DPTOR_MOUSE
ID DPTOR_MOUSE Reviewed; 409 AA.
AC Q570Y9; Q3UM00; Q3UT08;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DEP domain-containing mTOR-interacting protein;
DE AltName: Full=DEP domain-containing protein 6;
GN Name=Deptor; Synonyms=Depdc6, Kiaa4200;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-265; SER-280 AND
RP SER-293, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=30232230; DOI=10.1126/scitranslmed.aat9356;
RA Csukasi F., Duran I., Barad M., Barta T., Gudernova I., Trantirek L.,
RA Martin J.H., Kuo C.Y., Woods J., Lee H., Cohn D.H., Krejci P., Krakow D.;
RT "The PTH/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR
RT signaling.";
RL Sci. Transl. Med. 10:0-0(2018).
CC -!- FUNCTION: Negative regulator of the mTORC1 and mTORC2 signaling
CC pathways. Inhibits the kinase activity of both complexes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. Part of
CC the mammalian target of rapamycin complex 2 (mTORC2) which contains
CC MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and DEPTOR. Interacts (via PDZ
CC domain) with MTOR; interacts with MTOR within both mammalian target of
CC rapamycin complexes mTORC1 and mTORC2 (By similarity). Interacts (via
CC PDZ domain) with MINAR1 (via N-terminus) (By similarity). Interacts
CC with SIK3 (By similarity). {ECO:0000250|UniProtKB:Q8TB45}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q570Y9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q570Y9-2; Sequence=VSP_024648;
CC Name=3;
CC IsoId=Q570Y9-3; Sequence=VSP_024649;
CC -!- DEVELOPMENTAL STAGE: At postnatal day 1 (P1), in cartilage growth
CC plate, primarily expressed in resting and proliferating chondrocytes.
CC This expression pattern is maintained at least until P21 (at protein
CC level). {ECO:0000269|PubMed:30232230}.
CC -!- PTM: Phosphorylation weakens interaction with MTOR within mTORC1 and
CC mTORC2. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q8TB45}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90225.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220300; BAD90225.1; ALT_INIT; mRNA.
DR EMBL; AK139888; BAE24172.1; -; mRNA.
DR EMBL; AK145208; BAE26298.1; -; mRNA.
DR CCDS; CCDS27474.1; -. [Q570Y9-1]
DR CCDS; CCDS27475.1; -. [Q570Y9-2]
DR RefSeq; NP_001033026.1; NM_001037937.3. [Q570Y9-2]
DR RefSeq; NP_663445.2; NM_145470.3. [Q570Y9-1]
DR AlphaFoldDB; Q570Y9; -.
DR SMR; Q570Y9; -.
DR BioGRID; 220946; 1.
DR STRING; 10090.ENSMUSP00000094167; -.
DR iPTMnet; Q570Y9; -.
DR PhosphoSitePlus; Q570Y9; -.
DR MaxQB; Q570Y9; -.
DR PaxDb; Q570Y9; -.
DR PRIDE; Q570Y9; -.
DR ProteomicsDB; 277606; -. [Q570Y9-1]
DR ProteomicsDB; 277607; -. [Q570Y9-2]
DR ProteomicsDB; 277608; -. [Q570Y9-3]
DR Antibodypedia; 13704; 281 antibodies from 32 providers.
DR DNASU; 97998; -.
DR Ensembl; ENSMUST00000023056; ENSMUSP00000023056; ENSMUSG00000022419. [Q570Y9-2]
DR Ensembl; ENSMUST00000096433; ENSMUSP00000094167; ENSMUSG00000022419. [Q570Y9-1]
DR GeneID; 97998; -.
DR KEGG; mmu:97998; -.
DR UCSC; uc007vsb.2; mouse. [Q570Y9-1]
DR CTD; 64798; -.
DR MGI; MGI:2146322; Deptor.
DR VEuPathDB; HostDB:ENSMUSG00000022419; -.
DR eggNOG; ENOG502QS4Y; Eukaryota.
DR GeneTree; ENSGT00520000055667; -.
DR HOGENOM; CLU_042535_0_0_1; -.
DR InParanoid; Q570Y9; -.
DR OMA; DTHDSPF; -.
DR PhylomeDB; Q570Y9; -.
DR BioGRID-ORCS; 97998; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Deptor; mouse.
DR PRO; PR:Q570Y9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q570Y9; protein.
DR Bgee; ENSMUSG00000022419; Expressed in lacrimal gland and 221 other tissues.
DR ExpressionAtlas; Q570Y9; baseline and differential.
DR Genevisible; Q570Y9; MM.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISO:MGI.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:1903940; P:negative regulation of TORC2 signaling; ISO:MGI.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR CDD; cd04442; DEP_1_DEP6; 1.
DR CDD; cd04441; DEP_2_DEP6; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR037589; DEPTOR.
DR InterPro; IPR037335; DEPTOR_DEP_1.
DR InterPro; IPR037336; DEPTOR_DEP_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22829:SF18; PTHR22829:SF18; 1.
DR Pfam; PF00610; DEP; 2.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..409
FT /note="DEP domain-containing mTOR-interacting protein"
FT /id="PRO_0000284785"
FT DOMAIN 36..119
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 146..219
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 330..407
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB45"
FT VAR_SEQ 1..40
FT /note="MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQL -> MKQAFLVV
FT LRHSISEDRLPPLSVITSGC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024648"
FT VAR_SEQ 368..409
FT /note="VCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELDC -> DTGTES
FT RKIVTSRLAWATWQDLMGGKVGGDAIPI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024649"
FT CONFLICT 11
FT /note="S -> G (in Ref. 2; BAE26298)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> P (in Ref. 2; BAE26298)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="S -> N (in Ref. 2; BAE26298)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="T -> I (in Ref. 2; BAE26298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 46120 MW; 072062418DADDF8E CRC64;
MEEGSSGGSG SSDSNAGGSG GVQQRELERM AEVLVTGEQL RLRLHEEKVI KDRRHHLKTY
PNCFVAKELI DWLIEHKEAS DRETAIKLMQ KLADRGIIHH VCDEHKEFKD VKLFYRFRKD
DGTFALDSEV KAFMRGQRLY EKLMSPETTL LQPREEEGVK YERTFMASEF LDWLVQEGEA
TTRKEAEQLC HRLMDHGIIQ HVSNKHPFVD SNLLYQFRMN FRRRRRLMEL LNETSPSSQE
THDSPFCLRK QSHDSRKSTS FMSVSPSKEI KIVSAVRRSS MSSCGSSGYF SSSPTLSSSP
PVLCNPKSVL KRPVTSEELL TPGAPYARKT FTIVGDAVGW GFVVRGSKPC HIQAVDPSGP
AAAAGMKVCQ FVVSVNGLNV LNVDYRTVSN LILTGPRTIV MEVMEELDC
