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Fatty acid-binding protein (Sj-FABPc) (Sj14FABP)

 FABP_SCHJA              Reviewed;         132 AA.
O45035; O45036; Q26517; Q86D72; Q86D73; Q86D74; Q86D75; Q86D76;
Q9BME8;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
31-JAN-2018, entry version 70.
RecName: Full=Fatty acid-binding protein;
AltName: Full=Sj-FABPc;
AltName: Full=Sj14FABP;
Schistosoma japonicum (Blood fluke).
Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida;
Schistosomatoidea; Schistosomatidae; Schistosoma.
NCBI_TaxID=6182;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Chinese;
PubMed=7958962; DOI=10.1016/0378-1119(94)90706-4;
Becker M.M., Kalinna B.H., Waine G.J., McManus D.P.;
"Gene cloning, overproduction and purification of a functionally
active cytoplasmic fatty acid-binding protein (Sj-FABPC) from the
human blood fluke Schistosoma japonicum.";
Gene 148:321-325(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=Philippines;
PubMed=11118616; DOI=10.1016/S0167-4781(00)00254-2;
Scott J.C., Kennedy M.W., McManus D.P.;
"Molecular and immunological characterisation of a polymorphic
cytosolic fatty acid binding protein from the human blood fluke of
humans, Schistosoma japonicum.";
Biochim. Biophys. Acta 1517:53-62(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Chinese;
Liu J., Cai X., Lin J., Fu Z., Ye P., Yang G., Shi F., Cai Y.,
Shen W., Martin T., Wu X.;
"Gene cloning, overproduction and preliminary vaccine testing of
Schistosoma japonicum Chinese mainland strain fatty acid-binding
protein Sj14FABP.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
CHARACTERIZATION.
STRAIN=Philippines;
PubMed=10861250; DOI=10.1042/0264-6021:3490377;
Kennedy M.W., Scott J.C., Lo S., Beauchamp J., McManus D.P.;
"Sj-FABPc fatty-acid-binding protein of the human blood fluke
Schistosoma japonicum: structural and functional characterization and
unusual solvent exposure of a portal-proximal tryptophan residue.";
Biochem. J. 349:377-384(2000).
-!- FUNCTION: May play a role in the transport of fatty acids. Binds
to various fatty acids but not retinoids.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O45035-1; Sequence=Displayed;
Name=2;
IsoId=O45035-2; Sequence=VSP_010233;
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior. {ECO:0000250}.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; L23322; AAA64426.1; -; mRNA.
EMBL; AF044409; AAC00516.1; -; mRNA.
EMBL; AF044410; AAC00517.1; -; mRNA.
EMBL; AY257686; AAP14670.1; -; mRNA.
EMBL; AY257687; AAP14671.1; -; mRNA.
EMBL; AY257688; AAP14672.1; -; mRNA.
EMBL; AY257689; AAP14673.1; -; mRNA.
EMBL; AY257690; AAP14674.1; -; mRNA.
EMBL; AY257691; AAP14675.1; -; mRNA.
EMBL; AF331756; AAG50052.1; -; mRNA.
ProteinModelPortal; O45035; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
Alternative splicing; Cytoplasm; Lipid-binding; Transport.
CHAIN 1 132 Fatty acid-binding protein.
/FTId=PRO_0000067357.
REGION 127 129 Fatty acid binding. {ECO:0000250}.
BINDING 107 107 Fatty acid. {ECO:0000250}.
VAR_SEQ 24 35 Missing (in isoform 2).
{ECO:0000303|PubMed:11118616}.
/FTId=VSP_010233.
VARIANT 13 13 T -> S (in variants C, D, E, F and H).
VARIANT 28 28 P -> A (in variants C, D, E, F and H).
VARIANT 29 29 I -> T (in variants C, D, E, F and H).
VARIANT 32 32 M -> I (in variants C, D, E, F and H).
VARIANT 79 79 N -> S (in variants D, E and F).
VARIANT 89 89 E -> D (in variants D and E).
VARIANT 99 99 A -> S (in variants C, D, E, F and H).
VARIANT 111 111 G -> C (in variants C, D and E).
VARIANT 121 121 D -> N (in variant D).
VARIANT 122 122 D -> N (in variants C, D and E).
VARIANT 123 123 V -> F (in variant B).
VARIANT 131 131 R -> Q (in variants C, D and E).
CONFLICT 94 94 Q -> H (in Ref. 1; AAA64426).
{ECO:0000305}.
SEQUENCE 132 AA; 14832 MW; 6648A3876EC627B2 CRC64;
MSSFLGKWKL SETHNFDAVM SKLGVSWPIR QMGNTVTPTV TFTMDGDTMT MLTESTFKNL
SVTFKFGEEF DEKTSDGRNV KSVVTKDSES KITQTQKDAK NTTVIVREIV GDTMKTTVTV
DDVTAIRNYK RL


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Pathways :
WP1020: Fatty Acid Biosynthesis
WP105: Fatty Acid Beta Oxidation 2
WP1061: Fatty Acid Beta Oxidation
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1139: Fatty Acid Biosynthesis
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1228: Fatty Acid Biosynthesis
WP1237: Fatty Acid Beta Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1307: Fatty Acid Beta Oxidation
WP133: Fatty Acid Omega Oxidation
WP1352: Fatty Acid Biosynthesis
WP137: Fatty Acid Biosynthesis, Initial Steps
WP143: Fatty Acid Beta Oxidation
WP148: Fatty Acid Beta Oxidation 2
WP1531: Vitamin D synthesis
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WP1647: Fatty acid biosynthesis
WP1648: Fatty acid metabolism
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WP169: Fatty Acid Beta Oxidation 3

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[Fa2h Faah] Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase)
[Fa2h Faah] Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase)
[atnM ANIA_07873] Fatty acid synthase beta subunit aflB (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein M) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14)]
[FAA2 FAM1 YER015W] Long-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2)
[fadD13 Rv3089] Long-chain-fatty-acid--CoA ligase FadD13 (EC 6.2.1.3) (Fatty acyl-CoA ligase) (FACL) (FACL13) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Very-long-chain fatty-acyl-CoA synthetase) (ACSVL)
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[sph Spy49_0398] Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase) (Linoleate hydratase) (Myosin cross-reactive antigen) (MCRA)
[Slc27a3 Acsvl3 Fatp3] Solute carrier family 27 member 3 (EC 6.2.1.-) (Long-chain fatty acid transport protein 3) (FATP-3) (Fatty acid transport protein 3) (Very long-chain acyl-CoA synthetase homolog 3) (VLCS-3)
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Bibliography :
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