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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
 
 
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