FABP1_ECHGR
ID FABP1_ECHGR Reviewed; 133 AA.
AC Q02970; Q967X3; Q9BLY5; Q9BMK1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Fatty acid-binding protein homolog 1;
DE AltName: Full=EgDf1;
DE AltName: Full=EgFABP1;
GN Name=FABP1; Synonyms=DF1;
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8479446; DOI=10.1016/0166-6851(93)90043-w;
RA Esteves A., Dallagiovanna B., Ehrlich R.;
RT "A developmentally regulated gene of Echinococcus granulosus codes for a
RT 15.5-kilodalton polypeptide related to fatty acid binding proteins.";
RL Mol. Biochem. Parasitol. 58:215-222(1993).
RN [2]
RP SEQUENCE REVISION TO 76-84 AND 129.
RA Esteves A.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Lu J.H., Guo Z.M., Yu X.B., Pan X.H., Chen J.B.;
RT "Echinococcus granulosus gene for fatty acid binding protein.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lu J.H., Yu X.B., Guo Z.M., Hu M.;
RT "Cloning and identifying Echinococcus granulosus gene for fatty acid
RT binding protein.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PALMITATE, AND
RP ACETYLATION AT MET-1.
RX PubMed=12818189; DOI=10.1016/s1570-9639(03)00151-1;
RA Jakobsson E., Alvite G., Bergfors T., Esteves A., Kleywegt G.J.;
RT "The crystal structure of Echinococcus granulosus fatty-acid-binding
RT protein 1.";
RL Biochim. Biophys. Acta 1649:40-50(2003).
CC -!- FUNCTION: Has been implicated in the acquisition, storage, and
CC transport of lipids, and may be important to the organism since it is
CC incapable of synthesizing most of its lipids de novo.
CC -!- DEVELOPMENTAL STAGE: Expressed at the tegumental level in the
CC protoscolices.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; X65947; CAA46765.2; -; mRNA.
DR EMBL; AF321119; AAK12096.1; -; Genomic_DNA.
DR EMBL; AY024340; AAK00579.1; -; Genomic_DNA.
DR EMBL; AF359278; AAK51437.1; -; mRNA.
DR PIR; S29600; S29600.
DR PDB; 1O8V; X-ray; 1.60 A; A=1-133.
DR PDBsum; 1O8V; -.
DR AlphaFoldDB; Q02970; -.
DR SMR; Q02970; -.
DR iPTMnet; Q02970; -.
DR EvolutionaryTrace; Q02970; -.
DR GO; GO:0005504; F:fatty acid binding; IEA:InterPro.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR033073; FABP4.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF83; PTHR11955:SF83; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Lipid-binding; Transport.
FT CHAIN 1..133
FT /note="Fatty acid-binding protein homolog 1"
FT /id="PRO_0000067351"
FT BINDING 107
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:12818189,
FT ECO:0007744|PDB:1O8V"
FT BINDING 127..129
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:12818189,
FT ECO:0007744|PDB:1O8V"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12818189"
FT CONFLICT 6
FT /note="G -> V (in Ref. 4; AAK51437)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> T (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="T -> N (in Ref. 4; AAK51437)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:1O8V"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:1O8V"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1O8V"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:1O8V"
SQ SEQUENCE 133 AA; 15065 MW; 55583B43F8BE837B CRC64;
MEAFLGTWKM EKSEGFDKIM ERLGVDFVTR KMGNLVKPNL IVTDLGGGKY KMRSESTFKT
TECSFKLGEK FKEVTPDSRE VASLITVENG VMKHEQDDKT KVTYIERVVE GNELKATVKV
DEVVCVRTYS KVA
