Q6PSU2 (CONG7_ARAHY) Reviewed, UniProtKB/Swiss-Prot
Last modified
February 8, 2011.
Version 34.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Conglutin-7 Alternative name(s): 2S protein 1 Seed storage protein SSP1 Seed storage protein SSP2 Allergen=Ara h 2 |
| Organism | Arachis hypogaea (Peanut) |
| Taxonomic identifier | 3818 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Dalbergieae › Arachis |
Protein attributes
| Sequence length | 172 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Weak inhibitor of trypsin. Ref.14 |
| Tissue specificity | Expressed in seeds, not expressed in leaves, roots and pegs. Ref.9 |
| Developmental stage | Expressed at very low levels in immature seeds and at high levels from 40-75 days after pollination. Expression decreases after 75 days after pollination. Ref.9 |
| Induction | Repressed by water stress. Ref.10 |
| Post-translational modification | The hydroxyproline modifications determined by mass spectrometry (Ref.11) are probably 4-hydroxyproline as determined for other extracellular plant proteins. |
| Allergenic properties | Causes an allergic reaction in human. Binds to IgE. Ref.13 |
| Miscellaneous | Resistant to proteolysis. Ref.13 |
| Sequence similarities | Belongs to the 2S seed storage albumins family. |
| Biophysicochemical properties | Temperature dependence: Thermostable. Ref.13 |
| Mass spectrometry | Molecular mass is 18050 Da from positions 22 - 172. Determined by MALDI. Isoform 1. Ref.1 Molecular mass is 16670 Da from positions 22 - 172. Determined by MALDI. Isoform 3. Ref.1 |
| Sequence caution | The sequence AAT00598.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAT00599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAU21494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing |
| Disease | Allergen |
| Domain | Signal |
| Ligand | IgE-binding protein |
| Molecular function | Protease inhibitor Seed storage protein Serine protease inhibitor Storage protein |
| PTM | Disulfide bond Hydroxylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | IgE binding Inferred from electronic annotation. Source: UniProtKB-KW nutrient reservoir activityInferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase inhibitor activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q6PSU2-1) Also known as: P1; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q6PSU2-2) Also known as: P2; The sequence of this isoform differs from the canonical sequence as follows: 76-87: Missing. | ||||||
| Isoform 3 (identifier: Q6PSU2-3) Also known as: P3; The sequence of this isoform differs from the canonical sequence as follows: 170-172: DRY → D | ||||||
| Isoform 4 (identifier: Q6PSU2-4) Also known as: P4; The sequence of this isoform differs from the canonical sequence as follows: 76-87: Missing. 170-172: DRY → D |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Ref.1 Ref.10 Ref.11 Ref.12 | ||||||||
| Chain | 22 – 172 | 151 | Conglutin-7 Ref.1 Ref.10 | PRO_0000370687 | |||||||
Amino acid modifications | |||||||||||
| Modified residue | 67 | 1 | 4-hydroxyproline Ref.11 | ||||||||
| Modified residue | 74 | 1 | 4-hydroxyproline Ref.11 | ||||||||
| Modified residue | 86 | 1 | 4-hydroxyproline Ref.11 | ||||||||
| Disulfide bond | 33 ↔ 116 | Ref.11 UniProtKB Q647G9 | |||||||||
| Disulfide bond | 45 ↔ 103 | Or C-45 with C-104 Ref.11 UniProtKB Q647G9 | |||||||||
| Disulfide bond | 104 ↔ 152 | Or C-103 with C-152 Ref.11 UniProtKB Q647G9 | |||||||||
| Disulfide bond | 118 ↔ 160 | Ref.11 UniProtKB Q647G9 | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 76 – 87 | 12 | Missing in isoform 2 and isoform 4. | VSP_038916 | |||||||
| Alternative sequence | 170 – 172 | 3 | DRY → D in isoform 3 and isoform 4. | VSP_038917 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 2 – 3 | 2 | Missing in ACN62248. Ref.7 | ||||||||
| Sequence conflict | 10 | 1 | L → P in AAM78596. Ref.10 | ||||||||
| Sequence conflict | 27 | 1 | L → F in AAT00599. Ref.4 | ||||||||
| Sequence conflict | 61 | 1 | G → E in AAU21494. Ref.2 | ||||||||
| Sequence conflict | 61 | 1 | G → E in AAT00599. Ref.4 | ||||||||
| Sequence conflict | 61 | 1 | G → E in ACN62248. Ref.7 | ||||||||
| Sequence conflict | 61 | 1 | G → E in AAK96887. Ref.8 | ||||||||
| Sequence conflict | 65 – 78 | 14 | Missing in ABL14268. Ref.5 | ||||||||
| Sequence conflict | 163 | 1 | E → D in AAU21494. Ref.2 | ||||||||
| Sequence conflict | 163 | 1 | E → D in AAT00599. Ref.4 | ||||||||
| Sequence conflict | 163 | 1 | E → D in ACN62248. Ref.7 | ||||||||
| Sequence conflict | 163 | 1 | E → D in AAK96887. Ref.8 | ||||||||
Sequences
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References
| [1] | "Isolation and characterization of two complete Ara h 2 isoforms cDNA." Chatel J.-M., Bernard H., Orson F.M. Int. Arch. Allergy Immunol. 131:14-18(2003) [PubMed: 12759484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 22-31, MASS SPECTROMETRY. |
| [2] | "Isolation of peanut genes encoding arachins and conglutins by expressed sequence tags." Yan Y.-S., Lin X.-D., Zhang Y.-S., Wang L., Wu K., Huang S.-Z. Plant Sci. 169:439-445(2005) [Agricola: IND43739496] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Strain: cv. Shanyou 523. Tissue: Cotyledon. |
| [3] | "Chromosomal and phylogenetic context for conglutin genes in Arachis based on genomic sequence." Ramos M.L., Fleming G., Chu Y., Akiyama Y., Gallo M., Ozias-Akins P. Mol. Genet. Genomics 275:578-592(2006) [PubMed: 16614814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. F78-1339. |
| [4] | "cDNA cloning of peanut seed storage protein." Yan Y.-S., Wang L., Liao B., Li H., Lin X.-D., Huang S.-Z. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: cv. Shanyou 523. |
| [5] | "Isolation of peanut genes encoding seed storage proteins and stress proteins from developing cotyledons by expressed sequence tags." Fu G., Yan Y.-S., Wang L., Zhong Y., Huang S.-Z. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: cv. Shanyou 523. |
| [6] | "Cloning and characterization of four genes encoding peanut seed oleosins." Li C., Fu G., Zhong Y., Yan Y., Wang L., Huang S. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Shanyou 523. |
| [7] | "Proteolytical processing of Ara h 2 into mature form." Radosavljevic J., Dobrijevic D., Blanusa M., Jadranin M., Cirkovic Velickovic T. Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [8] | "Isolation and molecular characterization of the first genomic clone of a major peanut allergen, Ara h 2." Viquez O.M., Summer C.G., Dodo H.W. J. Allergy Clin. Immunol. 107:713-717(2001) [PubMed: 11295663] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168. Strain: cv. F78-1339. Tissue: Seed. |
| [9] | "Seed-specific, developmentally regulated genes of peanut." Paik-Ro O.G., Seib J.C., Smith R.L. Theor. Appl. Genet. 104:236-240(2002) [PubMed: 12582692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-168 (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: cv. FL435. Tissue: Seed. |
| [10] | "Re-investigation of the major peanut allergen Arah2 on the molecular level." Becker W.-M., Suhr M., Lindner B., Wicklein D., Lepp U. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-172 (ISOFORM 1). |
| [11] | "Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2." Li J., Shefcheck K., Callahan J., Fenselau C. Protein Sci. 19:174-182(2010) [PubMed: 19937656] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-172 (ISOFORMS 1; 2; 3 AND 4), MASS SPECTROMETRY, HYDROXYLATION AT PRO-67; PRO-74 AND PRO-86, DISULFIDE BONDS. |
| [12] | "Suppression of seed storage proteins upon water stress in Arachis hypogea var. M-13 seeds." Katam R., Vasanthaiah H.K.N., Basha S.M., McClung S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 22-33; 117-131; 147-155 AND 160-169, REPRESSION BY WATER STRESS. Strain: cv. M13. Tissue: Seed. |
| [13] | "Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions." Lehmann K., Schweimer K., Reese G., Randow S., Suhr M., Becker W.-M., Vieths S., Roesch P. Biochem. J. 395:463-472(2006) [PubMed: 16372900] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-31 AND 93-99, ALLERGEN, RESISTANCE TO HEAT AND PROTEOLYSIS. |
| [14] | "The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function." Maleki S.J., Viquez O.M., Jacks T., Dodo H.W., Champagne E.T., Chung S.-Y., Landry S.J. J. Allergy Clin. Immunol. 112:190-195(2003) [PubMed: 12847498] [Abstract] Cited for: FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY158467 mRNA. Translation: AAN77576.1. AY581853 mRNA. Translation: AAT00598.1. Different initiation. AY722689 mRNA. Translation: AAU21494.1. Different initiation. EF609644 Genomic DNA. Translation: ABQ96215.1. AY581854 mRNA. Translation: AAT00599.1. Different initiation. EF080817 mRNA. Translation: ABL14268.1. EF695402 Genomic DNA. Translation: ABS28872.1. FJ713110 Genomic DNA. Translation: ACN62248.1. AY007229 Genomic DNA. Translation: AAK96887.1. AF366560 mRNA. Translation: AAO61750.1. AY117434 mRNA. Translation: AAM78596.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1W2Q based on UniProtKB Q647G9. |
| ProteinModelPortal | Q6PSU2. |
| SMR | Q6PSU2. Positions 30-169. |
| ModBase | Search... |
Protein family/group databases | |
| Allergome | 1081. Ara h 2.0101. 1082. Ara h 2.0201. 51. Ara h 2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR016140. Bifunc_inhib/LTP/seed_store. IPR003612. LTP/seed_store/tryp_amyl_inhib. IPR013771. Trypsin/amylase_inhib. [Graphical view] |
| Gene3D | G3DSA:1.10.120.10. Trypsin/amylase_inhib. 1 hit. |
| Pfam | PF00234. Tryp_alpha_amyl. 1 hit. [Graphical view] |
| SMART | SM00499. AAI. 1 hit. [Graphical view] |
| SUPFAM | SSF47699. Bifunc_inhib/LTP/seed_store. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | CONG7_ARAHY | ||||||||
| Accession | Primary (citable) accession number: Q6PSU2 Secondary accession number(s): A1DZE8 Q941R0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Allergens Nomenclature of allergens and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with