NDRG1_BOVIN
ID NDRG1_BOVIN Reviewed; 384 AA.
AC Q3SYX0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Protein NDRG1;
DE AltName: Full=N-myc downstream-regulated gene 1 protein;
GN Name=NDRG1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC103346; AAI03347.1; -; mRNA.
DR RefSeq; NP_001030181.1; NM_001035009.2.
DR AlphaFoldDB; Q3SYX0; -.
DR SMR; Q3SYX0; -.
DR STRING; 9913.ENSBTAP00000000950; -.
DR ESTHER; bovin-ndr1; Ndr_family.
DR MEROPS; S33.988; -.
DR iPTMnet; Q3SYX0; -.
DR PaxDb; Q3SYX0; -.
DR PeptideAtlas; Q3SYX0; -.
DR PRIDE; Q3SYX0; -.
DR GeneID; 504499; -.
DR KEGG; bta:504499; -.
DR CTD; 10397; -.
DR eggNOG; KOG2931; Eukaryota.
DR InParanoid; Q3SYX0; -.
DR OrthoDB; 854690at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045576; P:mast cell activation; IEA:InterPro.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004142; NDRG.
DR InterPro; IPR030693; NDRG1.
DR PANTHER; PTHR11034; PTHR11034; 1.
DR PANTHER; PTHR11034:SF18; PTHR11034:SF18; 1.
DR Pfam; PF03096; Ndr; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT CHAIN 2..384
FT /note="Protein NDRG1"
FT /id="PRO_0000270756"
FT REPEAT 339..348
FT /note="1"
FT REPEAT 349..358
FT /note="2"
FT REGION 325..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="2 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..358
FT /note="Basic and acidic 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:0000250|UniProtKB:Q92597"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 328
FT /note="Phosphothreonine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 330
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
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:0000250|UniProtKB:Q92597"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62433"
FT MOD_RES 346
FT /note="Phosphothreonine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6JE36"
FT MOD_RES 356
FT /note="Phosphothreonine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:Q92597"
SQ SEQUENCE 384 AA; 41627 MW; 66A4932158F72331 CRC64;
MSRELQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSIHVTLCG TPKGNRPVIL
TYHDIGMNHK TCYNPLFNSE DMQEITQHFA VCHVDAPGQQ DGAASFPTGY MYPSMDQLAE
MLPGVLQQFG LKSIIGMGTG AGAYILTRFA LNNPEMVEGL VLINVNPCAE GWMDWAASKI
SGWTQALPDM VVSHLFGKEE MQNNVEVVHA YRHHVMNDMN PGNLQLFINA YNGRRDLEIE
RPMPGAHTVT LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK
LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLEGA RSRSHTSEGT RSRSHTSEGT
RLDIIPNSGG PGSSAGPNST EVSC
