ID A0A2U9BUM3_SCOMX Unreviewed; 1772 AA.
AC A0A2U9BUM3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN ORFNames=SMAX5B_016524 {ECO:0000313|EMBL:AWP07196.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP07196.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP07196.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP026251; AWP07196.1; -; Genomic_DNA.
DR Proteomes; UP000246464; Chromosome 9.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; BNIP - RELATED; 1.
DR PANTHER; PTHR12112:SF49; PRUNE HOMOLOG 2 WITH BCH DOMAIN; 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:UP000246464};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1772
FT /note="CRAL-TRIO domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015933137"
FT DOMAIN 1597..1757
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 315..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1772 AA; 194118 MW; E5C97AE499267DA8 CRC64;
MLHLIFLSLK DASGGLCLPV LCGRQCNAVL PEETVRYLKR LNISESLLLW REDVDLMTLH
HTGKLSLTLL RDGLLDSSEY HALESSILRV VHHDGQQDTG DDAALSAVTT VAREIRQEAA
EHIRATLGKS LGEALRLQNE AFWIKHGRQS TQLEDLRRSL EQLSDATADA ELQDMEQLLT
AELKEFSDGE MTIALSSVTT VKEHWIVNVD GLNAFSQHHG LDGLVVLLSI SDTVHHPGQQ
VAVYSNNTDI LNQICCELEE SSSWSLFGQL EARENLQVYH IPINTPSSIG TLLVEEIQGL
LKDFVDRRSS VLACHPSSRS SSTEGVAGSV EFSQGSSGIN DMDGSDIERV EGGSADVAAR
ARGMADGEED TRGVEVSAGG ELVSPDSGMT TLRSSRSSKE SSVFLSDDSP VGEVTAGGGP
AAGPGGIFLR NPPPLGLSSL SPPVPPERKK NRSCRNKSDN FDLFSFDPLH SSDPSLPAGG
ELTNSEVRGD GTETRSGSSN LSELEELSFM DFSAGSRNSS VDHHGQIHGN EMTDTVVPPT
PVNSLVGSRP PSRCGIRFFP EDVVERINCL QHKDSVSSSL SETWDELCFD TQGALSSSDN
NASNRTKDYE SPQNIIEDIR GKESLSDVTE IESREEILKP ENSHQRPKSL QPQLSVVTGQ
TESYENWNPD SVLKDEWNPV TLADLQLTPP EEEGTGKCKA GDIGSKGKTT SLSKKKAILN
TLTPDTSKEE DKGVQGKKED QKMELLDFWT YSAQKGFLKS DSGTTESYPE SLDMWNMTIR
DDSLSPLTTP DNLSENSGSF CGMNRNLLGG TSVESPPGFC DGGMEMWNTT IQEDSSSTIT
SPEGPDNGKD LSHMGSPDAH SPETHASIDM HDLSVPGMVT STSEYDNVGA GVWSLSSSPE
TFASPVVDVI QPQGQSSPFF VVTNPIHIDE KHDQSQRTNP LGKTECRSAI SDTEQSVTQM
FLFEGTCEVG HITSSIESEY DNKNKEGSAE ADWIEQSSDY SPFVMVDSSM THSESASLSH
ALPITVAQNE DGTAAESQRW ANIANNGNVE GKITETMGLG SSSGVKRDTL KFSPDSLQPG
SGDELRSNSD GDSSSGLEME YIVVSGTVKE AEREWDDRPK QGDKQTKRTR KPMETFSTLY
YAATVLGAHR EHQENTEQSR QNQNQAVLST HYLVNLDNST EHDMVPEKVS PSQSKNTLEA
TGCNQPQVFE GNYDDKSSIV ARSVSPSLRF PSDIFLKTRE EVYVHSQISM EDSDEGGQSP
SAPPLCPTSL GDFQDWGGQL VRHDTPRDTS ETQSPVLTNS SVSHPSSLTG TPLSELGIST
DRGLGLPFSG DLMEEENDEE EQEEETDMEN TTLSKWTSGD ESYYEAGVNA EYSLDDPDSK
IQNMMASVSM RQTILLTSLT DSHSTNRMFS LRGKIMHSMC PRDLFPFSCQ AMIIYVVAHY
CLSVPLSRHS QQRDGAVGMM TTMPSSEETA EELEDREDPP SSADLSGSSN QRRKLAAPPL
SVSLDRSEGS LLSEDALDTG DEALDTGDDL DINIDELDTP DEADSLELHR HGDSEESKMA
VGAASCDVVV GHGSAEESRE SKPWRSVLIG EQEHRIDMKS IAPYKRVISH GGYYAEQNAI
IVFAACFLPD SNCDNYNYVM ENLFLYVIST LELMVAEDYM IVYLNGATPR RRMPGFSWMK
KCYQMIDRRL KKNLKMFIIV HPSWFIRTLL GITRPFISSK FSNKIKYVNS LRELGKIIPM
EYVHIPTSIV KLDTDLQDTA AKADQKRGNS TV
//