SCP_SCYPA
ID SCP_SCYPA Reviewed; 193 AA.
AC I2DDG2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Sarcoplasmic calcium-binding protein {ECO:0000303|PubMed:28692255, ECO:0000303|PubMed:30187588, ECO:0000312|EMBL:AFJ80778.1};
DE Short=SCP {ECO:0000303|PubMed:28692255, ECO:0000303|PubMed:30187588};
DE AltName: Allergen=Scy p 4.0101 {ECO:0000305};
OS Scylla paramamosain (Mud crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Portunidae; Scylla.
OX NCBI_TaxID=85552 {ECO:0000312|EMBL:AFJ80778.1};
RN [1] {ECO:0000312|EMBL:AFJ80778.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP 3D-STRUCTURE MODELING, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE
RP SPECIFICITY, ALLERGEN, BIOTECHNOLOGY, AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:28692255};
RX PubMed=28692255; DOI=10.1021/acs.jafc.7b02381;
RA Hu M.J., Liu G.Y., Yang Y., Pan T.M., Liu Y.X., Sun L.C., Cao M.J.,
RA Liu G.M.;
RT "Cloning, Expression, and the Effects of Processing on Sarcoplasmic-
RT Calcium-Binding Protein: An Important Allergen in Mud Crab.";
RL J. Agric. Food Chem. 65:6247-6257(2017).
RN [2]
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=30187588; DOI=10.1111/cea.13266;
RA Yang Y., Hu M.J., Jin T.C., Zhang Y.X., Liu G.Y., Li Y.B., Zhang M.L.,
RA Cao M.J., Su W.J., Liu G.M.;
RT "A comprehensive analysis of the allergenicity and IgE epitopes of
RT myosinogen allergens in Scylla paramamosain.";
RL Clin. Exp. Allergy 49:108-119(2019).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Relatively stable at broad pH range (pH 1-11). Dimers are formed in
CC strongly acidic (pH 2-5) and alkaline (pH 10-11) conditions.
CC {ECO:0000269|PubMed:28692255};
CC Temperature dependence:
CC Stable at wide temperature range (4-100 degrees Celsius). Heating
CC does not cause degradation, but leads to polymerization. The polymer
CC content is highest at around 70 degrees Celsius.
CC {ECO:0000269|PubMed:28692255};
CC -!- SUBUNIT: Monomer and dimer. {ECO:0000269|PubMed:28692255}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:28692255, ECO:0000269|PubMed:30187588}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to crabs (PubMed:28692255, PubMed:30187588). Binds to
CC IgE in 17% of 30 crab-allergic patients tested (PubMed:30187588). Binds
CC to IgE in 100% of 22 patients tested allergic to crustaceans (crabs
CC and/or shrimps) (PubMed:28692255). Activates basophils
CC (PubMed:30187588). {ECO:0000269|PubMed:28692255,
CC ECO:0000269|PubMed:30187588}.
CC -!- BIOTECHNOLOGY: The Maillard reaction (glycation) and enzymatic cross-
CC linking reaction are effective methods to reduce allergenicity for the
CC industrial production of hypoallergenic crab meat.
CC {ECO:0000269|PubMed:28692255}.
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; JQ860424; AFJ80778.1; -; mRNA.
DR AlphaFoldDB; I2DDG2; -.
DR SMR; I2DDG2; -.
DR Allergome; 10174; Scy p 4.
DR Allergome; 12150; Scy p 4.0101.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
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"
FT /id="PRO_0000447339"
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 BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04571"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04571"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04571"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04571"
SQ SEQUENCE 193 AA; 21943 MW; F0FA28D696B7DF8F CRC64;
MAYSWDNRVK YVVRYMYDID NNGYLDKNDF ECLALRNTLI EGRGEFNSDA YANNQKIMSN
LWNEIAELAD FNKDGQVTVD EFKQAVQNLC CGKSFDGFPP CFKTVIGRLF KTIDINGDGL
AGVDEYRLDC ISRSAFSSVK EIDDAYAKLC TDDDKKAGGI SLNRYQELYA QFISNPDEKC
NAVYLFGPLK EVQ
