PRUN2_RAT
ID PRUN2_RAT Reviewed; 322 AA.
AC Q5BJR4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein prune homolog 2;
DE AltName: Full=BNIP2 motif-containing molecule at the C-terminal region 1;
GN Name=Prune2; Synonyms=Bmcc1;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
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: May play an important role in regulating differentiation,
CC survival and aggressiveness of the tumor cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; BC091368; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q5BJR4; -.
DR STRING; 10116.ENSRNOP00000051678; -.
DR jPOST; Q5BJR4; -.
DR PaxDb; Q5BJR4; -.
DR PRIDE; Q5BJR4; -.
DR Ensembl; ENSRNOT00000054794; ENSRNOP00000051678; ENSRNOG00000015088.
DR UCSC; RGD:1311350; rat.
DR RGD; 1311350; Prune2.
DR eggNOG; KOG4129; Eukaryota.
DR GeneTree; ENSGT00940000154422; -.
DR HOGENOM; CLU_039135_3_0_1; -.
DR InParanoid; Q5BJR4; -.
DR OMA; NREDYHE; -.
DR PRO; PR:Q5BJR4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015088; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q5BJR4; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR Pfam; PF12496; BNIP2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Reference proteome.
FT CHAIN 1..322
FT /note="Protein prune homolog 2"
FT /id="PRO_0000274883"
FT DOMAIN 130..291
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 36980 MW; 65428A8110300C30 CRC64;
MDIHFEEGVL SPSATDMRPE PPNSLDLNGS HPRRIKLTAP NINLSLDQSE GSILSDDNLD
SPDEIDINVD ELDTPDEADS FEYPGHEDPM ANRSSGQESE SIPEYTAEEE REDNRLWRTV
VIGEQEQRID MKVIEPYRRV ISHGGYYGDG LNAIIVFAAC FLPDSSRADY HYVMENLFLY
VISTLELMVA EDYMIVYLNG ATPRRKMPGL GWMKKCYQMI DRRLRKNLKS FIIVHPSWFI
RTILAVTRPF ISSKFSSKIK YVSSLSELSG LIPMDCIHIP ESIIKYDEEK SFKRSVRTSC
LYNDPEMTSM EKDIDMKLKE KP