ARGR1_ARGRF
ID ARGR1_ARGRF Reviewed; 159 AA.
AC Q5GQ85;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Allergen Arg r 1;
DE AltName: Allergen=Arg r 1;
DE Flags: Precursor;
OS Argas reflexus (European pigeon tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Argasidae; Argas.
OX NCBI_TaxID=34604;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-30, LACK OF
RP GLYCOSYLATION, AND ALLERGEN.
RX PubMed=15753913; DOI=10.1016/j.jaci.2004.11.052;
RA Hilger C., Bessot J.-C., Hutt N., Grigioni F., de Blay F., Pauli G.,
RA Hentges F.;
RT "IgE-mediated anaphylaxis caused by bites of the pigeon tick Argas
RT reflexus: cloning and expression of the major allergen Arg r 1.";
RL J. Allergy Clin. Immunol. 115:617-622(2005).
RN [2]
RP PROTEIN SEQUENCE OF 17-31, AND SEQUENCE REVISION TO 18 AND 26.
RA Hilger C.;
RL Submitted (SEP-2008) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Not glycosylated.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. Major
CC allergen responsible for anaphylactic reactions.
CC {ECO:0000269|PubMed:15753913}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Histamine-binding
CC salivary protein family. {ECO:0000305}.
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DR EMBL; AJ697694; CAG26895.1; -; mRNA.
DR PDB; 2X45; X-ray; 1.40 A; A/B/C=17-159.
DR PDB; 2X46; X-ray; 1.00 A; A=17-159.
DR PDBsum; 2X45; -.
DR PDBsum; 2X46; -.
DR AlphaFoldDB; Q5GQ85; -.
DR SMR; Q5GQ85; -.
DR Allergome; 1150; Arg r 1.
DR Allergome; 3101; Arg r 1.0101.
DR EvolutionaryTrace; Q5GQ85; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043176; F:amine binding; IEA:InterPro.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002970; Tick_his-bd.
DR Pfam; PF02098; His_binding; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:15753913, ECO:0000269|Ref.2"
FT CHAIN 17..159
FT /note="Allergen Arg r 1"
FT /id="PRO_5000072608"
FT DISULFID 50..155
FT /evidence="ECO:0000250"
FT DISULFID 109..134
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="C -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2X45"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2X46"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:2X46"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2X46"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2X46"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:2X46"
SQ SEQUENCE 159 AA; 16965 MW; BCA1BD9C6F9CB77C CRC64;
MALIILLVAC LSVVSADDCS GKTDAWTSIK GPKTGGYWLK QTTKTGENEC TYVKGTDFKE
NTKTATYTYG YKDASGKLTK TTGTATAKGS DIVVGSDTST VIYTDGKTCD VVKHGGHTEL
WVHSSKTSGG YNNCCDKKFT ETRGSTPANE VYKKCPGMP