NR13_COTJA
ID NR13_COTJA Reviewed; 177 AA.
AC Q90343;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Anti-apoptotic protein NR13;
DE AltName: Full=Apoptosis regulator Nr-13;
GN Name=NR13;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Fibroblast, and Neuroretina;
RX PubMed=7729415; DOI=10.1002/j.1460-2075.1995.tb07123.x;
RA Gillet G., Guerin M., Trembleau A., Brun G.;
RT "A Bcl-2-related gene is activated in avian cells transformed by the Rous
RT sarcoma virus.";
RL EMBO J. 14:1372-1381(1995).
CC -!- FUNCTION: Shows anti-apoptotic properties. Counteract the pro-apoptotic
CC activity of BAX. {ECO:0000269|PubMed:7729415}.
CC -!- SUBUNIT: Interacts with BAX. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Mainly expressed in neural and muscular tissues.
CC {ECO:0000269|PubMed:7729415}.
CC -!- DEVELOPMENTAL STAGE: Expression is dramatically down-regulated after
CC embryonic day 7 in the optic tectum, and correlates with the onset of
CC apoptosis in this area. {ECO:0000269|PubMed:7729415}.
CC -!- INDUCTION: By Rous sarcoma virus. {ECO:0000269|PubMed:7729415}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; X84418; CAA59136.1; -; Genomic_DNA.
DR AlphaFoldDB; Q90343; -.
DR SMR; Q90343; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..177
FT /note="Anti-apoptotic protein NR13"
FT /id="PRO_0000143071"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 75..94
FT /note="BH1"
FT MOTIF 126..141
FT /note="BH2"
SQ SEQUENCE 177 AA; 18826 MW; AD5CE79D3353CC1F CRC64;
MPGSLKEETA LLLEDYFQHR AGGAALPPSA TAAELRRAAA ELERRERPFF RSCAPLARAE
PREAAALLRK VAAQLETDGG LNWGRLLALV VFAGTLAAAL AESACEEGPS RLAAALTAYL
AEEQGEWMEE HGGWDGFCRF FGRHGSQPAD QNSTLSNAIM AAAGFGIAGL AFLLVVR