SAM22_SOYBN
ID SAM22_SOYBN Reviewed; 158 AA.
AC P26987; C6T1G1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Stress-induced protein SAM22 {ECO:0000303|PubMed:1371403};
DE AltName: Full=Pathogenesis-related protein 10 {ECO:0000303|PubMed:12417891};
DE AltName: Full=Starvation-associated message 22 {ECO:0000303|PubMed:1371403};
DE AltName: Allergen=Gly m 4 {ECO:0000305};
GN Name=PR-10 {ECO:0000303|PubMed:12417891};
GN ORFNames=GLYMA_07G243500 {ECO:0000312|EMBL:KRH50781.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Mandarin;
RX PubMed=1371403; DOI=10.1007/bf00040662;
RA Crowell D., John M.E., Russell D., Amasino R.M.;
RT "Characterization of a stress-induced, developmentally regulated gene
RT family from soybean.";
RL Plant Mol. Biol. 18:459-466(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Park S., Chen Z.-Y., Xie Y.-R., Schneider R.W.;
RT "Identification of proteins induced or suppressed during a susceptible
RT host-pathogen interaction between soybean and Phakopsora pachyrhizi.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [5]
RP ALLERGEN.
RX PubMed=12417891; DOI=10.1067/mai.2002.128946;
RA Kleine-Tebbe J., Vogel L., Crowell D.N., Haustein U.F., Vieths S.;
RT "Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v
RT 1- related PR-10 protein in soybean, SAM22.";
RL J. Allergy Clin. Immunol. 110:797-804(2002).
RN [6]
RP ALLERGEN.
RX PubMed=14713921; DOI=10.1016/j.jaci.2003.09.030;
RA Mittag D., Vieths S., Vogel L., Becker W.M., Rihs H.P., Helbling A.,
RA Wuthrich B., Ballmer-Weber B.K.;
RT "Soybean allergy in patients allergic to birch pollen: clinical
RT investigation and molecular characterization of allergens.";
RL J. Allergy Clin. Immunol. 113:148-154(2004).
RN [7]
RP STRUCTURE BY NMR OF 2-158.
RX PubMed=18834331; DOI=10.1042/bsr20080117;
RA Berkner H., Neudecker P., Mittag D., Ballmer-Weber B.K., Schweimer K.,
RA Vieths S., Rosch P.;
RT "Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member
RT of the Bet v 1 superfamily and closely resembles yellow lupine proteins.";
RL Biosci. Rep. 29:183-192(2009).
CC -!- FUNCTION: Involved in disease resistance.
CC {ECO:0000250|UniProtKB:E6YBW4}.
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls and leaves.
CC {ECO:0000269|PubMed:1371403}.
CC -!- INDUCTION: Induced by salicylate, methyl viologen, chitosan, hydrogen
CC peroxide and sodium phosphate. {ECO:0000269|PubMed:1371403}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12417891,
CC PubMed:14713921). Gly m 4 is the major soy allergen for patients
CC allergic to birch pollen with soy allergy (PubMed:12417891,
CC PubMed:14713921). Binds to IgE (PubMed:12417891, PubMed:14713921).
CC {ECO:0000269|PubMed:12417891, ECO:0000269|PubMed:14713921}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; X60043; CAA42646.1; -; mRNA.
DR EMBL; BT091267; ACU15400.1; -; mRNA.
DR EMBL; GU563345; ADR51747.1; -; Genomic_DNA.
DR EMBL; CM000840; KRH50781.1; -; Genomic_DNA.
DR PIR; S20518; S20518.
DR RefSeq; NP_001236038.1; NM_001249109.2.
DR RefSeq; NP_001238060.1; NM_001251131.1.
DR RefSeq; XP_006582821.1; XM_006582758.2.
DR PDB; 2K7H; NMR; -; A=2-158.
DR PDBsum; 2K7H; -.
DR AlphaFoldDB; P26987; -.
DR BMRB; P26987; -.
DR SMR; P26987; -.
DR STRING; 3847.GLYMA07G37240.1; -.
DR Allergome; 3297; Gly m 4.0101.
DR Allergome; 749; Gly m 4.
DR PRIDE; P26987; -.
DR ProMEX; P26987; -.
DR EnsemblPlants; KRH50781; KRH50781; GLYMA_07G243500.
DR GeneID; 100101844; -.
DR GeneID; 547915; -.
DR Gramene; KRH50781; KRH50781; GLYMA_07G243500.
DR KEGG; gmx:100101844; -.
DR KEGG; gmx:547915; -.
DR eggNOG; ENOG502RXTQ; Eukaryota.
DR InParanoid; P26987; -.
DR OMA; FVTHKID; -.
DR OrthoDB; 1381244at2759; -.
DR EvolutionaryTrace; P26987; -.
DR Proteomes; UP000008827; Chromosome 7.
DR Genevisible; P26987; GM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0010427; F:abscisic acid binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR024949; Bet_v_I_allergen.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR PRINTS; PR00634; BETALLERGEN.
DR SMART; SM01037; Bet_v_1; 1.
DR PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Pathogenesis-related protein; Plant defense;
KW Reference proteome.
FT CHAIN 1..158
FT /note="Stress-induced protein SAM22"
FT /id="PRO_0000154170"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:2K7H"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:2K7H"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:2K7H"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:2K7H"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2K7H"
FT HELIX 130..153
FT /evidence="ECO:0007829|PDB:2K7H"
SQ SEQUENCE 158 AA; 16772 MW; 9FA5167221DC929C CRC64;
MGVFTFEDEI NSPVAPATLY KALVTDADNV IPKALDSFKS VENVEGNGGP GTIKKITFLE
DGETKFVLHK IESIDEANLG YSYSVVGGAA LPDTAEKITF DSKLVAGPNG GSAGKLTVKY
ETKGDAEPNQ DELKTGKAKA DALFKAIEAY LLAHPDYN
