ID   11S2_SESIN              Reviewed;         459 AA.
AC   Q9XHP0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   28-JUN-2023, entry version 75.
DE   RecName: Full=11S globulin seed storage protein 2;
DE   AltName: Full=11S globulin Ses i 6 {ECO:0000303|PubMed:17517107};
DE   AltName: Full=11S globulin seed storage protein II;
DE   AltName: Full=Allergen Ses i 6 {ECO:0000303|PubMed:17556061};
DE   AltName: Full=Alpha-globulin;
DE   AltName: Allergen=Ses i 6.0101 {ECO:0000305};
DE   Contains:
DE     RecName: Full=11S globulin seed storage protein 2 acidic chain;
DE     AltName: Full=11S globulin seed storage protein II acidic chain;
DE   Contains:
DE     RecName: Full=11S globulin seed storage protein 2 basic chain;
DE     AltName: Full=11S globulin seed storage protein II basic chain;
DE   Flags: Precursor;
OS   Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX   NCBI_TaxID=4182;
RN   [1] {ECO:0000312|EMBL:AAD42944.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=cv. Tainan 1 {ECO:0000303|PubMed:10606554};
RC   TISSUE=Seed {ECO:0000269|PubMed:10606554};
RX   PubMed=10606554; DOI=10.1021/jf990366z;
RA   Tai S.S.K., Wu L.S.H., Chen E.C.F., Tzen J.T.C.;
RT   "Molecular cloning of 11S globulin and 2S albumin, the two major seed
RT   storage proteins in sesame.";
RL   J. Agric. Food Chem. 47:4932-4938(1999).
RN   [2]
RP   TISSUE SPECIFICITY, AND ALLERGEN.
RX   PubMed=17517107; DOI=10.1111/j.1365-2222.2007.02725.x;
RA   Wallowitz M.L., Chen R.J., Tzen J.T., Teuber S.S.;
RT   "Ses i 6, the sesame 11S globulin, can activate basophils and shows cross-
RT   reactivity with walnut in vitro.";
RL   Clin. Exp. Allergy 37:929-938(2007).
RN   [3]
RP   TISSUE SPECIFICITY, AND ALLERGEN.
RX   PubMed=17556061; DOI=10.1016/j.jaci.2007.03.041;
RA   Beyer K., Grishina G., Bardina L., Sampson H.A.;
RT   "Identification of 2 new sesame seed allergens: Ses i 6 and Ses i 7.";
RL   J. Allergy Clin. Immunol. 119:1554-1556(2007).
CC   -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:10606554,
CC       ECO:0000305|PubMed:17517107}.
CC   -!- SUBUNIT: Homohexamer (By similarity). Each subunit is composed of an
CC       acidic and a basic chain derived from a single precursor and linked by
CC       a disulfide bond (PubMed:10606554). {ECO:0000250|UniProtKB:A0A1L6K371,
CC       ECO:0000269|PubMed:10606554}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level)
CC       (PubMed:10606554, PubMed:17517107). Expressed in seeds
CC       (PubMed:17556061). {ECO:0000269|PubMed:10606554,
CC       ECO:0000269|PubMed:17517107, ECO:0000269|PubMed:17556061}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during seed maturation. Expressed in the
CC       maturing seeds 24 days after flowering. {ECO:0000269|PubMed:10606554}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC       patients allergic to sesame seeds (PubMed:17517107, PubMed:17556061).
CC       Recombinant protein binds to IgE in 58% of the 19 patients tested
CC       (PubMed:17517107). Recombinant protein binds strongly to IgE in 54% of
CC       the 24 patients tested (PubMed:17556061). Recombinant protein is able
CC       to activate basophils previously passively sensitized with sesame-
CC       allergic sera in 7 out of 11 patients (PubMed:17517107).
CC       {ECO:0000269|PubMed:17517107, ECO:0000269|PubMed:17556061}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000255}.
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DR   EMBL; AF091842; AAD42944.1; -; mRNA.
DR   RefSeq; NP_001291336.1; NM_001304407.1.
DR   AlphaFoldDB; Q9XHP0; -.
DR   SMR; Q9XHP0; -.
DR   Allergome; 2681; Ses i 6.
DR   Allergome; 3476; Ses i 6.0101.
DR   EnsemblPlants; SIN_1009682.t; SIN_1009682.t; SIN_1009682.
DR   GeneID; 105163414; -.
DR   Gramene; SIN_1009682.t; SIN_1009682.t; SIN_1009682.
DR   KEGG; sind:105163414; -.
DR   InParanoid; Q9XHP0; -.
DR   OrthoDB; 1219266at2759; -.
DR   PhylomeDB; Q9XHP0; -.
DR   Proteomes; UP000504604; Linkage group LG6.
DR   GO; GO:0042735; C:endosperm protein body; NAS:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; NAS:UniProtKB.
DR   GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
DR   CDD; cd02243; cupin_11S_legumin_C; 1.
DR   CDD; cd02242; cupin_11S_legumin_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR31189:SF54; CUPIN TYPE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Reference proteome; Seed storage protein; Signal;
KW   Storage protein.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..277
FT                   /note="11S globulin seed storage protein 2 acidic chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000043209"
FT   CHAIN           278..459
FT                   /note="11S globulin seed storage protein 2 basic chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000043210"
FT   DOMAIN          37..237
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          290..439
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          118..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        34..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        110..284
FT                   /note="Interchain (between acidic and basic chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P04405"
SQ   SEQUENCE   459 AA;  51830 MW;  E852F6C47B319200 CRC64;
     MVAFKFLLAL SLSLLVSAAI AQTREPRLTQ GQQCRFQRIS GAQPSLRIQS EGGTTELWDE
     RQEQFQCAGI VAMRSTIRPN GLSLPNYHPS PRLVYIERGQ GLISIMVPGC AETYQVHRSQ
     RTMERTEASE QQDRGSVRDL HQKVHRLRQG DIVAIPSGAA HWCYNDGSED LVAVSINDVN
     HLSNQLDQKF RAFYLAGGVP RSGEQEQQAR QTFHNIFRAF DAELLSEAFN VPQETIRRMQ
     SEEEERGLIV MARERMTFVR PDEEEGEQEH RGRQLDNGLE ETFCTMKFRT NVESRREADI
     FSRQAGRVHV VDRNKLPILK YMDLSAEKGN LYSNALVSPD WSMTGHTIVY VTRGDAQVQV
     VDHNGQALMN DRVNQGEMFV VPQYYTSTAR AGNNGFEWVA FKTTGSPMRS PLAGYTSVIR
     AMPLQVITNS YQISPNQAQA LKMNRGSQSF LLSPGGRRS
//