FABP_SCHMA
ID FABP_SCHMA Reviewed; 133 AA.
AC P29498; Q8T5U8; Q8T5U9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=14 kDa fatty acid-binding protein;
DE AltName: Full=Sm14;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=2022660; DOI=10.1016/s0021-9258(18)92995-9;
RA Moser D., Tendler M., Griffiths G., Klinkert M.-Q.;
RT "A 14-kDa Schistosoma mansoni polypeptide is homologous to a gene family of
RT fatty acid binding proteins.";
RL J. Biol. Chem. 266:8447-8454(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=Brazilian BH;
RA Romero-Ramos C.R., Tendler M., Ho P.L.;
RT "Cloning and sequence of the gene encoding Schistosoma mansoni fatty acid-
RT binding protein, Sm14.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), AND VARIANT THR-20.
RC STRAIN=Brazilian BH, and LE;
RA Romero-Ramos C.R., Figueredo R.C.R., Pertinhez T.A., Nasciemento A.L.T.O.,
RA Tendler M., Raw I., Spisni A., Ho P.L.;
RT "Polymorphism of the Schistosoma mansoni Sm14 fatty acid-binding protein:
RT structural and functional analysis.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:1VYF, ECO:0007744|PDB:1VYG}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH ARACHIDONATE AND
RP OLEATE.
RX PubMed=15476393; DOI=10.1021/bi048505f;
RA Angelucci F., Johnson K.A., Baiocco P., Miele A.E., Brunori M., Valle C.,
RA Vigorosi F., Troiani A.R., Liberti P., Cioli D., Klinkert M.-Q.,
RA Bellelli A.;
RT "Schistosoma mansoni fatty acid binding protein: specificity and functional
RT control as revealed by crystallographic structure.";
RL Biochemistry 43:13000-13011(2004).
CC -!- FUNCTION: May play a role in the transport of fatty acids. Binds
CC various fatty acids, such as arachidonic, oleic, palmitic and linolenic
CC acid (in vitro).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29498-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta E3;
CC IsoId=P29498-2; Sequence=VSP_010234;
CC -!- TISSUE SPECIFICITY: Tubercles, muscle layers and body.
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; M60895; AAA63516.1; -; mRNA.
DR EMBL; AY055467; AAL15461.1; -; Genomic_DNA.
DR EMBL; AF492389; AAM18480.1; -; mRNA.
DR EMBL; AF492390; AAM18481.1; -; mRNA.
DR PIR; A39818; A39818.
DR RefSeq; XP_018647195.1; XM_018792798.1. [P29498-2]
DR RefSeq; XP_018647196.1; XM_018792809.1. [P29498-1]
DR PDB; 1VYF; X-ray; 1.85 A; A=1-133.
DR PDB; 1VYG; X-ray; 2.40 A; A=1-133.
DR PDB; 2POA; NMR; -; A=1-133.
DR PDBsum; 1VYF; -.
DR PDBsum; 1VYG; -.
DR PDBsum; 2POA; -.
DR AlphaFoldDB; P29498; -.
DR BMRB; P29498; -.
DR SMR; P29498; -.
DR STRING; 6183.Smp_095360.1; -.
DR DrugBank; DB04557; Arachidonic Acid.
DR EnsemblMetazoa; Smp_095360.1; Smp_095360.1; Smp_095360. [P29498-1]
DR GeneID; 8344852; -.
DR KEGG; smm:Smp_095360.1; -.
DR WBParaSite; Smp_095360.1; Smp_095360.1; Smp_095360.
DR WBParaSite; Smp_095360.2; Smp_095360.2; Smp_095360.
DR CTD; 8344852; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_0_2_1; -.
DR OMA; LTAKCIM; -.
DR PhylomeDB; P29498; -.
DR EvolutionaryTrace; P29498; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR ExpressionAtlas; P29498; baseline.
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; Alternative splicing; Cytoplasm; Lipid-binding;
KW Reference proteome; Transport.
FT CHAIN 1..133
FT /note="14 kDa fatty acid-binding protein"
FT /id="PRO_0000067358"
FT BINDING 107
FT /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT /ligand_id="ChEBI:CHEBI:32395"
FT /evidence="ECO:0000269|PubMed:15476393,
FT ECO:0007744|PDB:1VYG"
FT BINDING 107
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|PubMed:15476393,
FT ECO:0007744|PDB:1VYF"
FT BINDING 127..129
FT /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT /ligand_id="ChEBI:CHEBI:32395"
FT /evidence="ECO:0000269|PubMed:15476393,
FT ECO:0007744|PDB:1VYG"
FT BINDING 127..129
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|PubMed:15476393,
FT ECO:0007744|PDB:1VYF"
FT VAR_SEQ 82..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010234"
FT VARIANT 20
FT /note="M -> T"
FT /evidence="ECO:0000269|Ref.3"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:1VYF"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:1VYF"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2POA"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1VYF"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2POA"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1VYF"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1VYF"
SQ SEQUENCE 133 AA; 14848 MW; 1A1E0E262C59D76F CRC64;
MSSFLGKWKL SESHNFDAVM SKLGVSWATR QIGNTVTPTV TFTMDGDKMT MLTESTFKNL
SCTFKFGEEF DEKTSDGRNV KSVVEKNSES KLTQTQVDPK NTTVIVREVD GDTMKTTVTV
GDVTAIRNYK RLS
