ID   FAR1_BRUMA              Reviewed;         178 AA.
AC   Q93142;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Fatty-acid and retinol-binding protein 1;
DE   AltName: Full=Bm-FAR-1;
DE   AltName: Full=Bm20;
DE   Flags: Precursor;
GN   Name=far-1 {ECO:0000303|PubMed:12106870};
GN   Synonyms=bm20 {ECO:0000312|EMBL:AAB08893.1};
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279;
RN   [1] {ECO:0000312|EMBL:AAB08893.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10569745; DOI=10.1128/iai.67.12.6329-6334.1999;
RA   Nirmalan N., Cordeiro N.J.V., Klager S.L., Bradley J.E., Allen J.E.;
RT   "Comparative analysis of glycosylated and nonglycosylated filarial
RT   homologues of the 20-kilodalton retinol binding protein from Onchocerca
RT   volvulus (Ov20).";
RL   Infect. Immun. 67:6329-6334(1999).
RN   [2] {ECO:0000305}
RP   LACK OF 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   [3] {ECO:0000305}
RP   RETINOL-BINDING AND FATTY ACID-BINDING.
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 acid 11-((5-
CC       dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid (DAUDA). The
CC       long chain fatty acid oleic acid can act competitively to displace
CC       bound DAUDA and retinol. {ECO:0000269|PubMed:12106870}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q25619}.
CC   -!- PTM: Not 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:12106870, ECO:0000305}.
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DR   EMBL; U69169; AAB08893.1; -; mRNA.
DR   AlphaFoldDB; Q93142; -.
DR   SMR; Q93142; -.
DR   STRING; 6279.Q93142; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS: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; Lipid-binding; Reference proteome; 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_0000008758"
FT   COILED          67..89
FT                   /evidence="ECO:0000255"
FT   COILED          130..153
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   178 AA;  20328 MW;  7402DDEAC3E20666 CRC64;
     MYHRLILLAL VGTTMANVIP FSMSNIPEEY KEFIPEEVRN FYKDLTVEDK EILRELASKH
     ATFANEDAAL EALKDKSDKL YKNAVELRNF VKAKIDSLKP DAKIFVDEII AKARSLRSDD
     GHKLDTEKIK QAARDIIAKY QALSEETKEE LKVTFPAIAK IIGNEKLKRN ASTFLQKN