ALL1_SINAL
ID ALL1_SINAL Reviewed; 145 AA.
AC P15322; Q41196; Q41277; Q41278; Q41279; Q41280; Q41281;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Allergen Sin a 1;
DE AltName: Full=Allergen Sin a I;
DE AltName: Allergen=Sin a 1;
DE Contains:
DE RecName: Full=Allergen Sin a 1 small chain;
DE Contains:
DE RecName: Full=Allergen Sin a 1 large chain;
DE Flags: Precursor;
OS Sinapis alba (White mustard) (Brassica hirta).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX NCBI_TaxID=3728;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-36; LEU-40; ALA-41;
RP TYR-43; GLY-44; GLU-100 AND GLN-111.
RX PubMed=8093997; DOI=10.1006/bbrc.1993.1097;
RA Gonzalez de la Pena M.A., Villalba M., Garcia-Lopez J.L., Rodriguez R.;
RT "Cloning and expression of the major allergen from yellow mustard seeds,
RT Sin a I.";
RL Biochem. Biophys. Res. Commun. 190:648-653(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-6; 43-GLU-GLY-44;
RP LYS-61; GLU-100; 108-GLN-VAL-109; GLN-111; ARG-125; PRO-130 AND GLN-138.
RC TISSUE=Seed;
RX PubMed=8647131; DOI=10.1111/j.1432-1033.1996.0827p.x;
RA Gonzalez de la Peya M.A., Monsalve R.I., Batanero E., Villalba M.,
RA Rodriguez R.;
RT "Expression in Escherichia coli of the major allergen from mustard, Sin a
RT 1.";
RL Eur. J. Biochem. 237:827-832(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-39 AND 55-145, AND VARIANTS GLY-6; GLU-100 AND
RP PRO-130.
RC TISSUE=Seed;
RX PubMed=3181153; DOI=10.1111/j.1432-1033.1988.tb14357.x;
RA Menendez-Arias L., Moneo I., Dominguez J., Rodriguez R.;
RT "Primary structure of the major allergen of yellow mustard (Sinapis alba
RT L.) seed, Sin a I.";
RL Eur. J. Biochem. 177:159-166(1988).
CC -!- FUNCTION: This is a 2S seed storage protein.
CC -!- SUBUNIT: The protein consists of two chains linked by disulfide bonds.
CC -!- POLYMORPHISM: There seems to be at least 8 variants: 1.0101
CC (PubMed:3181153), 1.0102/SA2S1 (PubMed:8093997), 1.0103/SA2S2
CC (PubMed:8093997), 1.0104/SIN1 (PubMed:8647131), 1.0105/SIN2
CC (PubMed:8647131), 1.0106/SIN3 (PubMed:8647131), 1.0107/SIN4
CC (PubMed:8647131), and 1.0108/SIN5 (PubMed:8647131).
CC {ECO:0000269|PubMed:3181153, ECO:0000269|PubMed:8093997,
CC ECO:0000269|PubMed:8647131}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Causes cabbage allergy.
CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC {ECO:0000305}.
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DR EMBL; S54101; AAB25214.2; -; Genomic_DNA.
DR EMBL; X91798; CAA62908.1; -; Genomic_DNA.
DR EMBL; X91799; CAA62909.1; -; Genomic_DNA.
DR EMBL; X91800; CAA62910.1; -; Genomic_DNA.
DR EMBL; X91801; CAA62911.1; -; Genomic_DNA.
DR EMBL; X91802; CAA62912.1; -; Genomic_DNA.
DR PIR; PC1246; PC1246.
DR PIR; PC1247; PC1247.
DR PIR; S01791; S01791.
DR PIR; S65447; S65447.
DR PIR; S65478; S65478.
DR PIR; S65479; S65479.
DR PIR; S65480; S65480.
DR PIR; S65481; S65481.
DR PIR; S65482; S65482.
DR AlphaFoldDB; P15322; -.
DR Allergome; 3477; Sin a 1.0101.
DR Allergome; 627; Sin a 1.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000617; Napin/2SS/CON.
DR PANTHER; PTHR35496; PTHR35496; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00496; NAPIN.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Seed storage protein;
KW Storage protein.
FT CHAIN 1..39
FT /note="Allergen Sin a 1 small chain"
FT /id="PRO_0000032167"
FT PROPEP 40..54
FT /evidence="ECO:0000269|PubMed:3181153"
FT /id="PRO_0000032168"
FT CHAIN 55..145
FT /note="Allergen Sin a 1 large chain"
FT /id="PRO_0000032169"
FT REGION 34..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 6
FT /note="R -> G (in 1.0101, 1.0104/SIN1, 1.0106/SIN3 and
FT 1.0108/SIN5)"
FT /evidence="ECO:0000269|PubMed:3181153,
FT ECO:0000269|PubMed:8647131"
FT VARIANT 36
FT /note="S -> G (in 1.0103/SA2S2)"
FT /evidence="ECO:0000269|PubMed:8093997"
FT VARIANT 40
FT /note="W -> L (in 1.0103/SA2S2)"
FT /evidence="ECO:0000269|PubMed:8093997"
FT VARIANT 41
FT /note="T -> A (in 1.0103/SA2S2)"
FT /evidence="ECO:0000269|PubMed:8093997"
FT VARIANT 43
FT /note="D -> E (in 1.0105/SIN2)"
FT VARIANT 43
FT /note="D -> Y (in 1.0103/SA2S2)"
FT /evidence="ECO:0000269|PubMed:8093997"
FT VARIANT 44
FT /note="D -> G (in 1.0103/SA2S2 and 1.0105/SIN2)"
FT /evidence="ECO:0000269|PubMed:8093997"
FT VARIANT 61
FT /note="R -> K (in 1.0108/SIN5)"
FT /evidence="ECO:0000269|PubMed:8647131"
FT VARIANT 100
FT /note="G -> E (in 1.0101, 1.0103/SA2S2, 1.0104/SIN1,
FT 1.0105/SIN2 and 1.0107/SIN4)"
FT /evidence="ECO:0000269|PubMed:3181153,
FT ECO:0000269|PubMed:8093997, ECO:0000269|PubMed:8647131"
FT VARIANT 108
FT /note="H -> Q (in 1.0106/SIN3 and 1.0108/SIN5)"
FT VARIANT 109
FT /note="L -> V (in 1.0106/SIN3 and 1.0108/SIN5)"
FT VARIANT 111
FT /note="H -> Q (in 1.0103/SA2S2)"
FT /evidence="ECO:0000269|PubMed:8093997,
FT ECO:0000269|PubMed:8647131"
FT VARIANT 125
FT /note="K -> R (in 1.0104/SIN1)"
FT /evidence="ECO:0000269|PubMed:8647131"
FT VARIANT 130
FT /note="R -> P (in 1.0101, 1.0105/SIN2, 1.0106/SIN3, 1.0107/
FT SIN4 and 1.0108/SIN5)"
FT /evidence="ECO:0000269|PubMed:3181153,
FT ECO:0000269|PubMed:8647131"
FT VARIANT 138
FT /note="K -> Q (in 1.0104/SIN1)"
FT /evidence="ECO:0000269|PubMed:8647131"
FT CONFLICT 108..110
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 16449 MW; F8EE8E5CC2C2DDA7 CRC64;
PAGPFRIPKC RKEFQQAQHL RACQQWLHKQ AMQSGSGPSW TLDDEFDFED DMENPQGPQQ
RPPLLQQCCN ELHQEEPLCV CPTLKGASKA VKQQVRQQLG QQGQQGPHLQ HVISRIYQTA
THLPKVCNIR QVSVCPFKKT MPGPS