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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
 
 
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