Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2S albumin

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

2S seed storage proteins.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Seed storage protein, Storage protein

Names & Taxonomyi

Protein namesi
Recommended name:
2S albumin
Alternative name(s):
Allergen: Ric c 1/3
Cleaved into the following 4 chains:
Alternative name(s):
4.7 kDa napin-like protein small chain
CB-1A small chain
RS1A
Alternative name(s):
CB-1A large chain
RL1
Alternative name(s):
2S albumin small chain
4 kDa napin-like protein small chain
RS2B
Alternative name(s):
2S albumin large chain
7.3 kDa napin-like protein large chain
RL2
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Biotechnological usei

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

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3467. Ric c 1.0101.
614. Ric c 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000003216225 – 35Add BLAST11
ChainiPRO_000004185736 – 76Allergen Ric c 3 small chainAdd BLAST41
PropeptideiPRO_000004185877 – 861 Publication10
ChainiPRO_000004185987 – 153Allergen Ric c 3 large chainAdd BLAST67
PropeptideiPRO_0000041860154 – 1563
ChainiPRO_0000032163157 – 190Allergen Ric c 1 small chainAdd BLAST34
PropeptideiPRO_0000032164191 – 1933
ChainiPRO_0000032165194 – 258Allergen Ric c 1 large chainAdd BLAST65

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 108Interchain (between Ric c 3 small and Ric c 3 large chains)1 Publication
Disulfide bondi61 ↔ 97Interchain (between Ric c 3 small and Ric c 3 large chains)1 Publication
Modified residuei69Phosphoserine1 Publication1
Modified residuei87Pyrrolidone carboxylic acidCurated1
Disulfide bondi98 ↔ 1451 Publication
Disulfide bondi110 ↔ 1491 Publication
Disulfide bondi162 ↔ 212Interchain (between Ric c 1 small and Ric c 1 large chains)By similarity
Disulfide bondi175 ↔ 201Interchain (between Ric c 1 small and Ric c 1 large chains)By similarity
Modified residuei194Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi202 ↔ 249By similarity
Disulfide bondi214 ↔ 256By similarity

Post-translational modificationi

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Pyrrolidone carboxylic acid

PTM databases

iPTMnetiP01089.

Expressioni

Developmental stagei

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

Interactioni

Subunit structurei

The 2 mature proteins consist of heterodimers of a small and a large chain; disulfide-linked.1 Publication

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 48Combined sources5
Helixi49 – 53Combined sources5
Helixi61 – 66Combined sources6
Beta strandi67 – 69Combined sources3
Beta strandi84 – 86Combined sources3
Beta strandi88 – 90Combined sources3
Helixi92 – 101Combined sources10
Helixi108 – 123Combined sources16
Helixi132 – 145Combined sources14
Turni149 – 151Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PSYNMR-A33-156[»]
ProteinModelPortaliP01089.
SMRiP01089.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01089.

Family & Domainsi

Sequence similaritiesi

Belongs to the 2S seed storage albumins family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.120.10. 1 hit.
InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000617. Napin.
IPR013771. Trypsin/amylase_inhib.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 2 hits.
[Graphical view]
PRINTSiPR00496. NAPIN.
SMARTiSM00499. AAI. 2 hits.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01089-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLIPTIAL VSVLLFIIAN ASFAYRTTIT TIEIDESKGE REGSSSQQCR
60 70 80 90 100
QEVQRKDLSS CERYLRQSSS RRSPGEEVLR MPGDENQQQE SQQLQQCCNQ
110 120 130 140 150
VKQVRDECQC EAIKYIAEDQ IQQGQLHGEE SERVAQRAGE IVSSCGVRCM
160 170 180 190 200
RQTRTNPSQQ GCRGQIQEQQ NLRQCQEYIK QQVSGQGPRR SDNQERSLRG
210 220 230 240 250
CCDHLKQMQS QCRCEGLRQA IEQQQSQGQL QGQDVFEAFR TAANLPSMCG

VSPTECRF
Length:258
Mass (Da):29,290
Last modified:November 1, 1990 - v2
Checksum:i27874CFC50E41072
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti194Q → E AA sequence (PubMed:8980648).Curated1
Sequence conflicti222E → Q AA sequence (PubMed:7174664).Curated1
Sequence conflicti226 – 229Missing AA sequence (PubMed:7174664).Curated4
Sequence conflicti234D → N AA sequence (PubMed:7174664).Curated1
Sequence conflicti255E → Q AA sequence (PubMed:7174664).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti74P → T.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54158 Genomic DNA. Translation: CAA38097.1.
PIRiS11499. RZCS.
RefSeqiXP_002522854.1. XM_002522808.2.
XP_002522855.1. XM_002522809.1.

Genome annotation databases

GeneIDi8280732.
8280733.
KEGGircu:8280732.
rcu:8280733.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54158 Genomic DNA. Translation: CAA38097.1.
PIRiS11499. RZCS.
RefSeqiXP_002522854.1. XM_002522808.2.
XP_002522855.1. XM_002522809.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PSYNMR-A33-156[»]
ProteinModelPortaliP01089.
SMRiP01089.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3467. Ric c 1.0101.
614. Ric c 1.

PTM databases

iPTMnetiP01089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8280732.
8280733.
KEGGircu:8280732.
rcu:8280733.

Miscellaneous databases

EvolutionaryTraceiP01089.

Family and domain databases

Gene3Di1.10.120.10. 1 hit.
InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000617. Napin.
IPR013771. Trypsin/amylase_inhib.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 2 hits.
[Graphical view]
PRINTSiPR00496. NAPIN.
SMARTiSM00499. AAI. 2 hits.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry namei2SS_RICCO
AccessioniPrimary (citable) accession number: P01089
Secondary accession number(s): Q9S872, Q9S873, Q9S874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.