FAR1_ONCVO
ID FAR1_ONCVO Reviewed; 178 AA.
AC Q25619; P91785; Q25622; Q25624;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Fatty-acid and retinol-binding protein 1;
DE AltName: Full=Antigen maltose-binding protein;
DE AltName: Full=Ov-FAR-1;
DE AltName: Full=Ov20;
DE AltName: Full=OvMBP/11;
DE AltName: Full=OvS1;
DE AltName: Full=S1 protein;
DE Flags: Precursor;
GN Name=far-1 {ECO:0000303|PubMed:12106870};
GN Synonyms=MOv2 {ECO:0000312|EMBL:AAA65186.1};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC32662.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=7770083; DOI=10.1016/0166-6851(94)00204-z;
RA Tree T.I.M., Gillespie A.J., Shepley K.J., Blaxter M.L., Tuan R.S.,
RA Bradley J.E.;
RT "Characterisation of an immunodominant glycoprotein antigen of Onchocerca
RT volvulus with homologues in other filarial nematodes and Caenorhabditis
RT elegans.";
RL Mol. Biochem. Parasitol. 69:185-195(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA59101.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8525284;
RA Erttmann K.D., Buettner D.W., Gallin M.Y.;
RT "A putative protein related to human chemokines encoded antisense to the
RT cDNA of an Onchocerca volvulus antigen.";
RL Trop. Med. Parasitol. 46:123-130(1995).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAA65186.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-178, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9223154; DOI=10.1046/j.1365-3024.1996.d01-10.x;
RA Jenkins R.E., Taylor M.J., Gilvary N., Bianco A.E.;
RT "Characterization of a secreted antigen of Onchocerca volvulus with host-
RT protective potential.";
RL Parasite Immunol. 18:29-42(1996).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAC60510.2}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-163.
RX PubMed=8058358; DOI=10.1111/j.1365-3024.1994.tb00341.x;
RA Trenholme K.R., Tree T.I.M., Gillespie A.J., Guderian R., Maizels R.M.,
RA Bradley J.E.;
RT "Heterogeneity of IgG antibody responses to cloned Onchocerca volvulus
RT antigens in microfiladermia positive individuals from Esmeraldas Province,
RT Ecuador.";
RL Parasite Immunol. 16:201-209(1994).
RN [5] {ECO:0000305}
RP RETINOL-BINDING, AND BINDING TO FATTY ACIDS.
RX PubMed=9368002; DOI=10.1074/jbc.272.47.29442;
RA Kennedy M.W., Garside L.H., Goodrick L.E., McDermott L., Brass A.,
RA Price N.C., Kelly S.M., Cooper A., Bradley J.E.;
RT "The Ov20 protein of the parasitic nematode Onchocerca volvulus. A
RT structurally novel class of small helix-rich retinol-binding proteins.";
RL J. Biol. Chem. 272:29442-29448(1997).
RN [6] {ECO:0000305}
RP LONG CHAIN FATTY ACID-BINDING.
RX PubMed=10693749; DOI=10.1016/s0166-6851(99)00191-7;
RA Mpagi J.L., Erttmann K.D., Brattig N.W.;
RT "The secretory Onchocerca volvulus protein OvS1/Ov20 exhibits the capacity
RT to compete with serum albumin for the host's long-chain fatty acids.";
RL Mol. Biochem. Parasitol. 105:273-279(2000).
RN [7] {ECO:0000305}
RP RETINOL-BINDING, BINDING TO FATTY ACIDS, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=12106870; DOI=10.1016/s0166-6851(02)00097-x;
RA Garofalo A., Klager S.L., Rowlinson M.C., Nirmalan N., Klion A.D.,
RA Allen J.E., Kennedy M.W., Bradley J.E.;
RT "The FAR proteins of filarial nematodes: secretion, glycosylation and lipid
RT binding characteristics.";
RL Mol. Biochem. Parasitol. 122:161-170(2002).
CC -!- FUNCTION: Binds retinol. Also binds the fluorescent fatty acids 11-((5-
CC dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid (DAUDA),
CC dansyl-DL-alpha-aminocaprylic acid (DACA) and parinaric acid. Binds
CC long chain fatty acids, with highest affinity for arachidonic acid,
CC linoleic acid and oleic acid. These long chain fatty acids can act
CC competitively to displace bound fluorescent fatty acids and retinol.
CC May compete with host albumin for fatty acid-binding.
CC {ECO:0000269|PubMed:10693749, ECO:0000269|PubMed:12106870,
CC ECO:0000269|PubMed:9368002}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12106870,
CC ECO:0000269|PubMed:7770083, ECO:0000269|PubMed:9223154}.
CC -!- TISSUE SPECIFICITY: Localized to the adult body wall, in particular to
CC the lateral chords. Found in the epithelium of the uterus of adult
CC females. {ECO:0000269|PubMed:7770083, ECO:0000269|PubMed:8525284,
CC ECO:0000269|PubMed:9223154}.
CC -!- DEVELOPMENTAL STAGE: Found in developing embryos, microfilariae, third
CC and fourth stage larvae and adults. {ECO:0000269|PubMed:7770083,
CC ECO:0000269|PubMed:8525284, ECO:0000269|PubMed:9223154}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12106870,
CC ECO:0000269|PubMed:7770083}.
CC -!- SIMILARITY: Belongs to the fatty-acid and retinol-binding protein
CC (FARBP) family. {ECO:0000269|PubMed:10693749,
CC ECO:0000269|PubMed:12106870, ECO:0000269|PubMed:9368002, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA59101.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; L27686; AAC32662.1; -; mRNA.
DR EMBL; X84358; CAA59101.1; ALT_SEQ; mRNA.
DR EMBL; L41652; AAA65186.1; -; mRNA.
DR EMBL; S71371; AAC60510.2; -; mRNA.
DR AlphaFoldDB; Q25619; -.
DR SMR; Q25619; -.
DR STRING; 6282.Q25619; -.
DR HOGENOM; CLU_117803_0_0_1; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IDA:UniProtKB.
DR InterPro; IPR008632; Gp-FAR-1.
DR PANTHER; PTHR31418; PTHR31418; 1.
DR Pfam; PF05823; Gp-FAR-1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Glycoprotein; Lipid-binding; Reference proteome;
KW Retinol-binding; Secreted; Signal; Vitamin A.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..178
FT /note="Fatty-acid and retinol-binding protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008765"
FT COILED 67..89
FT /evidence="ECO:0000255"
FT COILED 122..154
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="L -> H (in Ref. 2; CAA59101)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> T (in Ref. 2; CAA59101)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="I -> N (in Ref. 4; AAC60510)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> T (in Ref. 2; CAA59101)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..163
FT /note="IIT -> RNS (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ 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
