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FAR1_ACAVI
ID   FAR1_ACAVI              Reviewed;         178 AA.
AC   Q8MZJ8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Fatty-acid and retinol-binding protein 1;
DE   AltName: Full=Av-FAR-1;
DE   AltName: Full=Av20;
DE   Flags: Precursor;
GN   Name=far-1 {ECO:0000312|EMBL:AAM28244.1};
OS   Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX   NCBI_TaxID=6277;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAM28244.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, 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).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-178.
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   [3] {ECO:0000305}
RP   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   [4] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL 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).
CC   -!- FUNCTION: Binds retinol and different fatty acids. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12106870,
CC       ECO:0000269|PubMed:9223154}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in larvae and adults.
CC       {ECO:0000269|PubMed:12106870, 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:0000250|UniProtKB:Q25619, ECO:0000305}.
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DR   EMBL; AY099071; AAM28244.1; -; mRNA.
DR   AlphaFoldDB; Q8MZJ8; -.
DR   SMR; Q8MZJ8; -.
DR   GO; GO:0005576; C:extracellular region; IDA: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_0000008757"
FT   COILED          67..89
FT                   /evidence="ECO:0000255"
FT   COILED          123..153
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        22
FT                   /note="S -> P (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="I -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46..50
FT                   /note="TQEDR -> SIFLC (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="F -> L (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  20518 MW;  C05AE2C939EFF06E CRC64;
     MYHQLILMAL IGVIMANVVP FSMSNIPEEY KEFIPEEVKN FYKNLTQEDR QILRELASKH
     ATFTNEDAAL EALKNKSDKL YQKAVELRNF VKAKIDSLKP DAKAFVDEII AKVRSLRPED
     GQKLDVEKLK QAARDIIAKY EALNEETKEE LKAPFPNTTK IITNEKFTRI ANSFLQKN
 
 
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