Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08819 (CBP2_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. 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

Names and origin

Protein namesRecommended name:
Serine carboxypeptidase 2

EC=3.4.16.6
Alternative name(s):
CPDW-II
Short name=CP-WII
Carboxypeptidase D
Serine carboxypeptidase II

Cleaved into the following 2 chains:

  1. Serine carboxypeptidase 2 chain A
    Alternative name(s):
    Serine carboxypeptidase II chain A
  2. Serine carboxypeptidase 2 chain B
    Alternative name(s):
    Serine carboxypeptidase II chain B
Gene names
Name:CBP2
OrganismTriticum aestivum (Wheat) [Complete proteome]
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential release of a C-terminal arginine or lysine residue.

Subunit structure

Carboxypeptidase II is a dimer, where each monomer is composed of two chains linked by a disulfide bond.

Post-translational modification

N-glycosylated.

Allergenic properties

Causes an allergic reaction in human. Binds to IgE. Ref.2

Sequence similarities

Belongs to the peptidase S10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259Serine carboxypeptidase 2 chain A
PRO_0000004312
Propeptide260 – 28627Linker peptide
PRO_0000274569
Chain287 – 444158Serine carboxypeptidase 2 chain B
PRO_0000004313

Regions

Region51 – 533Substrate binding
Region157 – 1593Substrate binding

Sites

Active site1581
Active site3611
Active site4131
Binding site2511Substrate
Binding site4141Substrate

Amino acid modifications

Glycosylation1161N-linked (GlcNAc...)
Glycosylation1271N-linked (GlcNAc...)
Glycosylation2591N-linked (GlcNAc...)
Glycosylation3121N-linked (GlcNAc...)
Glycosylation3181N-linked (GlcNAc...)
Disulfide bond65 ↔ 324Interchain (between A and B chains)
Disulfide bond222 ↔ 234
Disulfide bond258 ↔ 291Interchain (between A and B chains)

Natural variations

Natural variant1 – 33Missing in a' chain.

Experimental info

Sequence conflict2091I → L in CAI64396. Ref.3
Sequence conflict2161R → Q in CAI64396. Ref.3
Sequence conflict2191K → R in CAI64396. Ref.3
Sequence conflict3071M → T in CAI64396. Ref.3
Sequence conflict3221A → S in CAI64396. Ref.3
Sequence conflict440 – 4412TK → AT in CAI64396. Ref.3
Sequence conflict4441T → TVA in CAI64396. Ref.3

Secondary structure

......................................................................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08819 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: 983B9BCC1C2DECB2

FASTA44449,506
        10         20         30         40         50         60 
VEPSGHAADR IARLPGQPAV DFDMYSGYIT VDEGAGRSLF YLLQEAPEDA QPAPLVLWLN 

        70         80         90        100        110        120 
GGPGCSSVAY GASEELGAFR VKPRGAGLVL NEYRWNKVAN VLFLDSPAGV GFSYTNTSSD 

       130        140        150        160        170        180 
IYTSGDNRTA HDSYAFLAKW FERFPHYKYR DFYIAGESYA GHYVPELSQL VHRSKNPVIN 

       190        200        210        220        230        240 
LKGFMVGNGL IDDYHDYVGT FEFWWNHGIV SDDTYRRLKE ACLHDSFIHP SPACDAATDV 

       250        260        270        280        290        300 
ATAEQGNIDM YSLYTPVCNI TSSSSSSSSS LSQQRRSRGR YPWLTGSYDP CTERYSTAYY 

       310        320        330        340        350        360 
NRRDVQMALH ANVTGAMNYT WATCSDTINT HWHDAPRSML PIYRELIAAG LRIWVFSGDT 

       370        380        390        400        410        420 
DAVVPLTATR YSIGALGLPT TTSWYPWYDD QEVGGWSQVY KGLTLVSVRG AGHEVPLHRP 

       430        440 
RQALVLFQYF LQGKPMPGQT KNAT 

« Hide

References

[1]"Primary structure and enzymatic properties of carboxypeptidase II from wheat bran."
Breddam K., Soerensen S.B., Svendsen I.
Carlsberg Res. Commun. 52:297-311(1987)
Cited for: PROTEIN SEQUENCE OF 1-263 AND 285-444.
[2]"Screening the allergenic repertoires of wheat and maize with sera from double-blind, placebo-controlled food challenge positive patients."
Weichel M., Vergoossen N.J., Bonomi S., Scibilia J., Ortolani C., Ballmer-Weber B.K., Pastorello E.A., Crameri R.
Allergy 61:128-135(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 187-444, ALLERGEN.
Strain: cv. Wyuna.
Tissue: Endosperm.
[3]"Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase."
Liao D.-I., Remington S.J.
J. Biol. Chem. 265:6528-6531(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[4]"Refined atomic model of wheat serine carboxypeptidase II at 2.2-A resolution."
Liao D.-I., Breddam K., Sweet R.M., Bullock T., Remington S.J.
Biochemistry 31:9796-9812(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]"Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-A resolution."
Bullock T.L., Branchaud B., Remington S.J.
Biochemistry 33:11127-11134(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[6]"Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity."
Bullock T.L., Breddam K., Remington S.J.
J. Mol. Biol. 255:714-725(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ890016 mRNA. Translation: CAI64396.1.
PIRA29639.
UniGeneTa.56555.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCRX-ray2.50A1-263[»]
B285-444[»]
1BCSX-ray2.08A1-263[»]
B285-444[»]
1WHSX-ray2.00A6-260[»]
B287-439[»]
1WHTX-ray2.00A5-260[»]
B287-439[»]
3SC2X-ray2.20A1-259[»]
B287-438[»]
ProteinModelPortalP08819.
SMRP08819. Positions 5-260, 287-439.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.005.

Proteomic databases

PRIDEP08819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP08819.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08819.

Entry information

Entry nameCBP2_WHEAT
AccessionPrimary (citable) accession number: P08819
Secondary accession number(s): Q4W1G1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references