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Database: UniProt
Entry: A0A2Y9LJU7_ENHLU
LinkDB: A0A2Y9LJU7_ENHLU
Original site: A0A2Y9LJU7_ENHLU 
ID   A0A2Y9LJU7_ENHLU        Unreviewed;       461 AA.
AC   A0A2Y9LJU7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein isoform X2 {ECO:0000313|RefSeq:XP_022381985.1};
GN   Name=LOC111162075 {ECO:0000313|RefSeq:XP_022381985.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022381985.1};
RN   [1] {ECO:0000313|RefSeq:XP_022381985.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022381985.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022381985.1; XM_022526277.1.
DR   AlphaFoldDB; A0A2Y9LJU7; -.
DR   Proteomes; UP000248482; 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:SF21; BCL-2_ADENOVIRUS E1B 19 KDA-INTERACTING PROTEIN 2-LIKE PROTEIN; 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:UP000248482}.
FT   DOMAIN          295..456
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          68..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  51231 MW;  04756D4D881E139E CRC64;
     MRKQIAFLNS PKTRHFRKCP LFPKTRPHIG RVFFWANLLL GKGKKKGGGK TCLKVRLLPF
     HTSLLLGGKS NNSETEKKDT EVLGSRDKEL PDSCKVAEGG RKTLKMGTTQ EAGEKTLDLG
     AGENAEAARP AASLRLGELE LKEEWQDEEF PRFLPEEADP SEGPDDPERG SQAGTPSTLA
     LCGPRPMRKR LSAPELRLNL TKGAGGDGTS PTNSVPSSPD GSSDLEVDEL ETPSDSEQLD
     SGHEFEWEDD LPRAEGLGAS EAAERLGQGC VWDMAGEDGR HWRVFRTGQR EQRVDMTVIE
     LYKKVLSHGG YHGDGLNAII VFSSCYLPSS SIPNYTYVME HLFRYMVGTL ELLVAENYLL
     VHLSGGTSRA QVPPLGWMRQ CYRALDRRLR KNLRALVVVH ATWYVKAFLA LLRPFISSKF
     TRKIRFLNSL GELAQLISLD QVHIPEAVRQ LDQELHGSRG T
//
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