ID   2SS_RICCO               Reviewed;         258 AA.
AC   P01089; Q9S872; Q9S873; Q9S874;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=2S seed storage albumin protein {ECO:0000305};
DE   AltName: Full=2S albumin;
DE   AltName: Allergen=Ric c 1/3;
DE   Contains:
DE     RecName: Full=Allergen Ric c 3 small chain;
DE     AltName: Full=4.7 kDa napin-like protein small chain;
DE     AltName: Full=CB-1A small chain;
DE     AltName: Full=RS1A;
DE   Contains:
DE     RecName: Full=Allergen Ric c 3 large chain;
DE     AltName: Full=CB-1A large chain;
DE     AltName: Full=RL1;
DE   Contains:
DE     RecName: Full=Allergen Ric c 1 small chain;
DE     AltName: Full=2S albumin small chain;
DE     AltName: Full=4 kDa napin-like protein small chain;
DE     AltName: Full=RS2B;
DE   Contains:
DE     RecName: Full=Allergen Ric c 1 large chain;
DE     AltName: Full=2S albumin large chain;
DE     AltName: Full=7.3 kDa napin-like protein large chain;
DE     AltName: Full=RL2;
DE   Flags: Precursor;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEOLYTIC PROCESSING OF PRECURSOR,
RP   BLOCKAGE OF N-TERMINUS, VARIANT THR-74, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Endosperm;
RX   PubMed=2274038; DOI=10.1007/bf00633846;
RA   Irwin S.D., Keen J.N., Findlay J.B.C., Lord J.M.;
RT   "The Ricinus communis 2S albumin precursor: a single preproprotein may be
RT   processed into two different heterodimeric storage proteins.";
RL   Mol. Gen. Genet. 222:400-408(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Endosperm;
RX   PubMed=2216785; DOI=10.1093/nar/18.19.5890;
RA   Irwin S.D., Lord J.M.;
RT   "Nucleotide sequence of a Ricinus communis 2S albumin precursor gene.";
RL   Nucleic Acids Res. 18:5890-5890(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 157-190 AND 194-258, AND PYROGLUTAMATE FORMATION AT
RP   GLN-194.
RX   PubMed=7174664; DOI=10.1016/s0021-9258(18)33344-1;
RA   Sharief F.S., Li S.S.-L.;
RT   "Amino acid sequence of small and large subunits of seed storage protein
RT   from Ricinus communis.";
RL   J. Biol. Chem. 257:14753-14759(1982).
RN   [4]
RP   PROTEIN SEQUENCE OF 36-76; 157-190 AND 194-258, AND PHOSPHORYLATION AT
RP   SER-69.
RX   PubMed=8980648; DOI=10.1016/s0167-4838(96)00133-1;
RA   Neumann G.M., Condron R., Polya G.M.;
RT   "Purification and sequencing of napin-like protein small and large chains
RT   from Momordica charantia and Ricinus communis seeds and determination of
RT   sites phosphorylated by plant Ca(2+)-dependent protein kinase.";
RL   Biochim. Biophys. Acta 1298:223-240(1996).
RN   [5]
RP   PROTEIN SEQUENCE OF 36-72; 87-153; 157-190 AND 194-258, PYROGLUTAMATE
RP   FORMATION AT GLN-87 AND GLN-194, AND NOMENCLATURE.
RX   PubMed=9430499; DOI=10.1159/000023833;
RA   Bashir M.E., Hubatsch I., Leinenbach H.P., Zeppezauer M., Panzani R.C.,
RA   Hussein I.H.;
RT   "Ric c 1 and Ric c 3, the allergenic 2S albumin storage proteins of Ricinus
RT   communis: complete primary structures and phylogenetic relationships.";
RL   Int. Arch. Allergy Immunol. 115:73-82(1998).
RN   [6]
RP   SIMILARITY TO PROTEINASE INHIBITORS.
RX   PubMed=6615448; DOI=10.1042/bj2130543;
RA   Odani S., Koide T., Ono T., Ohnishi K.;
RT   "Structural relationship between barley (Hordeum vulgare) trypsin inhibitor
RT   and castor-bean (Ricinus communis) storage protein.";
RL   Biochem. J. 213:543-545(1983).
RN   [7]
RP   STRUCTURE BY NMR OF 36-156, AND DISULFIDE BONDS.
RX   PubMed=14636051; DOI=10.1021/bi0352217;
RA   Pantoja-Uceda D., Bruix M., Gimenez-Gallego G., Rico M., Santoro J.;
RT   "Solution structure of RicC3, a 2S albumin storage protein from Ricinus
RT   communis.";
RL   Biochemistry 42:13839-13847(2003).
CC   -!- FUNCTION: 2S seed storage proteins.
CC   -!- SUBUNIT: The 2 mature proteins consist of heterodimers of a small and a
CC       large chain; disulfide-linked. {ECO:0000269|PubMed:14636051}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in ripening seeds during testa formation
CC       and desiccation. {ECO:0000269|PubMed:2274038}.
CC   -!- PTM: The N-terminus of both large chains is blocked.
CC   -!- PTM: The C-terminus of the allergen Ric c 1 and allergen Ric c 3 small
CC       chains are heterogeneous and the length of the chains can vary from 33
CC       to 36 amino acids and from 36 to 40 amino acids respectively.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- BIOTECHNOLOGY: Ric C 3 constitutes the peptidic component of the
CC       immunomodulator Inmunoferon.
CC   -!- MISCELLANEOUS: The allergen Ric c 1 small chain acts as a calmodulin
CC       (CaM) antagonist that inhibits CaM-dependent myosin light chain kinase
CC       with IC(50)= 0.25 uM.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000305}.
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DR   EMBL; X54158; CAA38097.1; -; Genomic_DNA.
DR   PIR; S11499; RZCS.
DR   RefSeq; XP_002522854.1; XM_002522808.2.
DR   RefSeq; XP_002522855.1; XM_002522809.1.
DR   PDB; 1PSY; NMR; -; A=33-156.
DR   PDBsum; 1PSY; -.
DR   AlphaFoldDB; P01089; -.
DR   SMR; P01089; -.
DR   Allergome; 3467; Ric c 1.0101.
DR   Allergome; 614; Ric c 1.
DR   iPTMnet; P01089; -.
DR   GeneID; 8280732; -.
DR   GeneID; 8280733; -.
DR   KEGG; rcu:8280732; -.
DR   KEGG; rcu:8280733; -.
DR   eggNOG; ENOG502S7EV; Eukaryota.
DR   OrthoDB; 612121at2759; -.
DR   EvolutionaryTrace; P01089; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   CDD; cd00261; AAI_SS; 2.
DR   Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 2.
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; 2S SEED STORAGE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR35496:SF18; BIFUNCTIONAL INHIBITOR_PLANT LIPID TRANSFER PROTEIN_SEED STORAGE HELICAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 2.
DR   PRINTS; PR00496; NAPIN.
DR   SMART; SM00499; AAI; 2.
DR   SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Phosphoprotein;
KW   Pyrrolidone carboxylic acid; Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..35
FT                   /id="PRO_0000032162"
FT   CHAIN           36..76
FT                   /note="Allergen Ric c 3 small chain"
FT                   /id="PRO_0000041857"
FT   PROPEP          77..86
FT                   /evidence="ECO:0000269|PubMed:9430499"
FT                   /id="PRO_0000041858"
FT   CHAIN           87..153
FT                   /note="Allergen Ric c 3 large chain"
FT                   /id="PRO_0000041859"
FT   PROPEP          154..156
FT                   /id="PRO_0000041860"
FT   CHAIN           157..190
FT                   /note="Allergen Ric c 1 small chain"
FT                   /id="PRO_0000032163"
FT   PROPEP          191..193
FT                   /id="PRO_0000032164"
FT   CHAIN           194..258
FT                   /note="Allergen Ric c 1 large chain"
FT                   /id="PRO_0000032165"
FT   REGION          64..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8980648"
FT   MOD_RES         87
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:9430499"
FT   MOD_RES         194
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:7174664,
FT                   ECO:0000269|PubMed:9430499"
FT   DISULFID        49..108
FT                   /note="Interchain (between Ric c 3 small and Ric c 3 large
FT                   chains)"
FT                   /evidence="ECO:0000269|PubMed:14636051"
FT   DISULFID        61..97
FT                   /note="Interchain (between Ric c 3 small and Ric c 3 large
FT                   chains)"
FT                   /evidence="ECO:0000269|PubMed:14636051"
FT   DISULFID        98..145
FT                   /evidence="ECO:0000269|PubMed:14636051"
FT   DISULFID        110..149
FT                   /evidence="ECO:0000269|PubMed:14636051"
FT   DISULFID        162..212
FT                   /note="Interchain (between Ric c 1 small and Ric c 1 large
FT                   chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        175..201
FT                   /note="Interchain (between Ric c 1 small and Ric c 1 large
FT                   chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        202..249
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..256
FT                   /evidence="ECO:0000250"
FT   VARIANT         74
FT                   /note="P -> T"
FT                   /evidence="ECO:0000269|PubMed:2274038"
FT   CONFLICT        194
FT                   /note="Q -> E (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226..229
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="D -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   HELIX           49..53
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   HELIX           61..66
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   HELIX           108..123
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   HELIX           132..145
FT                   /evidence="ECO:0007829|PDB:1PSY"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:1PSY"
SQ   SEQUENCE   258 AA;  29290 MW;  27874CFC50E41072 CRC64;
     MAKLIPTIAL VSVLLFIIAN ASFAYRTTIT TIEIDESKGE REGSSSQQCR QEVQRKDLSS
     CERYLRQSSS RRSPGEEVLR MPGDENQQQE SQQLQQCCNQ VKQVRDECQC EAIKYIAEDQ
     IQQGQLHGEE SERVAQRAGE IVSSCGVRCM RQTRTNPSQQ GCRGQIQEQQ NLRQCQEYIK
     QQVSGQGPRR SDNQERSLRG CCDHLKQMQS QCRCEGLRQA IEQQQSQGQL QGQDVFEAFR
     TAANLPSMCG VSPTECRF
//