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P01089 (2SS_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2S albumin
Alternative name(s):
Allergen=Ric c 1/3

Cleaved into the following 4 chains:

  1. Allergen Ric c 3 small chain
    Alternative name(s):
    4.7 kDa napin-like protein small chain
    CB-1A small chain
    RS1A
  2. Allergen Ric c 3 large chain
    Alternative name(s):
    CB-1A large chain
    RL1
  3. Allergen Ric c 1 small chain
    Alternative name(s):
    2S albumin small chain
    4 kDa napin-like protein small chain
    RS2B
  4. Allergen Ric c 1 large chain
    Alternative name(s):
    2S albumin large chain
    7.3 kDa napin-like protein large chain
    RL2
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

2S seed storage proteins.

Subunit structure

The 2 mature proteins consist of heterodimers of a small and a large chain; disulfide-linked. Ref.7

Developmental stage

Expressed in ripening seeds during testa formation and desiccation. Ref.1

Post-translational modification

The N-terminus of both large chains is blocked.

The C-terminus of the allergen Ric c 1 and allergen Ric c 3 small chains are heterogeneous and the length of the chains can vary from 33 to 36 amino acids and from 36 to 40 amino acids respectively.

Allergenic properties

Causes an allergic reaction in human.

Biotechnological use

Ric C 3 constitutes the peptidic component of the immunomodulator Inmunoferon.

Miscellaneous

The allergen Ric c 1 small chain acts as a calmodulin (CaM) antagonist that inhibits CaM-dependent myosin light chain kinase with IC50= 0.25 µM.

Sequence similarities

Belongs to the 2S seed storage albumins family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DiseaseAllergen
   DomainSignal
   Molecular functionSeed storage protein
Storage protein
   PTMCleavage on pair of basic residues
Disulfide bond
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular functionnutrient reservoir activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 3511
PRO_0000032162
Chain36 – 7641Allergen Ric c 3 small chain
PRO_0000041857
Propeptide77 – 8610
PRO_0000041858
Chain87 – 15367Allergen Ric c 3 large chain
PRO_0000041859
Propeptide154 – 1563
PRO_0000041860
Chain157 – 19034Allergen Ric c 1 small chain
PRO_0000032163
Propeptide191 – 1933
PRO_0000032164
Chain194 – 25865Allergen Ric c 1 large chain
PRO_0000032165

Amino acid modifications

Modified residue691Phosphoserine
Modified residue871Pyrrolidone carboxylic acid Probable
Modified residue1941Pyrrolidone carboxylic acid Ref.3
Disulfide bond49 ↔ 108Interchain (between Ric c 3 small and Ric c 3 large chains) Ref.7
Disulfide bond61 ↔ 97Interchain (between Ric c 3 small and Ric c 3 large chains) Ref.7
Disulfide bond98 ↔ 145 Ref.7
Disulfide bond110 ↔ 149 Ref.7
Disulfide bond162 ↔ 212Interchain (between Ric c 1 small and Ric c 1 large chains) By similarity
Disulfide bond175 ↔ 201Interchain (between Ric c 1 small and Ric c 1 large chains) By similarity
Disulfide bond202 ↔ 249 By similarity
Disulfide bond214 ↔ 256 By similarity

Natural variations

Natural variant741P → T. Ref.1

Experimental info

Sequence conflict1941Q → E AA sequence Ref.4
Sequence conflict2221E → Q AA sequence Ref.3
Sequence conflict226 – 2294Missing AA sequence Ref.3
Sequence conflict2341D → N AA sequence Ref.3
Sequence conflict2551E → Q AA sequence Ref.3

Secondary structure

1 ................... 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01089 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 27874CFC50E41072

FASTA25829,290
        10         20         30         40         50         60 
MAKLIPTIAL VSVLLFIIAN ASFAYRTTIT TIEIDESKGE REGSSSQQCR QEVQRKDLSS 

        70         80         90        100        110        120 
CERYLRQSSS RRSPGEEVLR MPGDENQQQE SQQLQQCCNQ VKQVRDECQC EAIKYIAEDQ 

       130        140        150        160        170        180 
IQQGQLHGEE SERVAQRAGE IVSSCGVRCM RQTRTNPSQQ GCRGQIQEQQ NLRQCQEYIK 

       190        200        210        220        230        240 
QQVSGQGPRR SDNQERSLRG CCDHLKQMQS QCRCEGLRQA IEQQQSQGQL QGQDVFEAFR 

       250 
TAANLPSMCG VSPTECRF

« Hide

References

[1]"The Ricinus communis 2S albumin precursor: a single preproprotein may be processed into two different heterodimeric storage proteins."
Irwin S.D., Keen J.N., Findlay J.B.C., Lord J.M.
Mol. Gen. Genet. 222:400-408(1990) [PubMed: 2274038] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEOLYTIC PROCESSING OF PRECURSOR, BLOCKAGE OF N-TERMINUS, VARIANT THR-74, DEVELOPMENTAL STAGE.
Tissue: Endosperm.
[2]"Nucleotide sequence of a Ricinus communis 2S albumin precursor gene."
Irwin S.D., Lord J.M.
Nucleic Acids Res. 18:5890-5890(1990) [PubMed: 2216785] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Endosperm.
[3]"Amino acid sequence of small and large subunits of seed storage protein from Ricinus communis."
Sharief F.S., Li S.S.-L.
J. Biol. Chem. 257:14753-14759(1982) [PubMed: 7174664] [Abstract]
Cited for: PROTEIN SEQUENCE OF 157-190 AND 194-258.
[4]"Purification and sequencing of napin-like protein small and large chains from Momordica charantia and Ricinus communis seeds and determination of sites phosphorylated by plant Ca(2+)-dependent protein kinase."
Neumann G.M., Condron R., Polya G.M.
Biochim. Biophys. Acta 1298:223-240(1996) [PubMed: 8980648] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-76; 157-190 AND 194-258, PHOSPHORYLATION.
[5]"Ric c 1 and Ric c 3, the allergenic 2S albumin storage proteins of Ricinus communis: complete primary structures and phylogenetic relationships."
Bashir M.E., Hubatsch I., Leinenbach H.P., Zeppezauer M., Panzani R.C., Hussein I.H.
Int. Arch. Allergy Immunol. 115:73-82(1998) [PubMed: 9430499] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-72; 87-153; 157-190 AND 194-258, BLOCKAGE OF N-TERMINUS, NOMENCLATURE.
[6]"Structural relationship between barley (Hordeum vulgare) trypsin inhibitor and castor-bean (Ricinus communis) storage protein."
Odani S., Koide T., Ono T., Ohnishi K.
Biochem. J. 213:543-545(1983) [PubMed: 6615448] [Abstract]
Cited for: SIMILARITY TO PROTEINASE INHIBITORS.
[7]"Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis."
Pantoja-Uceda D., Bruix M., Gimenez-Gallego G., Rico M., Santoro J.
Biochemistry 42:13839-13847(2003) [PubMed: 14636051] [Abstract]
Cited for: STRUCTURE BY NMR OF 36-156, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X54158 Genomic DNA. Translation: CAA38097.1.
PIRRZCS. S11499.
RefSeqXP_002522854.1. XM_002522808.1.
XP_002522855.1. XM_002522809.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSYNMR-A36-156[»]
ProteinModelPortalP01089.
SMRP01089. Positions 33-156.
ModBaseSearch...

Protein family/group databases

Allergome3467. Ric c 1.0101.
614. Ric c 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8280732.
8280733.
KEGGrcu:RCOM_0184110.
rcu:RCOM_0184120.

Phylogenomic databases

PhylomeDBP01089.
ProtClustDBCLSN2726124.

Family and domain databases

InterProIPR016140. Bifunc_inhib/LTP/seed_store.
IPR003612. LTP/seed_store/tryp_amyl_inhib.
IPR000617. Napin.
IPR013771. Trypsin/amylase_inhib.
[Graphical view]
Gene3DG3DSA:1.10.120.10. Trypsin/amylase_inhib. 2 hits.
PfamPF00234. Tryp_alpha_amyl. 2 hits.
[Graphical view]
PRINTSPR00496. NAPIN.
SMARTSM00499. AAI. 2 hits.
[Graphical view]
SUPFAMSSF47699. Bifunc_inhib/LTP/seed_store. 2 hits.
ProtoNetSearch...

Entry information

Entry name2SS_RICCO
AccessionPrimary (citable) accession number: P01089
Secondary accession number(s): Q9S872, Q9S873, Q9S874
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: December 14, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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