ACB5B_DANRE
ID ACB5B_DANRE Reviewed; 410 AA.
AC A5WV69;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5-B;
GN Name=acbd5b; ORFNames=si:ch211-112d19.6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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DR EMBL; CR956623; CAN87907.1; -; Genomic_DNA.
DR RefSeq; NP_001093558.1; NM_001100088.1.
DR RefSeq; XP_005171197.1; XM_005171140.2.
DR AlphaFoldDB; A5WV69; -.
DR SMR; A5WV69; -.
DR STRING; 7955.ENSDARP00000075696; -.
DR PaxDb; A5WV69; -.
DR Ensembl; ENSDART00000081253; ENSDARP00000075696; ENSDARG00000058410.
DR Ensembl; ENSDART00000140434; ENSDARP00000122411; ENSDARG00000058410.
DR GeneID; 100004736; -.
DR KEGG; dre:100004736; -.
DR CTD; 100004736; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000156350; -.
DR InParanoid; A5WV69; -.
DR OMA; PYMQFNG; -.
DR OrthoDB; 1546859at2759; -.
DR PhylomeDB; A5WV69; -.
DR PRO; PR:A5WV69; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000058410; Expressed in retina and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.20.80.10; -; 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 Pfam; PF00887; ACBP; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Lipid-binding; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..410
FT /note="Acyl-CoA-binding domain-containing protein 5-B"
FT /id="PRO_0000397927"
FT TRANSMEM 382..404
FT /evidence="ECO:0000255"
FT DOMAIN 12..101
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 119..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 326..355
FT /evidence="ECO:0000255"
FT COMPBIAS 143..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23..32
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 43..47
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
SQ SEQUENCE 410 AA; 45788 MW; 6C679B8DD0E5F887 CRC64;
MILRGMEDSK SAQKRFEAAV KVIRSLPEDG SYDLSDDMLV LFYSYYKQAT EGPCNTLKPN
SWDPIGKAKW EAWKDLGNMS KDQAMTEYVQ EIQLIIETLP VTDRMAELLD ALDPFYEIVE
DDDDDDDEGV SKAAPLFTGS TNADKDAERD EEVESESKEG NLDDYMELVE KQKDLSSTTG
EKGSLLVFNR SEENSISSLT DGTHSSLNTV DDEEELVYDG SDDEMDSDSM DKPATPEKGS
GVRSVRLADG SVVGANMQHG GNREPQCGSQ DGKPQGLISP VPHPPTLGTV RNDRISACSG
RERGCQGDGG QRGETADRMD KQAINTQITT ILSELEDNMQ DVLRRLTTLE QLTASQAEIS
PSKTWHSDKP KKRLSWWPLN SSPFTAVLTV LWPFAVHWLV QFYLQRRRRR
