MLR_PENVA
ID MLR_PENVA Reviewed; 177 AA.
AC B7SNI3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Myosin regulatory light chain 2 {ECO:0000305};
DE Short=MLC-2 {ECO:0000305};
DE AltName: Full=Allergen Lit v 3 {ECO:0000303|PubMed:18760458, ECO:0000303|PubMed:20471069, ECO:0000303|PubMed:22192087};
DE AltName: Full=Myosin light chain {ECO:0000303|PubMed:18760458, ECO:0000303|PubMed:20471069, ECO:0000303|PubMed:22192087};
DE Short=MLC {ECO:0000303|PubMed:18760458, ECO:0000303|PubMed:20471069, ECO:0000303|PubMed:22192087};
DE AltName: Allergen=Lit v 3.0101 {ECO:0000303|PubMed:18760458};
GN ORFNames=C7M84_013542 {ECO:0000312|EMBL:ROT68323.1};
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:ACC76803.1};
RN [1] {ECO:0000312|EMBL:ACC76803.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-30 AND 95-110, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX PubMed=18760458; DOI=10.1016/j.jaci.2008.07.023;
RA Ayuso R., Grishina G., Bardina L., Carrillo T., Blanco C., Ibanez M.D.,
RA Sampson H.A., Beyer K.;
RT "Myosin light chain is a novel shrimp allergen, Lit v 3.";
RL J. Allergy Clin. Immunol. 122:795-802(2008).
RN [2] {ECO:0000312|EMBL:ROT68323.1, ECO:0000312|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000312|EMBL:ROT68323.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in tail muscle (at protein level).
CC {ECO:0000269|PubMed:18760458}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to shrimp (PubMed:18760458, PubMed:20471069,
CC PubMed:22192087). Natural boiled protein binds to IgE in 55% of the 38
CC shrimp-allergic patients tested. Recombinant protein binds to IgE in
CC 89% of the 19 patients tested allergic to the natural protein
CC (PubMed:18760458). 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 {ECO:0000269|PubMed:18760458, ECO:0000269|PubMed:20471069,
CC ECO:0000269|PubMed:22192087}.
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DR EMBL; EU449515; ACC76803.1; -; mRNA.
DR EMBL; QCYY01002691; ROT68323.1; -; Genomic_DNA.
DR SMR; B7SNI3; -.
DR STRING; 6689.B7SNI3; -.
DR Allergome; 4052; Lit v 3.
DR Allergome; 4053; Lit v 3.0101.
DR Proteomes; UP000283509; Unassembled WGS sequence.
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 SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Allergen; Calcium; Direct protein sequencing; Metal-binding; Motor protein;
KW Muscle protein; Myosin; Reference proteome; Repeat.
FT CHAIN 1..177
FT /note="Myosin regulatory light chain 2"
FT /id="PRO_0000456251"
FT DOMAIN 30..65
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 135..170
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 13..30
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 22..48
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 49..66
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 58..90
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 79..99
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT REGION 118..141
FT /note="IgE-binding epitope"
FT /evidence="ECO:0000269|PubMed:20471069,
FT ECO:0000269|PubMed:22192087"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 18
FT /note="G -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="R -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..96
FT /note="QT -> SS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..110
FT /note="KAFL -> ASIR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 177 AA; 19269 MW; 33EC8281C4559779 CRC64;
MSRKSGSRSS SKRSKKSGGG SNVFDMFTQR QVAEFKEGFQ LMDRDKDGVI GKTDLRGTFD
EIGRIATDQE LDEMLADAPA PINFTMLLNM FAERQTGESD DDDVVAKAFL AFADEEGNID
CDTFRHALMT WGDKFSSQEA DDALDQMDID DGGKIDVQGV IQMLTAGGGD DAAAEEA
