FABPM_SCHGR
ID FABPM_SCHGR Reviewed; 134 AA.
AC P41496;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Fatty acid-binding protein, muscle;
DE AltName: Full=M-FABP;
OS Schistocerca gregaria (Desert locust) (Gryllus gregarius).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX NCBI_TaxID=7010;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-134, AND PROTEIN SEQUENCE OF 2-40.
RC TISSUE=Flight muscle;
RX PubMed=1497348; DOI=10.1016/0003-9861(92)90674-l;
RA Price H.M., Ryan R.O., Haunerland N.H.;
RT "Primary structure of locust flight muscle fatty acid binding protein.";
RL Arch. Biochem. Biophys. 297:285-290(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11267894; DOI=10.1016/s0965-1748(00)00158-2;
RA Wu Q., Andolfatto P., Haunerland N.H.;
RT "Cloning and sequence of the gene encoding the muscle fatty acid binding
RT protein from the desert locust, Schistocerca gregaria.";
RL Insect Biochem. Mol. Biol. 31:553-562(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7918460; DOI=10.1021/bi00207a004;
RA Haunerland N.H., Jacobson B.L., Wesenberg G., Rayment I., Holden H.M.;
RT "Three-dimensional structure of the muscle fatty-acid-binding protein
RT isolated from the desert locust Schistocerca gregaria.";
RL Biochemistry 33:12378-12385(1994).
CC -!- FUNCTION: Binds fatty acids in a 1:1 molar ratio.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Adult flight muscle.
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; M95918; AAA19622.1; ALT_SEQ; mRNA.
DR EMBL; AF244981; AAK20174.1; -; Genomic_DNA.
DR EMBL; AF244980; AAK20174.1; JOINED; Genomic_DNA.
DR PIR; A44870; A44870.
DR PDB; 1FTP; X-ray; 2.20 A; A/B=2-134.
DR PDBsum; 1FTP; -.
DR AlphaFoldDB; P41496; -.
DR BMRB; P41496; -.
DR SMR; P41496; -.
DR EvolutionaryTrace; P41496; -.
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:1497348"
FT CHAIN 2..134
FT /note="Fatty acid-binding protein, muscle"
FT /id="PRO_0000067364"
FT BINDING 109
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P41509"
FT BINDING 129..131
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P41509"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:1FTP"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1FTP"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1FTP"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1FTP"
SQ SEQUENCE 134 AA; 15080 MW; 161D7E4F49413EA5 CRC64;
MVKEFAGIKY KLDSQTNFEE YMKAIGVGAI ERKAGLALSP VIELEILDGD KFKLTSKTAI
KNTEFTFKLG EEFDEETLDG RKVKSTITQD GPNKLVHEQK GDHPTIIIRE FSKEQCVITI
KLGDLVATRI YKAQ
