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Database: UniProt
Entry: A0A3Q2VWJ0_HAPBU
LinkDB: A0A3Q2VWJ0_HAPBU
Original site: A0A3Q2VWJ0_HAPBU 
ID   A0A3Q2VWJ0_HAPBU        Unreviewed;       455 AA.
AC   A0A3Q2VWJ0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=BCL2 interacting protein 2 {ECO:0000313|Ensembl:ENSHBUP00000012893.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000012893.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000012893.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_005928791.1; XM_005928729.2.
DR   AlphaFoldDB; A0A3Q2VWJ0; -.
DR   Ensembl; ENSHBUT00000020480.1; ENSHBUP00000012893.1; ENSHBUG00000014659.1.
DR   GeneID; 102310142; -.
DR   CTD; 663; -.
DR   GeneTree; ENSGT00940000158531; -.
DR   OrthoDB; 5402707at2759; -.
DR   Proteomes; UP000264840; Unplaced.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   PANTHER; PTHR12112:SF12; BCL2_ADENOVIRUS E1B 19 KDA PROTEIN-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   Pfam; PF12496; BNIP2; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          286..443
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          14..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..168
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  51022 MW;  49ABB04886AC931E CRC64;
     MASDVIESEA VLKGVSNMNL NNSSPDTVTP RRTLEDLGNR QTSSPSSSGV SGEGDDEETD
     ELQNSTASAA EKGEEEFQDS LTKTSGTPQE RKTPDNVQKQ RGKSSTPVSV PQPRSPAGAT
     GSLERQESVA TTEARLRMEG VELKEEWQDE DFPRPLPEEE ELEDELFAEA SEAGNSGYAV
     NHGKKTKKKL AAPDISLTLD RSEGSLLSDE LDESTELDLS DMDTPSDNSN EFEWEDDLPK
     PKPTELLQKG VESVHEYSAS EEREDSRRWK MLRIGDQEHR VDMKAIEPYK RVISHGGYYG
     DGLNAVIVFA VCFMPESNQP NYRYIMENLF KYVIGTLELL VAENYMIVYL NGATSRKKMP
     TVGWLRKCYQ QIDRRLRKNL KSLIIVHPSW FIRTLLALTK PFISSKFSQK IKYVYSLSDL
     ADLVPMEYVS IPDCIKQIDQ DMHGKTESAA ATVPE
//
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