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P52711 (CBP23_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 II-3

EC=3.4.16.6
Alternative name(s):
CP-MII.3
Gene names
Name:CXP;2-3
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Developmental stage

Expressed in the germinating embryo. Also found in the roots and shoots of the growing seedling.

Post-translational modification

The linker peptide is endoproteolytically excised during enzyme maturation By similarity.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Molecular_functionserine-type carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 7757 Potential
PRO_0000004320
Chain78 – 341264Serine carboxypeptidase II-3 chain A
PRO_0000004321
Propeptide342 – 35211Linker peptide By similarity
PRO_0000004322
Chain353 – 516164Serine carboxypeptidase II-3 chain B
PRO_0000004323

Sites

Active site2361 By similarity
Active site4271 By similarity
Active site4841 By similarity

Amino acid modifications

Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond143 ↔ 391Interchain (between A and B chains) By similarity
Disulfide bond300 ↔ 315 By similarity
Disulfide bond339 ↔ 359Interchain (between A and B chains) By similarity

Sequences

Sequence LengthMass (Da)Tools
P52711 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D41AA1C56CF8D355

FASTA51655,914
        10         20         30         40         50         60 
MKCTVVALVL LVAVQCLVLG AGPAAAAKAR RTRQGDYLNR LRGSPSSRAS WESLAAVEEQ 

        70         80         90        100        110        120 
TTTKAAGRPA PVAAAVEAGR KEADRVEALP GHPRGVDFAQ YAGYVTVDAA AGRALFYYLA 

       130        140        150        160        170        180 
EAVGGNGDKT KPLLLWLNGG PGCSSLGYGA MEELGPFRVM SDGKTLYSNP YSWNHAANVL 

       190        200        210        220        230        240 
FLESPAGVGY SYSNTTADYG RSGDNGTAED AYQFLDNWLE RFPEYKGREF YITGESYAGH 

       250        260        270        280        290        300 
YVPQLAHAIL RHASPDINLK GIMIGNAVIN DWTDSKGMYD FFWTHALISD ETADGISKNC 

       310        320        330        340        350        360 
NFTAYGAGVA SNALCDAASD EVGESLADID IYNIYAPNCQ SEKLVTPPIA PSIDNFDPCT 

       370        380        390        400        410        420 
DYYVEAYLNR PDVQKALHAN VTRLDHPWSA CSDVLTRWVD SAKTVLPIIQ ELMKNSIRVW 

       430        440        450        460        470        480 
VYSGDTDGRV PVTSSRLSVN QLQLPVAAKW RPWFSSTKGA GEVGGYIVQY KGDLSLVTVR 

       490        500        510 
GAGHEVPSYQ PRRALVLVQN FLAGKALPDC KECEQD 

« Hide

References

[1]"The expression of serine carboxypeptidases during maturation and germination of the barley grain."
Dal Degan F., Rocher A., Cameron-Mills V., von Wettstein D.
Proc. Natl. Acad. Sci. U.S.A. 91:8209-8213(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Alexis.
Tissue: Grain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78877 mRNA. Translation: CAA55478.1.
PIRS44191.

3D structure databases

ProteinModelPortalP52711.
SMRP52711. Positions 82-340.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP52711.

Gene expression databases

GenevestigatorP52711.

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...

Entry information

Entry nameCBP23_HORVU
AccessionPrimary (citable) accession number: P52711
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 69 of the entry and version 1 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