ABA1_ASCSU
ID ABA1_ASCSU Reviewed; 1365 AA.
AC Q06811; O61566; Q9TWU7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Polyprotein ABA-1;
DE AltName: Full=Body fluid allergen 1;
DE AltName: Full=Nematode polyprotein allergen ABA-1;
DE Short=NPA ABA-1;
DE AltName: Allergen=Asc s 1;
DE Contains:
DE RecName: Full=ABA-1B1 repeat unit;
DE Contains:
DE RecName: Full=ABA-1A4 repeat unit;
DE Contains:
DE RecName: Full=ABA-1A3 repeat unit;
DE Contains:
DE RecName: Full=ABA-1A2 repeat unit;
DE Contains:
DE RecName: Full=ABA-1A1 repeat unit;
DE Contains:
DE RecName: Full=C-terminal extension peptide;
DE Flags: Precursor; Fragment;
GN Name=ABA-1;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1095.
RX PubMed=10229690; DOI=10.1042/bj3400337;
RA Moore J., McDermott L., Price N.C., Kelly S.M., Cooper A., Kennedy M.W.;
RT "Sequence-divergent units of the ABA-1 polyprotein array of the nematode
RT Ascaris suum have similar fatty-acid- and retinol-binding properties but
RT different binding-site environments.";
RL Biochem. J. 340:337-343(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 971-1365.
RC TISSUE=Larva;
RX PubMed=8433722; DOI=10.1016/0166-6851(93)90210-o;
RA Spence H.J., Moore J., Brass A., Kennedy M.W.;
RT "A cDNA encoding repeating units of the ABA-1 allergen of Ascaris.";
RL Mol. Biochem. Parasitol. 57:339-343(1993).
RN [3]
RP PROTEIN SEQUENCE OF 1066-1133.
RX PubMed=7682160; DOI=10.1111/j.1365-2249.1993.tb05958.x;
RA Christie J.F., Dunbar B., Kennedy M.W.;
RT "The ABA-1 allergen of the nematode Ascaris suum: epitope stability, mass
RT spectrometry, and N-terminal sequence comparison with its homologue in
RT Toxocara canis.";
RL Clin. Exp. Immunol. 92:125-132(1993).
RN [4]
RP PROTEIN SEQUENCE OF 1066-1106.
RX PubMed=2335378;
RA Christie J.F., Dunbar B., Davidson I., Kennedy M.W.;
RT "N-terminal amino acid sequence identity between a major allergen of
RT Ascaris lumbricoides and Ascaris suum, and MHC-restricted IgE responses to
RT it.";
RL Immunology 69:596-602(1990).
RN [5]
RP PROTEIN SEQUENCE OF 1066-1075.
RX PubMed=1690856; DOI=10.1016/0166-6851(90)90055-q;
RA McGibbon A.M., Christie J.F., Kennedy M.W., Lee T.D.;
RT "Identification of the major Ascaris allergen and its purification to
RT homogeneity by high-performance liquid chromatography.";
RL Mol. Biochem. Parasitol. 39:163-171(1990).
RN [6]
RP CHARACTERIZATION.
RX PubMed=7756301; DOI=10.1021/bi00020a015;
RA Kennedy M.W., Brasss A., McCruden A.B., Price N.C., Kelly S.M., Cooper A.;
RT "The ABA-1 allergen of the parasitic nematode Ascaris suum: fatty acid and
RT retinoid binding function and structural characterization.";
RL Biochemistry 34:6700-6710(1995).
CC -!- FUNCTION: Has high binding affinity for fatty acids and retinoids.
CC -!- TISSUE SPECIFICITY: Pseudocoelomic fluid.
CC -!- PTM: Nematode polyprotein allergens (NPAs) are synthesized as large
CC polypeptides that are subsequently proteolytically cleaved to active
CC polypeptide units.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the NPA family. {ECO:0000305}.
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DR EMBL; AF051702; AAC06015.1; -; mRNA.
DR EMBL; L03211; AAB41117.1; -; mRNA.
DR PIR; A48576; A48576.
DR PIR; T31423; T31423.
DR PDB; 2XV9; NMR; -; A=534-662.
DR PDBsum; 2XV9; -.
DR AlphaFoldDB; Q06811; -.
DR SMR; Q06811; -.
DR Allergome; 3541; Asc s 1.0101.
DR Allergome; 61; Asc s 1.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.533.30; -; 10.
DR InterPro; IPR032487; ABA-1_nematode.
DR InterPro; IPR038289; DVA-1_sf.
DR Pfam; PF16469; NPA; 10.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Cleavage on pair of basic residues;
KW Direct protein sequencing; Lipid-binding; Repeat; Retinol-binding.
FT CHAIN <1..1365
FT /note="Polyprotein ABA-1"
FT /id="PRO_0000287126"
FT PEPTIDE <1..133
FT /note="ABA-1B1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042221"
FT PEPTIDE 134..266
FT /note="ABA-1A4 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042222"
FT PEPTIDE 267..399
FT /note="ABA-1A3 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042223"
FT PEPTIDE 400..533
FT /note="ABA-1A2 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042224"
FT PEPTIDE 534..666
FT /note="ABA-1A1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042225"
FT PEPTIDE 667..799
FT /note="ABA-1A1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042226"
FT PEPTIDE 800..932
FT /note="ABA-1A1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042227"
FT PEPTIDE 933..1065
FT /note="ABA-1A1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042228"
FT PEPTIDE 1066..1198
FT /note="ABA-1A1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000020606"
FT PEPTIDE 1199..1331
FT /note="ABA-1A1 repeat unit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000020607"
FT PEPTIDE 1332..1365
FT /note="C-terminal extension peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020608"
FT NON_TER 1
FT STRAND 1199..1201
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:2XV9"
FT TURN 1207..1213
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1216..1227
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1232..1244
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1248..1269
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1271..1284
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1288..1298
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1305..1313
FT /evidence="ECO:0007829|PDB:2XV9"
FT HELIX 1315..1321
FT /evidence="ECO:0007829|PDB:2XV9"
SQ SEQUENCE 1365 AA; 156880 MW; F7F43B78606863DD CRC64;
TMEHYLKTYL SWLTEEQKEK LKEMKEAGKT KAEIQHEVMH YYDQLHGEEK QQATEKLKVG
CKMLLKGIIG EEKVVELRNM KEAGADIQEL QQKVEKMLSE VTDEKQKEKV HEYGPACKKI
FGATTLQHHR RRRHHFTLES SLDTHLKWLS QEQKDELLKM KKDGKTKKEL EAKILHYYDE
LEGDAKKEAT EHLKGGCGEI LKHVVGEEKA AELKNLKDSG ASKEELKAKV EEALHAVTDE
EKKQYIADFG PACKKIYGVH TSRRRRHHFT LESSLDTHLK WLSQEQKDEL LKMKKDGKAK
KELEAKILHY YDELEGDAKK EATEHLKGGC AEILKHVVGE EKAAELKNLK DSGASKEELK
AKVEEALHAV TDEEKKQYIA DFGPACKKIY GVHTSRRRRH HFTLESSLDT HLKWLSQEQK
DELLKMKKDG KTKKDLQAKI LHYYDELEGD AKKEATEHLK DGCREILKHV VGEEKEAELK
KLKDSGASKE EVKAKVEEAL HAVTDEEKKQ YIADFGPACK KIFGAAHTSR RRRHHFTLES
SLDTHLKWLS QEQKDELLKM KKDGKAKKEL EAKILHYYDE LEGDAKKEAT EHLKGGCREI
LKHVVGEEKA AELKNLKDSG ASKEELKAKV EEALHAVTDE EKKQYIADFG PACKKIYGVH
TSRRRRHHFT LESSLDTHLK WLSQEQKDEL LKMKKDGKAK KELEAKILHY YDELEGDAKK
EATEHLKGGC REILKHVVGE EKAAELKNLK DSGASKEELK AKVEEALHAV TDEEKKQYIA
DFGPACKKIY GVHTSRRRRH HFTLESSLDT HLKWLSQEQK DELLKMKKDG KAKKELEAKI
LHYYDELEGD AKKEATEHLK GGCREILKHV VGEEKAAELK NLKDSGASKE ELKAKVEEAL
HAVTDEEKKQ YIADFGPACK KIYGVHTSRR RRHHFTLESS LDTHLKWLSQ EQKDELLKMK
KDGKAKKELE AKILHYYDEL EGDAKKEATE HLKGGCREIL KHVVGEEKAA ELKNLKDSGA
SKEELKAKVE EALHAVTDEE KKQYIADFGP ACKKIYGVHT SRRRRHHFTL ESSLDTHLKW
LSQEQKDELL KMKKDGKAKK ELEAKILHYY DELEGDAKKE ATEHLKGGCR EILKHVVGEE
KAAELKNLKD SGASKEELKA KVEEALHAVT DEEKKQYIAD FGPACKKIYG VHTSRRRRHH
FTLESSLDTH LKWLSQEQKD ELLKMKKDGK AKKELEAKIL HYYDELEGDA KKEATEHLKG
GCREILKHVV GEEKAAELKN LKDSGASKEE LKAKVEEALH AVTDEEKKQY IADFGPACKK
IYGVHTSRRR RYHAEDGTDD IDGLAQSRQR RSGFFEKLID VFAFF
