FABP_SCHJA
ID FABP_SCHJA Reviewed; 132 AA.
AC O45035; O45036; Q26517; Q86D72; Q86D73; Q86D74; Q86D75; Q86D76; Q9BME8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Fatty acid-binding protein;
DE AltName: Full=Sj-FABPc;
DE AltName: Full=Sj14FABP;
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Chinese;
RX PubMed=7958962; DOI=10.1016/0378-1119(94)90706-4;
RA Becker M.M., Kalinna B.H., Waine G.J., McManus D.P.;
RT "Gene cloning, overproduction and purification of a functionally active
RT cytoplasmic fatty acid-binding protein (Sj-FABPC) from the human blood
RT fluke Schistosoma japonicum.";
RL Gene 148:321-325(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Philippines;
RX PubMed=11118616; DOI=10.1016/s0167-4781(00)00254-2;
RA Scott J.C., Kennedy M.W., McManus D.P.;
RT "Molecular and immunological characterisation of a polymorphic cytosolic
RT fatty acid binding protein from the human blood fluke of humans,
RT Schistosoma japonicum.";
RL Biochim. Biophys. Acta 1517:53-62(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Chinese;
RA Liu J., Cai X., Lin J., Fu Z., Ye P., Yang G., Shi F., Cai Y., Shen W.,
RA Martin T., Wu X.;
RT "Gene cloning, overproduction and preliminary vaccine testing of
RT Schistosoma japonicum Chinese mainland strain fatty acid-binding protein
RT Sj14FABP.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RC STRAIN=Philippines;
RX PubMed=10861250; DOI=10.1042/0264-6021:3490377;
RA Kennedy M.W., Scott J.C., Lo S., Beauchamp J., McManus D.P.;
RT "Sj-FABPc fatty-acid-binding protein of the human blood fluke Schistosoma
RT japonicum: structural and functional characterization and unusual solvent
RT exposure of a portal-proximal tryptophan residue.";
RL Biochem. J. 349:377-384(2000).
CC -!- FUNCTION: May play a role in the transport of fatty acids. Binds to
CC various fatty acids but not retinoids.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O45035-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O45035-2; Sequence=VSP_010233;
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}.
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DR EMBL; L23322; AAA64426.1; -; mRNA.
DR EMBL; AF044409; AAC00516.1; -; mRNA.
DR EMBL; AF044410; AAC00517.1; -; mRNA.
DR EMBL; AY257686; AAP14670.1; -; mRNA.
DR EMBL; AY257687; AAP14671.1; -; mRNA.
DR EMBL; AY257688; AAP14672.1; -; mRNA.
DR EMBL; AY257689; AAP14673.1; -; mRNA.
DR EMBL; AY257690; AAP14674.1; -; mRNA.
DR EMBL; AY257691; AAP14675.1; -; mRNA.
DR EMBL; AF331756; AAG50052.1; -; mRNA.
DR AlphaFoldDB; O45035; -.
DR SMR; O45035; -.
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 Alternative splicing; Cytoplasm; Lipid-binding; Transport.
FT CHAIN 1..132
FT /note="Fatty acid-binding protein"
FT /id="PRO_0000067357"
FT BINDING 107
FT /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT /ligand_id="ChEBI:CHEBI:32395"
FT /evidence="ECO:0000250|UniProtKB:P29498"
FT BINDING 107
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P29498"
FT BINDING 127..129
FT /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT /ligand_id="ChEBI:CHEBI:32395"
FT /evidence="ECO:0000250|UniProtKB:P29498"
FT BINDING 127..129
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P29498"
FT VAR_SEQ 24..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11118616"
FT /id="VSP_010233"
FT VARIANT 13
FT /note="T -> S (in variants C, D, E, F and H)"
FT VARIANT 28
FT /note="P -> A (in variants C, D, E, F and H)"
FT VARIANT 29
FT /note="I -> T (in variants C, D, E, F and H)"
FT VARIANT 32
FT /note="M -> I (in variants C, D, E, F and H)"
FT VARIANT 79
FT /note="N -> S (in variants D, E and F)"
FT VARIANT 89
FT /note="E -> D (in variants D and E)"
FT VARIANT 99
FT /note="A -> S (in variants C, D, E, F and H)"
FT VARIANT 111
FT /note="G -> C (in variants C, D and E)"
FT VARIANT 121
FT /note="D -> N (in variant D)"
FT VARIANT 122
FT /note="D -> N (in variants C, D and E)"
FT VARIANT 123
FT /note="V -> F (in variant B)"
FT VARIANT 131
FT /note="R -> Q (in variants C, D and E)"
FT CONFLICT 94
FT /note="Q -> H (in Ref. 1; AAA64426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 14832 MW; 6648A3876EC627B2 CRC64;
MSSFLGKWKL SETHNFDAVM SKLGVSWPIR QMGNTVTPTV TFTMDGDTMT MLTESTFKNL
SVTFKFGEEF DEKTSDGRNV KSVVTKDSES KITQTQKDAK NTTVIVREIV GDTMKTTVTV
DDVTAIRNYK RL
