NDRG2_PANTR
ID NDRG2_PANTR Reviewed; 357 AA.
AC A5A6K6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Protein NDRG2;
DE AltName: Full=N-myc downstream-regulated gene 2 protein;
GN Name=NDRG2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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; AB222134; BAF62379.1; -; mRNA.
DR RefSeq; NP_001182082.1; NM_001195153.2.
DR AlphaFoldDB; A5A6K6; -.
DR SMR; A5A6K6; -.
DR STRING; 9598.ENSPTRP00000010368; -.
DR ESTHER; pantr-ndrg2; Ndr_family.
DR MEROPS; S33.989; -.
DR PaxDb; A5A6K6; -.
DR GeneID; 100499579; -.
DR KEGG; ptr:100499579; -.
DR CTD; 57447; -.
DR eggNOG; KOG2931; Eukaryota.
DR InParanoid; A5A6K6; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
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:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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_0000441169"
FT REGION 1..28
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; 39361 MW; CC6931A80D18F30C CRC64;
MAELQEVQIT EEKPLLPGQT PEAAKTHSVE TPYGSVTFTV YGTPKPKRPA ILTYHDVGLN
YKSCFQPLFQ FEDMQEIIQN FVRVHVDAPG MEEGAPVFPL GYQYPSLDQL ADMIPCVLQY
LNFSTIIGVG VGAGAYILAR YALNHPDTVE GLVLINIDPN AKRWMDWAAH KLTGLTSSIP
EMILGHLFSQ EELSGNSELI QKYRNIITHA PNLDNIELYW NSYNNRRDLN FERGGDITLK
CPVMLVVGDQ APHEDAVVEC NSKLDPTQTS FLKMADSGGQ PQLTQPGKLT EAFKYFLQGM
GYMASSCMTR LSRSRTASLT SAASVDGNRS RSRTLSQSSE SGTLSSGPPG HTMEVSC
