ANIS5_ANISI
ID ANIS5_ANISI Reviewed; 152 AA.
AC A1IKL2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=SXP/RAL-2 family protein Ani s 5 {ECO:0000303|PubMed:17180690, ECO:0000312|EMBL:BAF43534.1};
DE AltName: Allergen=Ani s 5 {ECO:0000303|PubMed:17180690};
DE Flags: Precursor;
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000312|EMBL:BAF43534.1};
RN [1] {ECO:0000312|EMBL:BAF43534.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Larva {ECO:0000303|PubMed:17180690};
RX PubMed=17180690; DOI=10.1007/s00436-006-0396-4;
RA Kobayashi Y., Ishizaki S., Shimakura K., Nagashima Y., Shiomi K.;
RT "Molecular cloning and expression of two new allergens from Anisakis
RT simplex.";
RL Parasitol. Res. 100:1233-1241(2007).
RN [2]
RP PROTEIN SEQUENCE OF 19-33, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=18618144; DOI=10.1007/s00436-008-1105-2;
RA Caballero M.L., Moneo I., Gomez-Aguado F., Corcuera M.T., Casado I.,
RA Rodriguez-Perez R.;
RT "Isolation of Ani s 5, an excretory-secretory and highly heat-resistant
RT allergen useful for the diagnosis of Anisakis larvae sensitization.";
RL Parasitol. Res. 103:1231-1233(2008).
RN [3] {ECO:0007744|PDB:2MAR}
RP STRUCTURE BY NMR OF 19-152, SUBUNIT, ALLERGEN, REGIONS, AND CIRCULAR
RP DICHROISM ANALYSIS.
RX PubMed=24603892; DOI=10.1371/journal.pntd.0002735;
RA Garcia-Mayoral M.F., Trevino M.A., Perez-Pinar T., Caballero M.L.,
RA Knaute T., Umpierrez A., Bruix M., Rodriguez-Perez R.;
RT "Relationships between IgE/IgG4 epitopes, structure and function in
RT Anisakis simplex Ani s 5, a member of the SXP/RAL-2 protein family.";
RL PLoS Negl. Trop. Dis. 8:E2735-E2735(2014).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Resistant to heat. {ECO:0000269|PubMed:18618144};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24603892}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18618144}.
CC -!- TISSUE SPECIFICITY: Excretory gland, ventriculus, and the luminal
CC epithelium of the intestine of the larvae.
CC {ECO:0000269|PubMed:18618144}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE and IgG4.
CC A.simplex is a fish parasite that, when accidentally ingested by
CC humans, may cause allergic reactions in sensitized individuals.
CC {ECO:0000269|PubMed:17180690, ECO:0000269|PubMed:18618144,
CC ECO:0000269|PubMed:24603892}.
CC -!- SIMILARITY: Belongs to the SXP/RAL-2 family.
CC {ECO:0000303|PubMed:17180690}.
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DR EMBL; AB274998; BAF43534.1; -; mRNA.
DR PDB; 2MAR; NMR; -; A=19-152.
DR PDBsum; 2MAR; -.
DR AlphaFoldDB; A1IKL2; -.
DR SMR; A1IKL2; -.
DR Allergome; 3765; Ani s 5.
DR Allergome; 3766; Ani s 5.0101.
DR Proteomes; UP000036680; Genome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0019864; F:IgG binding; IDA:UniProtKB.
DR InterPro; IPR003677; ANIS5_cation-bd.
DR Pfam; PF02520; DUF148; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; IgE-binding protein;
KW IgG-binding protein; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:18618144"
FT CHAIN 19..152
FT /note="SXP/RAL-2 family protein Ani s 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18618144"
FT /id="PRO_5002634876"
FT REGION 25..42
FT /note="Necessary for IgE-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT REGION 49..68
FT /note="IgG4-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT REGION 49..54
FT /note="Necessary for IgE-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT REGION 58..66
FT /note="Necessary for IgE-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT REGION 103..120
FT /note="Necessary for IgE-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT REGION 118..137
FT /note="IgG4-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT REGION 127..146
FT /note="IgE-binding and IgG4-binding"
FT /evidence="ECO:0000269|PubMed:24603892"
FT CONFLICT 21
FT /note="T -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:2MAR"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:2MAR"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2MAR"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2MAR"
FT HELIX 69..95
FT /evidence="ECO:0007829|PDB:2MAR"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:2MAR"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:2MAR"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:2MAR"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2MAR"
SQ SEQUENCE 152 AA; 16587 MW; 8A10EA6797EE6C82 CRC64;
MKTLIVAALF CTIGMALADD TPPPPPFLAG APQDVVKAFF ELLKKDETKT DPEIEKDLDA
WVDTLGGDYK AKFETFKKEM KAKEAELAKA HEEAVAKMTP EAKKADAELS KIAEDDSLNG
IQKAQKIQAI YKTLPQSVKD ELEKGIGPAV PQ
