DEPP1_MOUSE
ID DEPP1_MOUSE Reviewed; 205 AA.
AC Q8K2F3; Q8BU66;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein DEPP1 {ECO:0000305};
DE AltName: Full=Fat-specific-expressed gene protein {ECO:0000303|Ref.1};
DE AltName: Full=Protein DEPP;
GN Name=Depp1; Synonyms=Depp, Fseg;
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].
RC TISSUE=Adipose tissue;
RA Matsuda M., Kuriyama H., Kishida K., Funahashi T., Shimomura I.,
RA Yamashita S., Matsuzawa Y.;
RT "Molecular cloning and characterization of a novel fat-specific expressed
RT gene transcript.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and C57BL/6J; TISSUE=Brain, and Mammary tumor;
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).
RN [4]
RP INDUCTION BY HYPOXIA.
RX PubMed=24530860; DOI=10.1016/j.bbamcr.2014.02.003;
RA Stepp M.W., Folz R.J., Yu J., Zelko I.N.;
RT "The c10orf10 gene product is a new link between oxidative stress and
RT autophagy.";
RL Biochim. Biophys. Acta 1843:1076-1088(2014).
CC -!- FUNCTION: Acts as a critical modulator of FOXO3-induced autophagy via
CC increased cellular ROS. {ECO:0000250|UniProtKB:Q9NTK1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NTK1}.
CC Peroxisome {ECO:0000250|UniProtKB:Q9NTK1}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9NTK1}. Note=May localize to aggresomes.
CC {ECO:0000250|UniProtKB:Q9NTK1}.
CC -!- INDUCTION: Up-regulated by hypoxia. {ECO:0000269|PubMed:24530860}.
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DR EMBL; AB024924; BAC87793.1; -; mRNA.
DR EMBL; AK078806; BAC37402.1; -; mRNA.
DR EMBL; AK087284; BAC39837.1; -; mRNA.
DR EMBL; BC031533; AAH31533.1; -; mRNA.
DR EMBL; BC058515; AAH58515.1; -; mRNA.
DR CCDS; CCDS51882.1; -.
DR RefSeq; NP_001160052.1; NM_001166580.1.
DR RefSeq; NP_666092.1; NM_145980.2.
DR AlphaFoldDB; Q8K2F3; -.
DR SMR; Q8K2F3; -.
DR STRING; 10090.ENSMUSP00000070203; -.
DR iPTMnet; Q8K2F3; -.
DR PhosphoSitePlus; Q8K2F3; -.
DR PaxDb; Q8K2F3; -.
DR PRIDE; Q8K2F3; -.
DR Antibodypedia; 62493; 27 antibodies from 12 providers.
DR DNASU; 213393; -.
DR Ensembl; ENSMUST00000067354; ENSMUSP00000070203; ENSMUSG00000048489.
DR Ensembl; ENSMUST00000178241; ENSMUSP00000136165; ENSMUSG00000048489.
DR GeneID; 213393; -.
DR KEGG; mmu:213393; -.
DR UCSC; uc009dkp.2; mouse.
DR CTD; 11067; -.
DR MGI; MGI:1918730; Depp1.
DR VEuPathDB; HostDB:ENSMUSG00000048489; -.
DR eggNOG; ENOG502T1TA; Eukaryota.
DR GeneTree; ENSGT00390000017909; -.
DR HOGENOM; CLU_114587_0_0_1; -.
DR InParanoid; Q8K2F3; -.
DR OMA; PHRQMDS; -.
DR OrthoDB; 1362909at2759; -.
DR PhylomeDB; Q8K2F3; -.
DR BioGRID-ORCS; 213393; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8K2F3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8K2F3; protein.
DR Bgee; ENSMUSG00000048489; Expressed in ciliary body and 215 other tissues.
DR ExpressionAtlas; Q8K2F3; baseline and differential.
DR Genevisible; Q8K2F3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR InterPro; IPR020133; DEPP.
DR PANTHER; PTHR15426; PTHR15426; 1.
DR Pfam; PF15343; DEPP; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Mitochondrion; Peroxisome; Reference proteome.
FT CHAIN 1..205
FT /note="Protein DEPP1"
FT /id="PRO_0000079868"
FT REGION 55..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 177..205
FT /note="CRALASVSSSRPSSILGTLYLHLPVIHEL -> LPGLSVRLQLSPHQYPRYS
FT LFAPPSDP (in Ref. 2; BAC39837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 205 AA; 22525 MW; 98276B47B74C873F CRC64;
MRSRLLLPVP HLPTIREMSE ELSHGAAGQE PPASPSLDDY VRCICQLAQP TSVLDKVTAQ
SRPNRPSRPA WTREKRRQAE SPGDSSLCVS SLQPTLPSPG TDNPLDWLFG KSQGEQADGR
GRPNRTGSSD PWDVPRQMGK DTGRLCEARV PEHSLGRKPG PRHQTSDLKS WTSRKSCRAL
ASVSSSRPSS ILGTLYLHLP VIHEL
