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P55748 (CBP22_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. 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-2

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

Protein attributes

Sequence length436 AA.
Sequence statusFragment.
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 By similarity.

Developmental stage

Expressed in the germinating embryo. Low levels in the developing aleurone and 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
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentvacuole

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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

Chain‹1 – 256›256Serine carboxypeptidase II-2 chain A
PRO_0000004317
Propeptide257 – 27014Linker peptide By similarity
PRO_0000004318
Chain271 – 436166Serine carboxypeptidase II-2 chain B
PRO_0000004319

Sites

Active site1491 By similarity
Active site3501 By similarity
Active site4031 By similarity

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 313Interchain (between A and B chains) By similarity
Disulfide bond217 ↔ 229 By similarity
Disulfide bond253 ↔ 281Interchain (between A and B chains) By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P55748 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: E0F82D97E0C34DC9

FASTA43648,952
        10         20         30         40         50         60 
VPRVPGQAFD ASFAHYAGYV TVSEDRGAAL FYWFFEAAHD PASKPLLLWL NGGPGCSSIA 

        70         80         90        100        110        120 
FGVGEEVGPF HVNADGKGVH MNPYSWNQVA NILFLDSPVG VGYSYSNTSA DILSNGDERT 

       130        140        150        160        170        180 
AKDSLVFLTK WLERFPQYKE REFYLTGESY AGHYVPQLAQ AIKRHHEATG DKSINLKGYM 

       190        200        210        220        230        240 
VGNALTDDFH DHYGIFQYMW TTGLISDQTY KLLNIFCDFE SFVHTSPQCD KILDIASTEA 

       250        260        270        280        290        300 
GNIDSYSIFT PTCHSSFASS RNKVVKRLRS VGKMGEQYDP CTEKHSIVYF NLHEVQKALH 

       310        320        330        340        350        360 
VNPVIGKSKW ETCSEVINTN WKDCERSVLH IYHELIQYGL RIWMFSGDTD AVIPVTSTRY 

       370        380        390        400        410        420 
SIDALKLPTV TPWHAWYDDD GEVGGWTQGY KGLNFVTVRG AGHEVPLHRP KQALTLIKSF 

       430 
LAGRPMPVLS DLRSDM 

« 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], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Alexis.
Tissue: Grain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78878 mRNA. Translation: CAB59202.1.

3D structure databases

ProteinModelPortalP55748.
SMRP55748. Positions 1-254, 278-427.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP55748.

Gene expression databases

GenevestigatorP55748.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBP22_HORVU
AccessionPrimary (citable) accession number: P55748
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 73 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