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Fatty-acid and retinol-binding protein 1 (Antigen maltose-binding protein) (Ov-FAR-1) (Ov20) (OvMBP/11) (OvS1) (S1 protein)

 FAR1_ONCVO              Reviewed;         178 AA.
Q25619; P91785; Q25622; Q25624;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 48.
RecName: Full=Fatty-acid and retinol-binding protein 1;
AltName: Full=Antigen maltose-binding protein;
AltName: Full=Ov-FAR-1;
AltName: Full=Ov20;
AltName: Full=OvMBP/11;
AltName: Full=OvS1;
AltName: Full=S1 protein;
Flags: Precursor;
Name=far-1 {ECO:0000303|PubMed:12106870};
Synonyms=MOv2 {ECO:0000312|EMBL:AAA65186.1};
Onchocerca volvulus.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida;
Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
NCBI_TaxID=6282;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC32662.1}
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
PubMed=7770083; DOI=10.1016/0166-6851(94)00204-Z;
Tree T.I.M., Gillespie A.J., Shepley K.J., Blaxter M.L., Tuan R.S.,
Bradley J.E.;
"Characterisation of an immunodominant glycoprotein antigen of
Onchocerca volvulus with homologues in other filarial nematodes and
Caenorhabditis elegans.";
Mol. Biochem. Parasitol. 69:185-195(1995).
[2] {ECO:0000305, ECO:0000312|EMBL:CAA59101.1}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=8525284;
Erttmann K.D., Buettner D.W., Gallin M.Y.;
"A putative protein related to human chemokines encoded antisense to
the cDNA of an Onchocerca volvulus antigen.";
Trop. Med. Parasitol. 46:123-130(1995).
[3] {ECO:0000305, ECO:0000312|EMBL:AAA65186.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 32-178, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=9223154; DOI=10.1046/j.1365-3024.1996.d01-10.x;
Jenkins R.E., Taylor M.J., Gilvary N., Bianco A.E.;
"Characterization of a secreted antigen of Onchocerca volvulus with
host-protective potential.";
Parasite Immunol. 18:29-42(1996).
[4] {ECO:0000305, ECO:0000312|EMBL:AAC60510.2}
NUCLEOTIDE SEQUENCE [MRNA] OF 66-163.
PubMed=8058358; DOI=10.1111/j.1365-3024.1994.tb00341.x;
Trenholme K.R., Tree T.I.M., Gillespie A.J., Guderian R.,
Maizels R.M., Bradley J.E.;
"Heterogeneity of IgG antibody responses to cloned Onchocerca volvulus
antigens in microfiladermia positive individuals from Esmeraldas
Province, Ecuador.";
Parasite Immunol. 16:201-209(1994).
[5] {ECO:0000305}
RETINOL-BINDING, AND BINDING TO FATTY ACIDS.
PubMed=9368002; DOI=10.1074/jbc.272.47.29442;
Kennedy M.W., Garside L.H., Goodrick L.E., McDermott L., Brass A.,
Price N.C., Kelly S.M., Cooper A., Bradley J.E.;
"The Ov20 protein of the parasitic nematode Onchocerca volvulus. A
structurally novel class of small helix-rich retinol-binding
proteins.";
J. Biol. Chem. 272:29442-29448(1997).
[6] {ECO:0000305}
LONG CHAIN FATTY ACID-BINDING.
PubMed=10693749; DOI=10.1016/S0166-6851(99)00191-7;
Mpagi J.L., Erttmann K.D., Brattig N.W.;
"The secretory Onchocerca volvulus protein OvS1/Ov20 exhibits the
capacity to compete with serum albumin for the host's long-chain fatty
acids.";
Mol. Biochem. Parasitol. 105:273-279(2000).
[7] {ECO:0000305}
RETINOL-BINDING, BINDING TO FATTY ACIDS, SUBCELLULAR LOCATION, AND
GLYCOSYLATION.
PubMed=12106870; DOI=10.1016/S0166-6851(02)00097-X;
Garofalo A., Klager S.L., Rowlinson M.C., Nirmalan N., Klion A.D.,
Allen J.E., Kennedy M.W., Bradley J.E.;
"The FAR proteins of filarial nematodes: secretion, glycosylation and
lipid binding characteristics.";
Mol. Biochem. Parasitol. 122:161-170(2002).
-!- FUNCTION: Binds retinol. Also binds the fluorescent fatty acids
11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid
(DAUDA), dansyl-DL-alpha-aminocaprylic acid (DACA) and parinaric
acid. Binds long chain fatty acids, with highest affinity for
arachidonic acid, linoleic acid and oleic acid. These long chain
fatty acids can act competitively to displace bound fluorescent
fatty acids and retinol. May compete with host albumin for fatty
acid-binding. {ECO:0000269|PubMed:10693749,
ECO:0000269|PubMed:12106870, ECO:0000269|PubMed:9368002}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12106870,
ECO:0000269|PubMed:7770083, ECO:0000269|PubMed:9223154}.
-!- TISSUE SPECIFICITY: Localized to the adult body wall, in
particular to the lateral chords. Found in the epithelium of the
uterus of adult females. {ECO:0000269|PubMed:7770083,
ECO:0000269|PubMed:8525284, ECO:0000269|PubMed:9223154}.
-!- DEVELOPMENTAL STAGE: Found in developing embryos, microfilariae,
third and fourth stage larvae and adults.
{ECO:0000269|PubMed:7770083, ECO:0000269|PubMed:8525284,
ECO:0000269|PubMed:9223154}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12106870,
ECO:0000269|PubMed:7770083}.
-!- SIMILARITY: Belongs to the fatty-acid and retinol-binding protein
(FARBP) family. {ECO:0000269|PubMed:10693749,
ECO:0000269|PubMed:12106870, ECO:0000269|PubMed:9368002,
ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA59101.1; Type=Erroneous termination; Positions=2; Note=Translated as Tyr.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L27686; AAC32662.1; -; mRNA.
EMBL; X84358; CAA59101.1; ALT_SEQ; mRNA.
EMBL; L41652; AAA65186.1; -; mRNA.
EMBL; S71371; AAC60510.2; -; mRNA.
SMR; Q25619; -.
Proteomes; UP000024404; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
GO; GO:0019841; F:retinol binding; IDA:UniProtKB.
InterPro; IPR008632; Gp-FAR-1.
Pfam; PF05823; Gp-FAR-1; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Glycoprotein; Lipid-binding;
Reference proteome; Retinol-binding; Secreted; Signal; Vitamin A.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 178 Fatty-acid and retinol-binding protein 1.
{ECO:0000255}.
/FTId=PRO_0000008765.
COILED 67 89 {ECO:0000255}.
COILED 122 154 {ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 53 53 L -> H (in Ref. 2; CAA59101).
{ECO:0000305}.
CONFLICT 75 75 N -> T (in Ref. 2; CAA59101).
{ECO:0000305}.
CONFLICT 137 137 I -> N (in Ref. 4; AAC60510).
{ECO:0000305}.
CONFLICT 153 153 A -> T (in Ref. 2; CAA59101).
{ECO:0000305}.
CONFLICT 161 163 IIT -> RNS (in Ref. 4). {ECO:0000305}.
SEQUENCE 178 AA; 20581 MW; DF1ABE6A29FFF07E CRC64;
MYHQLILMAL IGVIMANVVP FSMSNIPEEY KEFIPEEVKN FYKNLTQEDR QILRELASKH
ATFTNEDAAL EALKNKSDKL YQKAVELRNF VKAKIDSLKP DAKAFVDEII AKVRSLRPED
GQKLDMEKLK QAARDIIAKY EALNEETKEE LKATFPNTTK IITNEKFKRI ANSFLQKN


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