ID   BOK_CHICK               Reviewed;         213 AA.
AC   Q9I8I2; Q9DGJ5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Bcl-2-related ovarian killer protein {ECO:0000303|PubMed:11034351, ECO:0000303|Ref.2};
GN   Name=BOK {ECO:0000303|PubMed:11034351, ECO:0000303|Ref.2};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11034351; DOI=10.1016/s0014-5793(00)01921-9;
RA   Zhang H., Holzgreve W., De Geyter C.;
RT   "Evolutionarily conserved Bok proteins in the Bcl-2 family.";
RL   FEBS Lett. 480:311-313(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mills E.M., Johnson A.L., Bridgham J.T.;
RT   "Characterization and expression of Bok in the hen ovary.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in apoptosis. {ECO:0000250|UniProtKB:O35425}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9UMX3}; Single-
CC       pass membrane protein {ECO:0000250|UniProtKB:O35425}.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR   EMBL; AF275944; AAF81282.1; -; mRNA.
DR   EMBL; AF290888; AAG01182.1; -; mRNA.
DR   RefSeq; NP_990037.1; NM_204706.1.
DR   PDB; 5WDD; X-ray; 1.80 A; A/B=19-181.
DR   PDBsum; 5WDD; -.
DR   AlphaFoldDB; Q9I8I2; -.
DR   SMR; Q9I8I2; -.
DR   STRING; 9031.ENSGALP00000009257; -.
DR   PaxDb; Q9I8I2; -.
DR   GeneID; 395445; -.
DR   KEGG; gga:395445; -.
DR   CTD; 666; -.
DR   VEuPathDB; HostDB:geneid_395445; -.
DR   eggNOG; KOG4728; Eukaryota.
DR   InParanoid; Q9I8I2; -.
DR   OrthoDB; 1278637at2759; -.
DR   PhylomeDB; Q9I8I2; -.
DR   PRO; PR:Q9I8I2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd06845; Bcl-2_like; 1.
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; IPR026309; BOK.
DR   PANTHER; PTHR11256; PTHR11256; 1.
DR   PANTHER; PTHR11256:SF48; PTHR11256:SF48; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..213
FT                   /note="Bcl-2-related ovarian killer protein"
FT                   /id="PRO_0000143089"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           32..44
FT                   /note="BH4"
FT   MOTIF           67..83
FT                   /note="BH3"
FT   MOTIF           113..132
FT                   /note="BH1"
FT   MOTIF           165..179
FT                   /note="BH2"
FT   HELIX           24..46
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           63..81
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           83..86
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           100..115
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           121..140
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           146..161
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           163..168
FT                   /evidence="ECO:0007829|PDB:5WDD"
FT   HELIX           172..178
FT                   /evidence="ECO:0007829|PDB:5WDD"
SQ   SEQUENCE   213 AA;  23620 MW;  B3AF7049F25442E3 CRC64;
     MEVLRRSSVF AAEVMEVFDR SPTDKELVSQ AKALCRDYIN SRLIRAGVSW SKPEHNTPVP
     GGKLAEVSAI LLRLGDELEY IRPNVYRNIA RQLNISLHSE TVVTDAFLAV AAQIFTAGIT
     WGKVVSLYAV AAGLAVDCVR HAQPAMVHTI VDCLGEFVRK TLVTWLKRRG GWADITKCVV
     STDPSLRSHW LVAAVCSFGH FLKAIFFVLL PER