ID NDRG1_RAT Reviewed; 394 AA.
AC Q6JE36;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Protein NDRG1;
DE AltName: Full=N-myc downstream-regulated gene 1 protein;
DE Short=Protein Ndr1;
GN Name=Ndrg1; Synonyms=Ndr1;
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].
RA Wang X., Jing N.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 133-148; 213-234 AND 328-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-326; THR-328; SER-330;
RP SER-333; SER-336; THR-346; SER-352; SER-362; THR-366 AND THR-375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Stress-responsive protein involved in hormone responses, cell
CC growth, and differentiation. Acts as a tumor suppressor in many cell
CC types. Necessary but not sufficient for p53/TP53-mediated caspase
CC activation and apoptosis. Has a role in cell trafficking notably of the
CC Schwann cell and is necessary for the maintenance and development of
CC the peripheral nerve myelin sheath. Required for vesicular recycling of
CC CDH1 and TF. May also function in lipid trafficking. Protects cells
CC from spindle disruption damage. Functions in p53/TP53-dependent mitotic
CC spindle checkpoint. Regulates microtubule dynamics and maintains
CC euploidy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAB4A (membrane-bound form); the interaction
CC involves NDRG1 in vesicular recycling of CDH1. Interacts with APOA1,
CC APOA2, PRA1 and RTN1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Mainly
CC cytoplasmic but differentially localized to other regions. Associates
CC with the plasma membrane in intestinal epithelia and lactating mammary
CC gland. Translocated to the nucleus in a p53/TP53-dependent manner. In
CC prostate epithelium and placental chorion, located in both the
CC cytoplasm and in the nucleus. No nuclear localization in colon
CC epithelium cells. In intestinal mucosa, prostate and renal cortex,
CC located predominantly adjacent to adherens junctions. Cytoplasmic with
CC granular staining in proximal tubular cells of the kidney and salivary
CC gland ducts. Recruits to the membrane of recycling/sorting and late
CC endosomes via binding to phosphatidylinositol 4-phosphate. Associates
CC with microtubules. Colocalizes with TUBG1 in the centrosome.
CC Cytoplasmic location increased with hypoxia. Phosphorylated form found
CC associated with centromeres during S-phase of mitosis and with the
CC plasma membrane (By similarity). {ECO:0000250}.
CC -!- PTM: Under stress conditions, phosphorylated in the C-terminal on many
CC serine and threonine residues. Phosphorylated in vitro by PKA.
CC Phosphorylation enhanced by increased intracellular cAMP levels.
CC Homocysteine induces dephosphorylation. Phosphorylation by SGK1 is cell
CC cycle dependent (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
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DR EMBL; AY500369; AAS78638.1; -; mRNA.
DR EMBL; BC081898; AAH81898.1; -; mRNA.
DR RefSeq; NP_001011991.1; NM_001011991.1.
DR AlphaFoldDB; Q6JE36; -.
DR SMR; Q6JE36; -.
DR BioGRID; 256379; 1.
DR STRING; 10116.ENSRNOP00000010811; -.
DR ESTHER; ratno-q6je36; Ndr_family.
DR MEROPS; S33.988; -.
DR iPTMnet; Q6JE36; -.
DR PhosphoSitePlus; Q6JE36; -.
DR PaxDb; 10116-ENSRNOP00000010811; -.
DR Ensembl; ENSRNOT00000010811.8; ENSRNOP00000010811.5; ENSRNOG00000007393.8.
DR GeneID; 299923; -.
DR KEGG; rno:299923; -.
DR UCSC; RGD:1307303; rat.
DR AGR; RGD:1307303; -.
DR CTD; 10397; -.
DR RGD; 1307303; Ndrg1.
DR eggNOG; KOG2931; Eukaryota.
DR GeneTree; ENSGT00950000182872; -.
DR HOGENOM; CLU_035361_1_0_1; -.
DR InParanoid; Q6JE36; -.
DR OMA; DMNQNNL; -.
DR OrthoDB; 5352016at2759; -.
DR PhylomeDB; Q6JE36; -.
DR TreeFam; TF313168; -.
DR PRO; PR:Q6JE36; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007393; Expressed in adult mammalian kidney and 19 other cell types or tissues.
DR ExpressionAtlas; Q6JE36; baseline and differential.
DR Genevisible; Q6JE36; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:0045576; P:mast cell activation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004142; NDRG.
DR PANTHER; PTHR11034; N-MYC DOWNSTREAM REGULATED; 1.
DR PANTHER; PTHR11034:SF18; PROTEIN NDRG1; 1.
DR Pfam; PF03096; Ndr; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT CHAIN 2..394
FT /note="Protein NDRG1"
FT /id="PRO_0000270758"
FT REPEAT 339..348
FT /note="1"
FT REPEAT 349..358
FT /note="2"
FT REPEAT 359..368
FT /note="3"
FT REGION 325..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..368
FT /note="3 X 10 AA tandem repeats of G-[PST]-R-S-R-S-H-T-S-E"
FT COMPBIAS 325..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 356
FT /note="Phosphothreonine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 394 AA; 42955 MW; 42B2B95FBDBC9A16 CRC64;
MSRELHDVDL AEVKPLVEKG ESITGLLQEF DVQEQDIETL HGSLHVTLCG TPKGNRPVIL
TYHDIGMNHK TCYNPLFNSE DMQEITQHFA VCHVDAPGQQ DGAPSFPVGY MYPSMDQLAE
MLPGVLHKFG LKSVIGMGTG AGAYILTRFA LNNPEMVEGL VLMNVNPCAE GWMDWAASKI
SGWTQALPDM VVSHLFGKEE IHSNVEVVHT YRQHILNDMN PSNLHLFISA YNSRRDLEIE
RPMPGTHTVT LQCPALLVVG DNSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK
LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLEGT RSRSHTSEGP RSRSHTSEGS
RSRSHTSEDA RLNITPSSGA TGNNAGPKSM EVSC
//
