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   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.
DR   Genevisible; Q6JE36; RN.
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
//