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P07519 (CBP1_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 101. 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 1

EC=3.4.16.5
Alternative name(s):
CP-MI
Carboxypeptidase C
Serine carboxypeptidase I

Cleaved into the following 2 chains:

  1. Serine carboxypeptidase 1 chain A
    Alternative name(s):
    Serine carboxypeptidase I chain A
  2. Serine carboxypeptidase 1 chain B
    Alternative name(s):
    Serine carboxypeptidase I chain B
Gene names
Name:CBP1
Synonyms:CXP;1
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the degradation of small peptides (2-5 residues) or in the degradation of storage proteins in the embryo.

Catalytic activity

Release of a C-terminal amino acid with broad specificity.

Subunit structure

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

Subcellular location

Secreted. Note: Secreted into the endosperm.

Developmental stage

After one day of germination, mainly found in the scutellum of the developing grain; barely detectable after four days, and absent from the mature grain. A lower level of expression is seen in the aleurone both during development and germination.

Post-translational modification

The linker peptide is endoproteolytically excised during enzyme maturation.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuole

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

Signal peptide1 – 3030 Potential
Chain31 – 296266Serine carboxypeptidase 1 chain A
PRO_0000004301
Propeptide297 – 35155Linker peptide
PRO_0000004302
Chain352 – 499148Serine carboxypeptidase 1 chain B
PRO_0000004303

Regions

Motif497 – 4993Microbody targeting signal Potential

Sites

Active site1881 By similarity
Active site4231 By similarity
Active site4761 By similarity

Amino acid modifications

Glycosylation1481N-linked (GlcNAc...)
Glycosylation2621N-linked (GlcNAc...)
Glycosylation4071N-linked (GlcNAc...)
Disulfide bond92 ↔ 388Interchain (between A and B chains) By similarity
Disulfide bond256 ↔ 268 By similarity
Disulfide bond291 ↔ 355Interchain (between A and B chains) By similarity

Experimental info

Sequence conflict1021H → P AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P07519 [UniParc].

Last modified November 1, 1997. Version 4.
Checksum: 9C6674B14D9DB9BF

FASTA49954,096
        10         20         30         40         50         60 
MARCRRRSGC TAGAALLLLL ALALSGGGGA APQGAEVTGL PGFDGALPSK HYAGYVTVDE 

        70         80         90        100        110        120 
GHGRNLFYYV VESERDPGKD PVVLWLNGGP GCSSFDGFVY EHGPFNFESG GSVKSLPKLH 

       130        140        150        160        170        180 
LNPYAWSKVS TMIYLDSPAG VGLSYSKNVS DYETGDLKTA TDSHTFLLKW FQLYPEFLSN 

       190        200        210        220        230        240 
PFYIAGESYA GVYVPTLSHE VVKGIQGGAK PTINFKGYMV GNGVCDTIFD GNALVPFAHG 

       250        260        270        280        290        300 
MGLISDEIYQ QASTSCHGNY WNATDGKCDT AISKIESLIS GLNIYDILEP CYHSRSIKEV 

       310        320        330        340        350        360 
NLQNSKLPQS FKDLGTTNKP FPVRTRMLGR AWPLRAPVKA GRVPSWQEVA SGVPCMSDEV 

       370        380        390        400        410        420 
ATAWLDNAAV RSAIHAQSVS AIGPWLLCTD KLYFVHDAGS MIAYHKNLTS QGYRAIIFSG 

       430        440        450        460        470        480 
DHDMCVPFTG SEAWTKSLGY GVVDSWRPWI TNGQVSGYTE GYEHGLTFAT IKGAGHTVPE 

       490 
YKPQEAFAFY SRWLAGSKL 

« Hide

References

[1]Rocher A., Lok F., Cameron-Mills V., von Wettstein D.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Aleurone.
[2]"The A- and B-chains of carboxypeptidase I from germinated barley originate from a single precursor polypeptide."
Doan N.P., Fincher G.B.
J. Biol. Chem. 263:11106-11110(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 88-499.
[3]"Primary structure of carboxypeptidase I from malted barley."
Soerensen S.B., Breddam K., Svendsen I.
Carlsberg Res. Commun. 51:475-485(1986)
Cited for: PROTEIN SEQUENCE OF 31-296 AND 352-499.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09603 mRNA. Translation: CAA70816.1.
J03897 mRNA. Translation: AAA32940.1.
PIRCPBHS. T05367.
UniGeneHv.12403.

3D structure databases

ProteinModelPortalP07519.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP07519.

Gene expression databases

GenevestigatorP07519.

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. 2 hits.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBP1_HORVU
AccessionPrimary (citable) accession number: P07519
Secondary accession number(s): P07520
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 101 of the entry and version 4 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