SCPA_PENVA
ID SCPA_PENVA Reviewed; 193 AA.
AC C7A639;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Sarcoplasmic calcium-binding protein, alpha chain {ECO:0000303|PubMed:19523674};
DE Short=SCP alpha chain {ECO:0000303|PubMed:19523674};
DE AltName: Full=Allergen Lit v 4 {ECO:0000303|PubMed:20471069, ECO:0000303|PubMed:22192087};
DE AltName: Allergen=Lit v 4.0101 {ECO:0000303|PubMed:19523674};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000312|EMBL:ACM89179.1};
RN [1] {ECO:0000312|EMBL:ACM89179.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND ALLERGEN.
RX PubMed=19523674; DOI=10.1016/j.jaci.2009.04.016;
RA Ayuso R., Grishina G., Ibanez M.D., Blanco C., Carrillo T.,
RA Bencharitiwong R., Sanchez S., Nowak-Wegrzyn A., Sampson H.A.;
RT "Sarcoplasmic calcium-binding protein is an EF-hand-type protein identified
RT as a new shrimp allergen.";
RL J. Allergy Clin. Immunol. 124:114-120(2009).
RN [2]
RP ALLERGEN, AND REGIONS.
RX PubMed=20471069; DOI=10.1016/j.jaci.2010.03.010;
RA Ayuso R., Sanchez-Garcia S., Lin J., Fu Z., Ibanez M.D., Carrillo T.,
RA Blanco C., Goldis M., Bardina L., Sastre J., Sampson H.A.;
RT "Greater epitope recognition of shrimp allergens by children than by adults
RT suggests that shrimp sensitization decreases with age.";
RL J. Allergy Clin. Immunol. 125:1286-1293(2010).
RN [3]
RP ALLERGEN, AND REGIONS.
RX PubMed=22192087; DOI=10.1111/j.1365-2222.2011.03920.x;
RA Ayuso R., Sanchez-Garcia S., Pascal M., Lin J., Grishina G., Fu Z.,
RA Ibanez M.D., Sastre J., Sampson H.A.;
RT "Is epitope recognition of shrimp allergens useful to predict clinical
RT reactivity?";
RL Clin. Exp. Allergy 42:293-304(2012).
CC -!- FUNCTION: Like parvalbumins, SCPs seem to be more abundant in fast
CC contracting muscles, but no functional relationship can be established
CC from this distribution. {ECO:0000305}.
CC -!- SUBUNIT: SCPs from crayfish, lobster, and shrimp are polymorphic
CC dimers; three isotypes (alpha-alpha, alpha-beta, and beta-beta) have
CC been identified. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in tail muscle (at protein level).
CC {ECO:0000269|PubMed:19523674}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to shrimp (PubMed:19523674, PubMed:20471069,
CC PubMed:22192087). Natural boiled protein binds to IgE in 59.6% of the
CC 52 shrimp-allergic patients tested. Recombinant protein binds to IgE in
CC 64.5% of the 31 patients tested allergic to the natural protein. 85% of
CC the patients binding the recombinant protein are children
CC (PubMed:19523674). Epitope diversity and the frequency and intensity of
CC IgE-binding is significantly more pronounced in children than in adults
CC (PubMed:20471069). Patients (children or adults) with positive double-
CC blind placebo-controlled food challenge (DBPCFC) to shrimp have a more
CC frequent, intense and diverse recognition of the epitopes of this
CC protein than those with negative challenge (PubMed:22192087).
CC Recombinant protein activates rat basophilic leukemia (RBL) cells
CC expressing human immunoglobulin epsilon Fc receptor type 1 and releases
CC beta-hexosaminidase from the cells (PubMed:19523674).
CC {ECO:0000269|PubMed:19523674, ECO:0000269|PubMed:20471069,
CC ECO:0000269|PubMed:22192087}.
CC -!- MISCELLANEOUS: The sarcoplasmic calcium-binding proteins are abundant
CC in the muscle of arthropods, mollusks, annelids, and protochordates.
CC {ECO:0000305}.
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DR EMBL; FJ184279; ACM89179.1; -; mRNA.
DR SMR; C7A639; -.
DR Allergome; 6092; Lit v 4.
DR Allergome; 6093; Lit v 4.0101.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Allergen; Calcium; Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..193
FT /note="Sarcoplasmic calcium-binding protein, alpha chain"
FT /id="PRO_0000456252"
FT DOMAIN 16..40
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 57..92
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 101..136
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 10..36
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 49..72
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 130..147
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000255|PROSITE-ProRule:PRU10142"
SQ SEQUENCE 193 AA; 22078 MW; FEF9929F15966EB9 CRC64;
MAYSWDNRVK YVVRYMYDID NNGFLDKNDF ECLAVRNTLI EGRGEFSADA YANNQKIMRN
LWNEIAELAD FNKDGEVTVD EFKQAVQKHC QGKKYGDFPG AFKVFIANQF KAIDVNGDGK
VGLDEYRLDC ITRSAFAEVK EIDDAYNKLT TEDDRKAGGL TLERYQDLYA QFISNPDESC
SACYLFGPLK VVQ
