NDRG2_RAT
ID NDRG2_RAT Reviewed; 371 AA.
AC Q8VBU2; Q8VBW2; Q8VI00; Q8VI01;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein NDRG2;
DE AltName: Full=Antidepressant-related protein ADRG123;
DE AltName: Full=N-myc downstream-regulated gene 2 protein;
DE AltName: Full=NDRG1-related protein;
GN Name=Ndrg2;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=12072429; DOI=10.1074/jbc.m200272200;
RA Boulkroun S., Fay M., Zennaro M.-C., Escoubet B., Jaisser F.,
RA Blot-Chabaud M., Farman N., Courtois-Coutry N.;
RT "Characterization of rat NDRG2 (N-Myc downstream regulated gene 2), a novel
RT early mineralocorticoid-specific induced gene.";
RL J. Biol. Chem. 277:31506-31515(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INDUCTION.
RX PubMed=15769300; DOI=10.1017/s1461145705005134;
RA Takahashi K., Yamada M., Ohata H., Momose K., Higuchi T., Honda K.,
RA Yamada M.;
RT "Expression of Ndrg2 in the rat frontal cortex after antidepressant and
RT electroconvulsive treatment.";
RL Int. J. Neuropsychopharmacol. 8:381-389(2005).
RN [3]
RP PROTEIN SEQUENCE OF 62-76 AND 155-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 1), AND PHOSPHORYLATION AT
RP SER-332.
RX PubMed=14985363; DOI=10.1074/jbc.m401504200;
RA Burchfield J.G., Lennard A.J., Narasimhan S., Hughes W.E., Wasinger V.C.,
RA Corthals G.L., Okuda T., Kondoh H., Biden T.J., Schmitz-Peiffer C.;
RT "Akt mediates insulin-stimulated phosphorylation of Ndrg2: evidence for
RT cross-talk with protein kinase C theta.";
RL J. Biol. Chem. 279:18623-18632(2004).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16039777; DOI=10.1016/j.neulet.2005.06.055;
RA Takahashi K., Yamada M., Ohata H., Honda K., Yamada M.;
RT "Ndrg2 promotes neurite outgrowth of NGF-differentiated PC12 cells.";
RL Neurosci. Lett. 388:157-162(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-326; SER-328;
RP THR-330; SER-332 AND SER-338, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Contributes to the regulation of the Wnt signaling pathway.
CC Down-regulates CTNNB1-mediated transcriptional activation of target
CC genes, such as CCND1, and may thereby act as tumor suppressor (By
CC similarity). May be involved in dendritic cell and neuron
CC differentiation. {ECO:0000250, ECO:0000269|PubMed:16039777}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell projection, growth cone. Note=In neurons,
CC seems to concentrate at axonal growth cone.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ndrg2L;
CC IsoId=Q8VBU2-1; Sequence=Displayed;
CC Name=2; Synonyms=Ndrg2S;
CC IsoId=Q8VBU2-2; Sequence=VSP_019032;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in heart,
CC liver, skeletal muscle and aorta. {ECO:0000269|PubMed:12072429}.
CC -!- INDUCTION: Up-regulated by aldosterone in kidney and colon, but not in
CC heart. Down-regulated in cortex by antidepressant treatments.
CC {ECO:0000269|PubMed:12072429, ECO:0000269|PubMed:15769300}.
CC -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
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DR EMBL; AJ426424; CAD19997.1; -; mRNA.
DR EMBL; AJ426425; CAD19998.1; -; mRNA.
DR EMBL; AJ426426; CAD19999.1; -; mRNA.
DR EMBL; AJ426427; CAD20000.1; -; mRNA.
DR EMBL; AF334105; AAL73186.1; -; mRNA.
DR EMBL; AF334106; AAL73187.1; -; mRNA.
DR RefSeq; NP_001257791.1; NM_001270862.1.
DR RefSeq; NP_001257792.1; NM_001270863.1.
DR RefSeq; NP_001257793.1; NM_001270864.1.
DR RefSeq; NP_598267.2; NM_133583.2.
DR AlphaFoldDB; Q8VBU2; -.
DR SMR; Q8VBU2; -.
DR BioGRID; 251122; 3.
DR IntAct; Q8VBU2; 2.
DR MINT; Q8VBU2; -.
DR STRING; 10116.ENSRNOP00000042949; -.
DR ESTHER; ratno-NDRG2; Ndr_family.
DR iPTMnet; Q8VBU2; -.
DR PhosphoSitePlus; Q8VBU2; -.
DR SwissPalm; Q8VBU2; -.
DR PaxDb; Q8VBU2; -.
DR PRIDE; Q8VBU2; -.
DR GeneID; 171114; -.
DR KEGG; rno:171114; -.
DR UCSC; RGD:621874; rat. [Q8VBU2-1]
DR CTD; 57447; -.
DR RGD; 621874; Ndrg2.
DR eggNOG; KOG2931; Eukaryota.
DR InParanoid; Q8VBU2; -.
DR OrthoDB; 854690at2759; -.
DR PhylomeDB; Q8VBU2; -.
DR TreeFam; TF313168; -.
DR PRO; PR:Q8VBU2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0090361; P:regulation of platelet-derived growth factor production; ISO:RGD.
DR GO; GO:0010574; P:regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004142; NDRG.
DR InterPro; IPR030690; NDRG2.
DR PANTHER; PTHR11034; PTHR11034; 1.
DR PANTHER; PTHR11034:SF17; PTHR11034:SF17; 1.
DR Pfam; PF03096; Ndr; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Neurogenesis; Phosphoprotein; Reference proteome; Tumor suppressor;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT CHAIN 2..371
FT /note="Protein NDRG2"
FT /id="PRO_0000441171"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14985363,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT VAR_SEQ 26..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12072429,
FT ECO:0000303|PubMed:15769300"
FT /id="VSP_019032"
FT CONFLICT 121
FT /note="Q -> L (in Ref. 2; AAL73186/AAL73187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 40779 MW; C049A1AAF37D115A CRC64;
MAELQEVQIT EEKPLLPGQT PEAAKEAELA ARILLDQGQT HSVETPYGSV TFTVYGTPKP
KRPAIFTYHD VGLNYKSCFQ PLFQFGDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS
QDQLADMIPC ILQYLNFSTI IGVGVGAGAY ILSRYALNHP DTVEGLVLIN IDPNAKGWMD
WAAHKLTGLT SSIPEMILGH LFSQEELSGN SELIQKYRSL ITHAPNLENI ELYWNSYNNR
RDLNFERGGE MTLKCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP
GKLTEAFKYF VQGMGYMASS CMTRLSRSRT ASLTSAASID GSRSRSRTLS QSSESGTLPS
GPPGHTMEVS C
