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Database: UniProt
Entry: Q62433
LinkDB: Q62433
Original site: Q62433 
ID   NDRG1_MOUSE             Reviewed;         394 AA.
AC   Q62433; P97862;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-OCT-2014, entry version 117.
DE   RecName: Full=Protein NDRG1;
DE   AltName: Full=N-myc downstream-regulated gene 1 protein;
DE            Short=Protein Ndr1;
GN   Name=Ndrg1; Synonyms=Ndr1, Ndrl, Tdd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   AND INDUCTION.
RC   TISSUE=Embryo;
RX   PubMed=10381566; DOI=10.1016/S0925-4773(99)00025-8;
RA   Shimono A., Okuda T., Kondoh H.;
RT   "N-myc-dependent repression of ndr1, a gene identified by direct
RT   subtraction of whole mouse embryo cDNAs between wild type and N-myc
RT   mutant.";
RL   Mech. Dev. 83:39-52(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Hybridoma;
RX   PubMed=9144177; DOI=10.1073/pnas.94.10.4988;
RA   Lin T.-M., Chang C.;
RT   "Cloning and characterization of TDD5, an androgen target gene that is
RT   differentially repressed by testosterone and dihydrotestosterone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:4988-4993(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION AT THR-346; THR-356 AND THR-366, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15461589; DOI=10.1042/BJ20041057;
RA   Murray J.T., Campbell D.G., Morrice N., Auld G.C., Shpiro N.,
RA   Marquez R., Peggie M., Bain J., Bloomberg G.B., Grahammer F., Lang F.,
RA   Wulff P., Kuhl D., Cohen P.;
RT   "Exploitation of KESTREL to identify NDRG family members as
RT   physiological substrates for SGK1 and GSK3.";
RL   Biochem. J. 384:477-488(2004).
RN   [5]
RP   DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   PubMed=15082788; DOI=10.1128/MCB.24.9.3949-3956.2004;
RA   Okuda T., Higashi Y., Kokame K., Tanaka C., Kondoh H., Miyata T.;
RT   "Ndrg1-deficient mice exhibit a progressive demyelinating disorder of
RT   peripheral nerves.";
RL   Mol. Cell. Biol. 24:3949-3956(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-336, AND
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=21636852; DOI=10.1074/jbc.M111.256446;
RA   Yamamoto H., Kokame K., Okuda T., Nakajo Y., Yanamoto H., Miyata T.;
RT   "NDRG4 protein-deficient mice exhibit spatial learning deficits and
RT   vulnerabilities to cerebral ischemia.";
RL   J. Biol. Chem. 286:26158-26165(2011).
RN   [9]
RP   DISRUPTION PHENOTYPE, CHARACTERISTICS OF A MOUSE MODEL OF CMT4D,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21303696; DOI=10.1016/j.nbd.2011.01.030;
RA   King R.H., Chandler D., Lopaticki S., Huang D., Blake J., Muddle J.R.,
RA   Kilpatrick T., Nourallah M., Miyata T., Okuda T., Carter K.W.,
RA   Hunter M., Angelicheva D., Morahan G., Kalaydjieva L.;
RT   "Ndrg1 in development and maintenance of the myelin sheath.";
RL   Neurobiol. Dis. 42:368-380(2011).
CC   -!- FUNCTION: Stress-responsive protein involved in hormone responses,
CC       cell growth, and differentiation. Acts as a tumor suppressor in
CC       many cell types. Necessary but not sufficient for p53/TP53-
CC       mediated caspase activation and apoptosis. Required for vesicular
CC       recycling of CDH1 and TF. May also function in lipid trafficking.
CC       Protects cells from spindle disruption damage. Functions in
CC       p53/TP53-dependent mitotic spindle checkpoint. Regulates
CC       microtubule dynamics and maintains euploidy (By similarity). Has a
CC       role in cell trafficking notably of the Schwann cell and is
CC       necessary for the maintenance and development of the peripheral
CC       nerve myelin sheath. {ECO:0000250, ECO:0000269|PubMed:15082788,
CC       ECO:0000269|PubMed:21303696}.
CC   -!- SUBUNIT: Interacts with RAB4A (membrane-bound form); the
CC       interaction involves NDRG1 in vesicular recycling of CDH1.
CC       Interacts with APOA1, APOA2, PRA1 and RTN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome. Nucleus. Cell membrane
CC       {ECO:0000250}. Note=Mainly cytoplasmic but differentially
CC       localized to other regions. Associates with the plasma membrane in
CC       intestinal epithelia and lactating mammary gland. Translocated to
CC       the nucleus in a p53/TP53-dependent manner. In prostate epithelium
CC       and placental chorion, located in both the cytoplasm and in the
CC       nucleus. No nuclear localization in colon epithelium cells. In
CC       intestinal mucosa, prostate and renal cortex, located
CC       predominantly adjacent to adherens junctions. Cytoplasmic with
CC       granular staining in proximal tubular cells of the kidney and
CC       salivary gland ducts. Recruits to the membrane of
CC       recycling/sorting and late endosomes via binding to
CC       phosphatidylinositol 4-phosphate. Associates with microtubules.
CC       Colocalizes with TUBG1 in the centrosome. Cytoplasmic location
CC       increased with hypoxia. Phosphorylated form found associated with
CC       centromeres during S-phase of mitosis and with the plasma membrane
CC       (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
CC       kidney followed by brain, pancreas, small intestine, colon and
CC       spleen (at protein level). Also detected in heart and preputial
CC       gland, and in much smaller quantities in other tissues. Not
CC       detected in duodenum and prostate. Highly expressed in Schwann
CC       cells. {ECO:0000269|PubMed:15082788, ECO:0000269|PubMed:15461589,
CC       ECO:0000269|PubMed:21636852, ECO:0000269|PubMed:9144177}.
CC   -!- DEVELOPMENTAL STAGE: In early stages of embryo development,
CC       expression low when MYCN expression is high. Later, when MYCN
CC       levels diminish, levels increase. {ECO:0000269|PubMed:10381566}.
CC   -!- INDUCTION: Repressed by testosterone and also to a lesser extent
CC       by dihydrotestosterone. Down-regulated by MYCN.
CC       {ECO:0000269|PubMed:10381566, ECO:0000269|PubMed:9144177}.
CC   -!- PTM: Under stress conditions, phosphorylated in the C-terminal on
CC       many serine and threonine residues. Phosphorylated in vitro by
CC       PKA. Phosphorylation enhanced by increased intracellular cAMP
CC       levels. Homocysteine induces dephosphorylation. Phosphorylation by
CC       SGK1 is cell cycle dependent (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice exhibit defects in peripheral
CC       nerve development. Initial hind limb weakness developed around age
CC       12 weeks, and significant functional impairment (dragging of hind
CC       legs) and muscle atrophy became apparent at age 1 year. After
CC       about 5 weeks extensive demyelination of nerve fibers is observed.
CC       In later life, large inclusions were seen in the adaxonal Schwann
CC       cell cytoplasm. There is no evidence of apoptotic response.
CC       {ECO:0000269|PubMed:15082788, ECO:0000269|PubMed:21303696}.
CC   -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
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DR   EMBL; U60593; AAB03484.1; -; mRNA.
DR   EMBL; U52073; AAB58249.1; -; mRNA.
DR   EMBL; BC015282; AAH15282.1; -; mRNA.
DR   EMBL; BC071235; AAH71235.1; -; mRNA.
DR   CCDS; CCDS37092.1; -.
DR   RefSeq; NP_032707.2; NM_008681.2.
DR   RefSeq; XP_006520631.1; XM_006520568.1.
DR   UniGene; Mm.30837; -.
DR   ProteinModelPortal; Q62433; -.
DR   SMR; Q62433; 35-311.
DR   IntAct; Q62433; 6.
DR   MINT; MINT-1849784; -.
DR   MEROPS; S33.987; -.
DR   PhosphoSite; Q62433; -.
DR   MaxQB; Q62433; -.
DR   PaxDb; Q62433; -.
DR   PRIDE; Q62433; -.
DR   DNASU; 17988; -.
DR   Ensembl; ENSMUST00000005256; ENSMUSP00000005256; ENSMUSG00000005125.
DR   GeneID; 17988; -.
DR   KEGG; mmu:17988; -.
DR   UCSC; uc007wax.1; mouse.
DR   CTD; 10397; -.
DR   MGI; MGI:1341799; Ndrg1.
DR   eggNOG; NOG310435; -.
DR   GeneTree; ENSGT00390000001874; -.
DR   HOGENOM; HOG000230891; -.
DR   HOVERGEN; HBG052591; -.
DR   InParanoid; Q62433; -.
DR   KO; K18266; -.
DR   OMA; TLHGSIH; -.
DR   OrthoDB; EOG7KH9JS; -.
DR   PhylomeDB; Q62433; -.
DR   TreeFam; TF313168; -.
DR   ChiTaRS; NDRG1; mouse.
DR   NextBio; 292963; -.
DR   PRO; PR:Q62433; -.
DR   Bgee; Q62433; -.
DR   CleanEx; MM_NDRG1; -.
DR   ExpressionAtlas; Q62433; baseline and differential.
DR   Genevestigator; Q62433; -.
DR   GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0045576; P:mast cell activation; IDA:MGI.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:UniProtKB.
DR   GO; GO:0090232; P:positive regulation of spindle checkpoint; IEA:Ensembl.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR004142; NDRG.
DR   PANTHER; PTHR11034; PTHR11034; 1.
DR   Pfam; PF03096; Ndr; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Membrane; Microtubule; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    394       Protein NDRG1.
FT                                /FTId=PRO_0000159574.
FT   REPEAT      339    348       1.
FT   REPEAT      349    358       2.
FT   REPEAT      359    368       3.
FT   REGION      339    368       3 X 10 AA tandem repeats of G-[PST]-R-S-
FT                                R-S-H-T-S-E.
FT   MOD_RES       2      2       N-acetylserine. {ECO:0000250}.
FT   MOD_RES     326    326       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     328    328       Phosphothreonine; by SGK1.
FT   MOD_RES     330    330       Phosphoserine; by SGK1.
FT                                {ECO:0000269|PubMed:17242355}.
FT   MOD_RES     332    332       Phosphoserine; by SGK1. {ECO:0000250}.
FT   MOD_RES     333    333       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     336    336       Phosphoserine.
FT                                {ECO:0000269|PubMed:17242355}.
FT   MOD_RES     346    346       Phosphothreonine; by SGK1.
FT                                {ECO:0000269|PubMed:15461589}.
FT   MOD_RES     356    356       Phosphothreonine; by SGK1. {ECO:0000250}.
FT   MOD_RES     364    364       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     366    366       Phosphothreonine; by SGK1. {ECO:0000250}.
FT   MOD_RES     375    375       Phosphothreonine. {ECO:0000250}.
FT   CONFLICT     33     35       QEQ -> LEE (in Ref. 2; AAB58249).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       F -> P (in Ref. 2; AAB58249).
FT                                {ECO:0000305}.
FT   CONFLICT    103    109       APSFPVG -> PLPSQW (in Ref. 2; AAB58249).
FT                                {ECO:0000305}.
FT   CONFLICT    141    148       AGAYILTR -> PWXLHPDP (in Ref. 2;
FT                                AAB58249). {ECO:0000305}.
FT   CONFLICT    191    208       VVSHLFGKEEIHNNVEVV -> CVPPLRXGGDTQQRGGM
FT                                (in Ref. 2; AAB58249). {ECO:0000305}.
FT   CONFLICT    241    241       R -> A (in Ref. 2; AAB58249).
FT                                {ECO:0000305}.
FT   CONFLICT    298    350       PAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLE
FT                                GTRSRSHTSEGP -> RPSLLRPSSTLCRHGIHAFCQHDSP
FT                                DRVPHPVWLQCHILEGT (in Ref. 2; AAB58249).
FT                                {ECO:0000305}.
SQ   SEQUENCE   394 AA;  43009 MW;  905CA71ECF4C87C2 CRC64;
     MSRELHDVDL AEVKPLVEKG ESITGLLQEF DVQEQDIETL HGSLHVTLCG TPKGNRPVIL
     TYHDIGMNHK TCYNPLFNSE DMQEITQHFA VCHVDAPGQQ DGAPSFPVGY MYPSMDQLAE
     MLPGVLHQFG LKSVIGMGTG AGAYILTRFA LNNPEMVEGL VLMNVNPCAE GWMDWAASKI
     SGWTQALPDM VVSHLFGKEE IHNNVEVVHT YRQHILNDMN PSNLHLFISA YNSRRDLEIE
     RPMPGTHTVT LQCPALLVVG DNSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK
     LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLEGT RSRSHTSEGP RSRSHTSEGS
     RSRSHTSEDA RLNITPNSGA TGNNAGPKSM EVSC
//
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