T53I2_MOUSE
ID T53I2_MOUSE Reviewed; 221 AA.
AC Q8CFU8; Q3TDL6; Q711P5; Q8CHM4;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tumor protein p53-inducible nuclear protein 2;
DE AltName: Full=Diabetes and obesity-regulated protein;
GN Name=Tp53inp2; Synonyms=Dor, Trp53inp2;
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 2), AND FUNCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RA Burghardt H.E., Baumgartner B.G., Bach D., Pich S., Zorzano A.;
RT "A novel transcription factor in mouse.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryonic heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CFU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CFU8-2; Sequence=VSP_007752;
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; AJ297793; CAC82594.1; -; mRNA.
DR EMBL; AJ311669; CAC84145.1; -; Genomic_DNA.
DR EMBL; AL845325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK146589; BAE27284.1; -; mRNA.
DR EMBL; AK170132; BAE41585.1; -; mRNA.
DR EMBL; BC036958; AAH36958.2; -; mRNA.
DR EMBL; BC043086; AAH43086.1; -; mRNA.
DR CCDS; CCDS16947.1; -. [Q8CFU8-1]
DR RefSeq; NP_835212.1; NM_178111.3. [Q8CFU8-1]
DR RefSeq; XP_006500176.1; XM_006500113.3. [Q8CFU8-1]
DR AlphaFoldDB; Q8CFU8; -.
DR SMR; Q8CFU8; -.
DR BioGRID; 213017; 4.
DR IntAct; Q8CFU8; 3.
DR MINT; Q8CFU8; -.
DR STRING; 10090.ENSMUSP00000037627; -.
DR iPTMnet; Q8CFU8; -.
DR PhosphoSitePlus; Q8CFU8; -.
DR MaxQB; Q8CFU8; -.
DR PaxDb; Q8CFU8; -.
DR PRIDE; Q8CFU8; -.
DR ProteomicsDB; 254641; -. [Q8CFU8-1]
DR ProteomicsDB; 254642; -. [Q8CFU8-2]
DR Antibodypedia; 43096; 190 antibodies from 20 providers.
DR Ensembl; ENSMUST00000043237; ENSMUSP00000037627; ENSMUSG00000038375. [Q8CFU8-1]
DR GeneID; 68728; -.
DR KEGG; mmu:68728; -.
DR UCSC; uc008nkk.1; mouse. [Q8CFU8-1]
DR CTD; 68728; -.
DR MGI; MGI:1915978; Trp53inp2.
DR VEuPathDB; HostDB:ENSMUSG00000038375; -.
DR eggNOG; ENOG502RZHB; Eukaryota.
DR GeneTree; ENSGT00530000063829; -.
DR HOGENOM; CLU_091034_0_0_1; -.
DR InParanoid; Q8CFU8; -.
DR OMA; EDPECPR; -.
DR OrthoDB; 1537138at2759; -.
DR PhylomeDB; Q8CFU8; -.
DR TreeFam; TF333017; -.
DR BioGRID-ORCS; 68728; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trp53inp2; mouse.
DR PRO; PR:Q8CFU8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CFU8; protein.
DR Bgee; ENSMUSG00000038375; Expressed in cardiac muscle of left ventricle and 264 other tissues.
DR ExpressionAtlas; Q8CFU8; baseline and differential.
DR Genevisible; Q8CFU8; 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; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IMP:MGI.
DR GO; GO:1903828; P:negative regulation of protein localization; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
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:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
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; Alternative splicing; Autophagy; Cytoplasm; Cytoplasmic vesicle;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..221
FT /note="Tumor protein p53-inducible nuclear protein 2"
FT /id="PRO_0000072410"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..210
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 COMPBIAS 177..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXH6"
FT VAR_SEQ 22..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18030323"
FT /id="VSP_007752"
FT CONFLICT 42
FT /note="D -> G (in Ref. 2; CAC84145)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="P -> S (in Ref. 1; CAC82594 and 2; CAC84145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 24288 MW; A4D3E1AD8E290E96 CRC64;
MFQRFTSLFF NTPAPPEDSN CPGAFVSEED EVDGWLIIDL QDSYTAPPDP GASPAPAGRP
PPAPSLMDES WFVTPPACFT AEGPGLGPAR LQSNPLEDLL IEHPSMSVYV TGSTIVLESG
PPSPHPEAAL PDQDLSDGEL APALREPRAL HHAAAPMPAR AVLLEKAGQV RRLQRARQRA
ERHTLSAKVL QRQNRARESR SRRPKHQGSF IYQPCQRQFN Y
