ID   FABP2_MANSE             Reviewed;         132 AA.
AC   P31417;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Fatty acid-binding protein 2;
DE            Short=FABP 2;
GN   Name=MFB2;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=1730603; DOI=10.1016/s0021-9258(18)48505-5;
RA   Smith A.F., Tsuchida K., Hanneman E., Suzuki T.C., Wells M.A.;
RT   "Isolation, characterization, and cDNA sequence of two fatty acid-binding
RT   proteins from the midgut of Manduca sexta larvae.";
RL   J. Biol. Chem. 267:380-384(1992).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH PALMITATE, AND
RP   ACETYLATION AT SER-2.
RX   PubMed=1447782; DOI=10.1016/0022-2836(92)90501-a;
RA   Benning M.M., Smith A.F., Wells M.A., Holden H.M.;
RT   "Crystallization, structure determination and least-squares refinement to
RT   1.75-A resolution of the fatty-acid-binding protein isolated from Manduca
RT   sexta L.";
RL   J. Mol. Biol. 228:208-219(1992).
CC   -!- FUNCTION: Binds fatty acids in a 1:1 molar ratio.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1447782}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Midgut.
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}.
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; M77755; AAA29314.1; -; mRNA.
DR   PIR; B41749; B41749.
DR   PDB; 1MDC; X-ray; 1.75 A; A=2-132.
DR   PDBsum; 1MDC; -.
DR   AlphaFoldDB; P31417; -.
DR   SMR; P31417; -.
DR   iPTMnet; P31417; -.
DR   EvolutionaryTrace; P31417; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; PTHR11955; 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; Cytoplasm; Lipid-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..132
FT                   /note="Fatty acid-binding protein 2"
FT                   /id="PRO_0000067361"
FT   BINDING         40
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000269|PubMed:1447782,
FT                   ECO:0007744|PDB:1MDC"
FT   BINDING         128..130
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000269|PubMed:1447782,
FT                   ECO:0007744|PDB:1MDC"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1447782"
FT   STRAND          8..15
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   HELIX           16..21
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   HELIX           27..35
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          100..109
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          112..119
FT                   /evidence="ECO:0007829|PDB:1MDC"
FT   STRAND          122..131
FT                   /evidence="ECO:0007829|PDB:1MDC"
SQ   SEQUENCE   132 AA;  14212 MW;  6971DFF301FE9F29 CRC64;
     MSYLGKVYSL VKQENFDGFL KSAGLSDDKI QALVSDKPTQ KMEANGDSYS ITSTGIGGER
     TVSFKSGVEF DDVIGAGESV KSMYTVDGNV VTHVVKGDAG VATFKKEYNG DDLVVTITSS
     NWDGVARRYY KA