ID   FABPM_LOCMI             Reviewed;         134 AA.
AC   P41509;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Fatty acid-binding protein, muscle;
DE   AltName: Full=M-FABP;
OS   Locusta migratoria (Migratory locust).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Oedipodinae; Locusta.
OX   NCBI_TaxID=7004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-42.
RC   TISSUE=Flight muscle;
RX   PubMed=8174560; DOI=10.1111/j.1432-1033.1994.tb18794.x;
RA   Maatman R.G.H.J., Degano M., van Moerkerk H.T.B., van Marrewijk W.J.A.,
RA   van der Horst D.J., Sacchettini J.C., Veerkamp J.H.;
RT   "Primary structure and binding characteristics of locust and human muscle
RT   fatty-acid-binding proteins.";
RL   Eur. J. Biochem. 221:801-810(1994).
RN   [2] {ECO:0007744|PDB:2FLJ}
RP   STRUCTURE BY NMR IN COMPLEX WITH OLEATE.
RX   PubMed=16700541; DOI=10.1021/bi060224f;
RA   Luecke C., Qiao Y., van Moerkerk H.T.B., Veerkamp J.H., Hamilton J.A.;
RT   "Fatty-acid-binding protein from the flight muscle of Locusta migratoria:
RT   evolutionary variations in fatty acid binding.";
RL   Biochemistry 45:6296-6305(2006).
CC   -!- FUNCTION: Binds fatty acids in a 1:1 molar ratio.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; S70162; AAB30739.1; -; mRNA.
DR   PIR; S43470; S43470.
DR   PDB; 2FLJ; NMR; -; A=1-134.
DR   PDBsum; 2FLJ; -.
DR   AlphaFoldDB; P41509; -.
DR   BMRB; P41509; -.
DR   SMR; P41509; -.
DR   EvolutionaryTrace; P41509; -.
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; Cytoplasm; Direct protein sequencing; Lipid-binding;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8174560"
FT   CHAIN           2..134
FT                   /note="Fatty acid-binding protein, muscle"
FT                   /id="PRO_0000067363"
FT   BINDING         109
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000269|PubMed:16700541,
FT                   ECO:0007744|PDB:2FLJ"
FT   BINDING         129..131
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000269|PubMed:16700541,
FT                   ECO:0007744|PDB:2FLJ"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          9..17
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   HELIX           18..24
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   HELIX           29..37
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          82..99
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          113..122
FT                   /evidence="ECO:0007829|PDB:2FLJ"
FT   STRAND          125..133
FT                   /evidence="ECO:0007829|PDB:2FLJ"
SQ   SEQUENCE   134 AA;  15064 MW;  1C74BAC6965ED0A5 CRC64;
     MVKEFAGIKY KLDSQTNFEE YMKAIGVGAI ERKAGLALSP VIELEVLDGD KFKLTSKTAI
     KNTEFTFKLG EEFDEDTLDG RKVKSIITQD GPNKLVHEQK GDHPTIIIRE FSKEQCVITI
     KLGDLVATRI YKAQ