTTG1; Synonyms=PTTG;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Klima J., Anger M., Motlik J., Carnwath J.W., Niemann H.;
RT   "Porcine homolog for pituitary tumor-transforming protein (PTTG).";
RL   Submitted (JAN-2001) 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 p53/TP53. The negative regulation of p53/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 the caspase-like ESPL1, and prevents its
CC       protease activity probably by covering its active site. Interacts with
CC       p53/TP53 and blocks its activity probably by blocking its binding to
CC       DNA. Interacts with the Ku 70 kDa subunit of ds-DNA kinase. Interacts
CC       with PTTG1IP. Interacts with RPS10 and DNAJA1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 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}.
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DR   EMBL; AF339886; AAK17204.1; -; mRNA.
DR   AlphaFoldDB; Q9BDP6; -.
DR   STRING; 9823.ENSSSCP00000018044; -.
DR   PaxDb; Q9BDP6; -.
DR   eggNOG; ENOG502S2GG; Eukaryota.
DR   HOGENOM; CLU_1363209_0_0_1; -.
DR   InParanoid; Q9BDP6; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q9BDP6; SS.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm; DNA damage;
KW   DNA repair; Mitosis; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Repeat; SH3-binding; Ubl conjugation.
FT   CHAIN           <1..>121
FT                   /note="Securin"
FT                   /id="PRO_0000206363"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           3..5
FT                   /note="TEK-box 1"
FT   MOTIF           26..28
FT                   /note="TEK-box 2"
FT   MOTIF           95..105
FT                   /note="SH3-binding"
FT   COMPBIAS        106..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         97
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:O95997"
FT   NON_TER         1
FT   NON_TER         121
SQ   SEQUENCE   121 AA;  13564 MW;  4BC58532AF859D4F CRC64;
     RATEKSVKTN GPLKQKQTTF SAKKVTEKTV KAKSSVPASD DNYPEIEKFF PFNPLDFESF
     DLPEEHQIAH LPLNGVPLMV LREERELEQL LHLGPPSPLN MPSPPWESDV LQSPSSILST
     L