ID   FAR1_ONCDU              Reviewed;         178 AA.
AC   Q8WT58;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Fatty-acid and retinol-binding protein 1;
DE   AltName: Full=Od-FAR-1;
DE   Flags: Precursor;
GN   Name=far-1 {ECO:0000312|EMBL:AAL33790.1};
OS   Onchocerca dukei (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=173668;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL33790.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 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 and different fatty acids. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q25619}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12106870}.
CC   -!- SIMILARITY: Belongs to the fatty-acid and retinol-binding protein
CC       (FARBP) family. {ECO:0000250|UniProtKB:Q25619, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY050254; AAL33790.1; -; mRNA.
DR   AlphaFoldDB; Q8WT58; -.
DR   SMR; Q8WT58; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0019841; F:retinol binding; ISS: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; Retinol-binding; Secreted;
KW   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_0000008762"
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"
SQ   SEQUENCE   178 AA;  20552 MW;  C402134AA86CFB44 CRC64;
     MYHQLILMAL IGVIMANVVP FSMSNIPEEY KEFIPEEVKN FYKNLTQEDR QILRELASKH
     ATFANEDAAL EALKNTSDKL YQKAVELRNF VKAKIDSLKP DAKAFVDEII AKVRSLRPED
     GQKLDMEKLK QAARDIIAKY EALNEETREE LKATFPNTTK IITNEKFKRI ANSFLQKN