NDRG2_BOVIN
ID NDRG2_BOVIN Reviewed; 357 AA.
AC Q3ZBA8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein NDRG2;
DE AltName: Full=N-myc downstream-regulated gene 2 protein;
GN Name=NDRG2;
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=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. May be
CC involved in dendritic cell and neuron differentiation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}.
CC Note=In neurons, seems to concentrate at axonal growth cone.
CC Perinuclear in neurons (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
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DR EMBL; BC103467; AAI03468.1; -; mRNA.
DR RefSeq; NP_001030381.1; NM_001035304.1.
DR AlphaFoldDB; Q3ZBA8; -.
DR SMR; Q3ZBA8; -.
DR STRING; 9913.ENSBTAP00000001121; -.
DR ESTHER; bovin-ndrg2; Ndr_family.
DR PeptideAtlas; Q3ZBA8; -.
DR Ensembl; ENSBTAT00000080282; ENSBTAP00000073589; ENSBTAG00000000843.
DR GeneID; 515063; -.
DR KEGG; bta:515063; -.
DR CTD; 57447; -.
DR VEuPathDB; HostDB:ENSBTAG00000000843; -.
DR VGNC; VGNC:50007; NDRG2.
DR eggNOG; KOG2931; Eukaryota.
DR GeneTree; ENSGT00950000182872; -.
DR InParanoid; Q3ZBA8; -.
DR OMA; KTCFQPL; -.
DR OrthoDB; 854690at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000000843; Expressed in temporal cortex and 103 other tissues.
DR ExpressionAtlas; Q3ZBA8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0090361; P:regulation of platelet-derived growth factor production; IEA:Ensembl.
DR GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Cell projection; Cytoplasm; Developmental protein;
KW Differentiation; Neurogenesis; Phosphoprotein; Reference proteome;
KW Tumor suppressor; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT CHAIN 2..357
FT /note="Protein NDRG2"
FT /id="PRO_0000441165"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..357
FT /note="Disordered"
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:0000250|UniProtKB:Q9UN36"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
SQ SEQUENCE 357 AA; 39208 MW; 9F255C18E283F0C4 CRC64;
MAELREVQIT EEKPLLPGQT PEVAKTHSVE TPYGSVTFTV YGTPKPKRPA ILTYHDVGLN
YKSCFQPLFQ FADMQEIIQN FVRVHVDAPG MEEGAPVFPL GYQYPSLDQL ADMIPCILQY
LNFSTIIGIG VGAGAYVLSR YALTHPDTVE GLVLINIDPN AKGWMDWAAH KLTGLTSSIS
EMILGHLFSQ EELSGNSELI QKYRNIIAHA PNLDNIELYW NSYNNRRDLN FVRGGDTTLK
CPVMLVVGDQ APHEDAVVEC NSKLDPTQTS FLKMADSGGQ PQLTQPGKLT EAFKYFLQGM
GYMASSCMTR LSRSRTASLT SAASIDGNRS RSRTLSQSSE SGTLSSGPPG HTMEVSC
