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