T53I1_RAT
ID T53I1_RAT Reviewed; 239 AA.
AC Q80YE2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Tumor protein p53-inducible nuclear protein 1;
DE AltName: Full=Stress-induced protein;
DE AltName: Full=Thymus-expressed acidic protein;
DE Short=TEAP;
DE AltName: Full=p53-dependent damage-inducible nuclear protein 1;
DE Short=p53DINP1;
GN Name=Trp53inp1; Synonyms=Sip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Wakizono T., Suzuki G., Nibuya M., Nomura S.;
RT "Cloning of rat SIP protein.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15254349;
RA Jiang P.-H., Motoo Y., Iovanna J.L., Pebusque M.-J., Xie M.-J., Okada G.,
RA Sawabu N.;
RT "Tumor protein p53-induced nuclear protein 1 (TP53INP1) in spontaneous
RT chronic pancreatitis in the WBN/Kob rat: drug effects on its expression in
RT the pancreas.";
RL J. Pancreas 5:205-216(2004).
CC -!- FUNCTION: Antiproliferative and proapoptotic protein involved in cell
CC stress response which acts as a dual regulator of transcription and
CC autophagy. Acts as a positive regulator of autophagy. In response to
CC cellular stress or activation of autophagy, relocates to autophagosomes
CC where it interacts with autophagosome-associated proteins GABARAP,
CC GABARAPL1/L2, MAP1LC3A/B/C and regulates autophagy. Acts as an
CC antioxidant and plays a major role in p53/TP53-driven oxidative stress
CC response. Possesses both a p53/TP53-independent intracellular reactive
CC oxygen species (ROS) regulatory function and a p53/TP53-dependent
CC transcription regulatory function. Positively regulates p53/TP53 and
CC p73/TP73 and stimulates their capacity to induce apoptosis and regulate
CC cell cycle. In response to double-strand DNA breaks, promotes p53/TP53
CC phosphorylation on 'Ser-46' and subsequent apoptosis. Acts as a tumor
CC suppressor by inducing cell death by an autophagy and caspase-dependent
CC mechanism. Can reduce cell migration by regulating the expression of
CC SPARC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with p53/TP53 and HIPK2. Interacts with PRKCG,
CC GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250}. Note=Shuttles between the nucleus and the
CC cytoplasm, depending on cellular stress conditions, and re-localizes to
CC autophagosomes on autophagy activation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed by acinar cells of chronic
CC pancreatitis tissue. {ECO:0000269|PubMed:15254349}.
CC -!- INDUCTION: In chronic pancreatitis tissue, expression is suppressed by
CC camostat mesilate, a serine protease inhibitor, and by Saiko-keishi-to,
CC a herbal medicine. {ECO:0000269|PubMed:15254349}.
CC -!- DOMAIN: The LC3 interacting region (LIR) motif mediates interaction
CC with GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C.
CC {ECO:0000250}.
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DR EMBL; AB107917; BAC75468.1; -; mRNA.
DR RefSeq; NP_851598.1; NM_181084.2.
DR AlphaFoldDB; Q80YE2; -.
DR STRING; 10116.ENSRNOP00000010591; -.
DR PhosphoSitePlus; Q80YE2; -.
DR PaxDb; Q80YE2; -.
DR GeneID; 297822; -.
DR KEGG; rno:297822; -.
DR UCSC; RGD:631423; rat.
DR CTD; 94241; -.
DR RGD; 631423; Trp53inp1.
DR eggNOG; ENOG502QTG4; Eukaryota.
DR InParanoid; Q80YE2; -.
DR OrthoDB; 1537138at2759; -.
DR PhylomeDB; Q80YE2; -.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q80YE2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0048102; P:autophagic cell death; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0071361; P:cellular response to ethanol; ISO:RGD.
DR GO; GO:0071447; P:cellular response to hydroperoxide; ISO:RGD.
DR GO; GO:0072703; P:cellular response to methyl methanesulfonate; ISO:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR InterPro; IPR029431; TP53INP.
DR InterPro; IPR029556; TP53INP1.
DR PANTHER; PTHR31671; PTHR31671; 1.
DR PANTHER; PTHR31671:SF0; PTHR31671:SF0; 1.
DR Pfam; PF14839; DOR; 1.
PE 2: Evidence at transcript level;
KW Activator; Antioxidant; Apoptosis; Autophagy; Cytoplasm;
KW Cytoplasmic vesicle; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..239
FT /note="Tumor protein p53-inducible nuclear protein 1"
FT /id="PRO_0000072408"
FT MOTIF 25..37
FT /note="LIR"
SQ SEQUENCE 239 AA; 26976 MW; 593502B9798B55B5 CRC64;
MFQRLNKMFV GEVTTSSSHE PEFSEKEDDE WILVDFIDTC TGFSAEEEEE DEDIGEESSA
EHTSVFSCLP TSLECLADTS DSCFLQFESC PMEESWFITP PPCFTAGGLT TIKVETSPME
NLLIEHPSMS VYAVHNSCPG LSEASCGNDD YNSSGPRMEA QSELGTHIHC CVAALAAQAT
FLEQPKSFRP SQWIKGHSER QSLNRNGLRR QNLTRDCHTR QMKHRCWAVH QPCPRQYNY
