ACBP_CHAVI
ID ACBP_CHAVI Reviewed; 87 AA.
AC P82934;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Acyl-CoA-binding protein;
DE Short=ACBP;
DE AltName: Full=EP;
GN Name=DBI;
OS Chaetophractus villosus (South American armadillo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Cingulata; Chlamyphoridae; Chaetophractus.
OX NCBI_TaxID=29080;
RN [1]
RP PROTEIN SEQUENCE OF 2-87, AND ACETYLATION AT SER-2.
RC TISSUE=Harderian gland;
RX PubMed=11342056; DOI=10.1016/s0167-4838(00)00294-6;
RA Cavagnari B.M., Sterin-Speziale N., Affanni J.M., Knudsen J., Santome J.A.;
RT "Acyl-CoA-binding protein in the armadillo Harderian gland: its primary
RT structure and possible role in lipid secretion.";
RL Biochim. Biophys. Acta 1545:314-325(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=17012783; DOI=10.1107/s1744309106038164;
RA Costabel M.D., Ermacora M.R., Santome J.A., Alzari P.M., Guerin D.M.A.;
RT "Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein
RT family.";
RL Acta Crystallogr. F 62:958-961(2006).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity and may function as an intracellular carrier of acyl-CoA
CC esters.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P07108}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P07108}. Note=Golgi localization is dependent on
CC ligand binding. {ECO:0000250|UniProtKB:P07108}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR PDB; 2FDQ; X-ray; 3.50 A; A/B/C=2-87.
DR PDBsum; 2FDQ; -.
DR AlphaFoldDB; P82934; -.
DR SMR; P82934; -.
DR iPTMnet; P82934; -.
DR EvolutionaryTrace; P82934; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR CDD; cd00435; ACBP; 1.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Endoplasmic reticulum; Golgi apparatus; Hydroxylation; Lipid-binding;
KW Phosphoprotein; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11342056"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000214003"
FT DOMAIN 2..87
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 14
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 29..33
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:11342056"
FT MOD_RES 8
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 8
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 17
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 55
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 55
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 77
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 77
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2FDQ"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2FDQ"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:2FDQ"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2FDQ"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:2FDQ"
SQ SEQUENCE 87 AA; 10022 MW; B4BA1D728DA2B602 CRC64;
MSQAEFDKAA EEVKNLKTKP ADDEMLFIYS HYKQATVGDI NTERPGMLDF KGKAKWDAWN
QLKGTSKEDA MKSYIDKVEE LKKKYGI
