ID   T53I2_RAT               Reviewed;         199 AA.
AC   Q8CHM3;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Tumor protein p53-inducible nuclear protein 2;
DE   AltName: Full=Diabetes and obesity-regulated gene;
DE   Flags: Fragment;
GN   Name=Tp53inp2; Synonyms=Dor, Trp53inp2;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Muscle;
RX   PubMed=18030323; DOI=10.1371/journal.pone.0001183;
RA   Baumgartner B.G., Orpinell M., Duran J., Ribas V., Burghardt H.E., Bach D.,
RA   Villar A.V., Paz J.C., Gonzalez M., Camps M., Oriola J., Rivera F.,
RA   Palacin M., Zorzano A.;
RT   "Identification of a novel modulator of thyroid hormone receptor-mediated
RT   action.";
RL   PLoS ONE 2:E1183-E1183(2007).
CC   -!- FUNCTION: Dual regulator of transcription and autophagy. Positively
CC       regulates autophagy and is required for autophagosome formation and
CC       processing. May act as a scaffold protein that recruits MAP1LC3A,
CC       GABARAP and GABARAPL2 and brings them to the autophagosome membrane by
CC       interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase
CC       class III complex, they trigger autophagosome development. Acts as a
CC       transcriptional activator of THRA. {ECO:0000269|PubMed:18030323}.
CC   -!- SUBUNIT: Interacts with VMP1, GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A,
CC       MAP1LC3B, MAP1LC3C and THRA. {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: Abundantly expressed in skeletal muscle and heart
CC       and expression is highly repressed in muscle from obese diabetic rats.
CC       {ECO:0000269|PubMed:18030323}.
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; AJ297794; CAC82596.1; -; mRNA.
DR   AlphaFoldDB; Q8CHM3; -.
DR   SMR; Q8CHM3; -.
DR   STRING; 10116.ENSRNOP00000052180; -.
DR   PaxDb; Q8CHM3; -.
DR   PeptideAtlas; Q8CHM3; -.
DR   UCSC; RGD:735085; rat.
DR   RGD; 735085; Tp53inp2.
DR   eggNOG; ENOG502RZHB; Eukaryota.
DR   InParanoid; Q8CHM3; -.
DR   PhylomeDB; Q8CHM3; -.
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:0043130; F:ubiquitin binding; ISO:RGD.
DR   GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; ISO:RGD.
DR   GO; GO:1903828; P:negative regulation of protein localization; ISO:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR   GO; GO:0010508; P:positive regulation of autophagy; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   InterPro; IPR029431; TP53INP.
DR   InterPro; IPR029558; TP53INP2.
DR   PANTHER; PTHR31671; PTHR31671; 1.
DR   PANTHER; PTHR31671:SF2; PTHR31671:SF2; 1.
DR   Pfam; PF14839; DOR; 1.
PE   2: Evidence at transcript level;
KW   Activator; Autophagy; Cytoplasm; Cytoplasmic vesicle; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..>199
FT                   /note="Tumor protein p53-inducible nuclear protein 2"
FT                   /id="PRO_0000072411"
FT   REGION          41..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           26..41
FT                   /note="LIR"
FT   COMPBIAS        49..63
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXH6"
FT   NON_TER         199
SQ   SEQUENCE   199 AA;  21624 MW;  6576FEFB92B87226 CRC64;
     MFQRFTSLFF STPAPPEDSN CPGAFVSEED EVDGWLIIDL QDSYTAPPDP RASPAPAGRP
     PPAPSLMDES WFVTPPACFT AEGPGLGPAR LQSNPLEDLL IEHPSMSVYV TGSTIVLESG
     PPSPHPEAAL PDQDLSDGEL APARREPRAL HHAAAPMPAR AVLLEKAGQV RRLQRARQRA
     ERHTLSAKVL QRQNRARES