ID   FABP2_ECHGR             Reviewed;         133 AA.
AC   Q9BMK3; Q9BMK2;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Fatty acid-binding protein homolog 2;
GN   Name=FABP2;
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 [GENOMIC DNA / MRNA].
RA   Esteves A.;
RT   "Searching and characterization of Echinococcus granulosus genes involved
RT   in development.";
RL   Thesis (1996), PEDECIBA, Uruguay.
CC   -!- FUNCTION: May play a role in the acquisition, storage, and transport of
CC       lipids, and may be important to the organism since it is incapable of
CC       synthesizing most of its lipids de novo. {ECO:0000305}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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; AF321117; AAK12094.1; -; Genomic_DNA.
DR   EMBL; AF321118; AAK12095.1; -; mRNA.
DR   AlphaFoldDB; Q9BMK3; -.
DR   SMR; Q9BMK3; -.
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   2: Evidence at transcript level;
KW   Lipid-binding; Transport.
FT   CHAIN           1..133
FT                   /note="Fatty acid-binding protein homolog 2"
FT                   /id="PRO_0000067352"
FT   BINDING         107
FT                   /ligand="a fatty acid"
FT                   /ligand_id="ChEBI:CHEBI:28868"
FT                   /evidence="ECO:0000250|UniProtKB:Q02970"
FT   BINDING         127..129
FT                   /ligand="a fatty acid"
FT                   /ligand_id="ChEBI:CHEBI:28868"
FT                   /evidence="ECO:0000250|UniProtKB:Q02970"
FT   CONFLICT        110
FT                   /note="Y -> D (in Ref. 1; AAK12095)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   133 AA;  15409 MW;  AB562FE2DBB55E84 CRC64;
     MEPFIGTWKM EKSEGFDKIM ERLGVDYFTR KMGNMMKPNL IISDLGDGRY NMRSESKFKT
     SEFSFKLGEQ FKEVTPDSRE VMSMLTVEDG VLKQEQVGKD KTTYIDRVVY GNELRATVKA
     DELVCVRTYS RGM