2SS_RICCO
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 25-MAY-2022, entry version 122.
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; 1466684at2759; -.
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; -; 2.
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; 2.
DR Pfam; PF00234; Tryp_alpha_amyl; 2.
DR PRINTS; PR00496; NAPIN.
DR SMART; SM00499; AAI; 2.
DR SUPFAM; SSF47699; SSF47699; 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
