T53I1_MOUSE
ID T53I1_MOUSE Reviewed; 239 AA.
AC Q9QXE4; Q923I6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=10630289; DOI=10.1007/s002510050601;
RA Carrier A., Nguyen C., Victorero G., Granjeaud S., Rocha D., Bernard K.,
RA Miazek A., Ferrier P., Malissen M., Naquet P., Malissen B., Jordan B.R.;
RT "Differential gene expression in CD3epsilon- and RAG1-deficient thymuses:
RT definition of a set of genes potentially involved in thymocyte
RT maturation.";
RL Immunogenetics 50:255-270(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX PubMed=11557757; DOI=10.1074/jbc.m105647200;
RA Tomasini R., Samir A.A., Vaccaro M.I., Pebusque M.-J., Dagorn J.-C.,
RA Iovanna J.L., Dusetti N.J.;
RT "Molecular and functional characterization of the stress-induced protein
RT (SIP) gene and its two transcripts generated by alternative splicing. SIP
RT induced by stress and promotes cell death.";
RL J. Biol. Chem. 276:44185-44192(2001).
RN [3]
RP FUNCTION.
RX PubMed=16044147; DOI=10.1038/sj.onc.1208951;
RA Tomasini R., Seux M., Nowak J., Bontemps C., Carrier A., Dagorn J.C.,
RA Pebusque M.J., Iovanna J.L., Dusetti N.J.;
RT "TP53INP1 is a novel p73 target gene that induces cell cycle arrest and
RT cell death by modulating p73 transcriptional activity.";
RL Oncogene 24:8093-8104(2005).
RN [4]
RP FUNCTION.
RX PubMed=19118006; DOI=10.1158/0008-5472.can-08-2320;
RA Cano C.E., Gommeaux J., Pietri S., Culcasi M., Garcia S., Seux M.,
RA Barelier S., Vasseur S., Spoto R.P., Pebusque M.J., Dusetti N.J.,
RA Iovanna J.L., Carrier A.;
RT "Tumor protein 53-induced nuclear protein 1 is a major mediator of p53
RT antioxidant function.";
RL Cancer Res. 69:219-226(2009).
RN [5]
RP FUNCTION.
RX PubMed=21339733; DOI=10.1038/onc.2011.25;
RA Seux M., Peuget S., Montero M.P., Siret C., Rigot V., Clerc P., Gigoux V.,
RA Pellegrino E., Pouyet L., N'Guessan P., Garcia S., Dufresne M.,
RA Iovanna J.L., Carrier A., Andre F., Dusetti N.J.;
RT "TP53INP1 decreases pancreatic cancer cell migration by regulating SPARC
RT expression.";
RL Oncogene 30:3049-3061(2011).
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. {ECO:0000269|PubMed:11557757, ECO:0000269|PubMed:16044147,
CC ECO:0000269|PubMed:19118006, ECO:0000269|PubMed:21339733}.
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:0000269|PubMed:11557757}. Nucleus, PML body {ECO:0000250}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=Shuttles between
CC the nucleus and the cytoplasm, depending on cellular stress conditions,
CC and re-localizes to autophagosomes on autophagy activation.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SIP27, TEAP;
CC IsoId=Q9QXE4-1; Sequence=Displayed;
CC Name=2; Synonyms=SIP18;
CC IsoId=Q9QXE4-2; Sequence=VSP_013177;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in the
CC thymus. {ECO:0000269|PubMed:10630289, ECO:0000269|PubMed:11557757}.
CC -!- INDUCTION: By adriamycin, methymethane sulfonate, ethanol, H(2)O(2),
CC ultraviolet irradiation and heat shock. Rapidly induced in acinar cells
CC of the pancreas with acute pancreatitis upon caerulein treatment.
CC {ECO:0000269|PubMed:11557757}.
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; AJ131776; CAB66138.1; -; mRNA.
DR EMBL; AY034611; AAK60419.1; -; mRNA.
DR EMBL; AY034612; AAK60420.1; -; mRNA.
DR CCDS; CCDS17964.1; -. [Q9QXE4-1]
DR RefSeq; NP_001186034.1; NM_001199105.1. [Q9QXE4-2]
DR RefSeq; NP_068697.1; NM_021897.3. [Q9QXE4-1]
DR AlphaFoldDB; Q9QXE4; -.
DR SMR; Q9QXE4; -.
DR STRING; 10090.ENSMUSP00000029865; -.
DR PhosphoSitePlus; Q9QXE4; -.
DR PaxDb; Q9QXE4; -.
DR PRIDE; Q9QXE4; -.
DR Antibodypedia; 12951; 357 antibodies from 38 providers.
DR DNASU; 60599; -.
DR Ensembl; ENSMUST00000029865; ENSMUSP00000029865; ENSMUSG00000028211. [Q9QXE4-1]
DR GeneID; 60599; -.
DR KEGG; mmu:60599; -.
DR UCSC; uc008ryz.1; mouse. [Q9QXE4-1]
DR UCSC; uc008rzb.1; mouse. [Q9QXE4-2]
DR CTD; 60599; -.
DR MGI; MGI:1926609; Trp53inp1.
DR VEuPathDB; HostDB:ENSMUSG00000028211; -.
DR eggNOG; ENOG502QTG4; Eukaryota.
DR GeneTree; ENSGT00530000063829; -.
DR HOGENOM; CLU_091034_1_0_1; -.
DR InParanoid; Q9QXE4; -.
DR OMA; TCHSLNE; -.
DR PhylomeDB; Q9QXE4; -.
DR TreeFam; TF333017; -.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR BioGRID-ORCS; 60599; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trp53inp1; mouse.
DR PRO; PR:Q9QXE4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QXE4; protein.
DR Bgee; ENSMUSG00000028211; Expressed in stroma of bone marrow and 262 other tissues.
DR ExpressionAtlas; Q9QXE4; baseline and differential.
DR Genevisible; Q9QXE4; MM.
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; IDA:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IMP: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; IDA:MGI.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IDA:MGI.
DR GO; GO:0072703; P:cellular response to methyl methanesulfonate; IDA:MGI.
DR GO; GO:0034644; P:cellular response to UV; IDA:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; IDA:MGI.
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; Alternative splicing; Antioxidant; Apoptosis; Autophagy;
KW Cytoplasm; 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_0000072407"
FT MOTIF 25..37
FT /note="LIR"
FT VAR_SEQ 158..239
FT /note="MEAQSEMGKHIHCCVAALAAQATFLEQPKSFRPSQWIKGHSERQSLNRNGLR
FT RQNLTRDCHTRQMKHSGWVVHQPCPRQYNY -> ARKSCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11557757"
FT /id="VSP_013177"
SQ SEQUENCE 239 AA; 26935 MW; 71F25DB7600D7C7B CRC64;
MFQRLNKMFV GEVTTSSSQE PEFSEKEDDE WILVDFIDTC PGFSAEEEEE DEDIGEESSA
EHTSVFSCLP ASLECLTDTS DSCFLQFESC PMEESWFITP PPCFTAGGLT TIKVETSPME
NLLIEHPSMS VYAVHNSCPG LSEASCGNDE YNSSGPRMEA QSEMGKHIHC CVAALAAQAT
FLEQPKSFRP SQWIKGHSER QSLNRNGLRR QNLTRDCHTR QMKHSGWVVH QPCPRQYNY
