ID A0A3P9MXE8_POERE Unreviewed; 514 AA.
AC A0A3P9MXE8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA binding domain containing 3 {ECO:0000313|Ensembl:ENSPREP00000001915.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000001915.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000001915.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000001915.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3P9MXE8; -.
DR STRING; 8081.ENSPREP00000001915; -.
DR Ensembl; ENSPRET00000001959.1; ENSPREP00000001915.1; ENSPREG00000001402.1.
DR GeneTree; ENSGT00530000063651; -.
DR OMA; SYSIWRS; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000001402; Expressed in head and 1 other cell type or tissue.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22973:SF14; GOLGI RESIDENT PROTEIN GCP60; 1.
DR PANTHER; PTHR22973; LD35087P; 1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638}.
FT DOMAIN 77..168
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT DOMAIN 369..512
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 59587 MW; EF5009B166A3901C CRC64;
MEAAEVQSGD LDSATTSRLE VSIDGLTLSP DPEDEQNQVE EPNLAPTQPG TDTPADEEGD
DGESGKSAIE RKWGFPLLEL YGLALKFFKD KDGKAFHPTY EEKLRLVALH KQVLLGPYNP
DASPEVGFFD VLGNDRRKEW ASLGNMEKEE AMVEFVKLLN KCCNLFAPYV ISHRIEREEQ
ERKRKEEEER LRQEEEERER QRQEEERRRL EEEDRLRREE EERRQAEEER LRIEQQKQQI
MAALNAQTAV QFQQYAAQQY PNNPEQQMSL IRQLQEQHYQ QYMQQLYQVQ LAQQQVTTTT
RERAACFGLE KYASPTVNGG QSDSYSESMD REQEPELAEE VSENGPLLDS PPVIAAPSMW
TRPQIKDFKE KIRQDPDSVI TVGRGEVVTV RVPTHEEGAY LFWEFATDYY DIGFGVFFEW
TDAASASVSV HVSESSDEDE EDEGDPPTEE EKAKKEAGKP HVDEIVPVYR RDCHEEVYAG
SHQYPGRGVY LLKFDNSYSL WRSKSVYYRV YYTR
//
