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P09955 (CBPB1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 121. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase B

EC=3.4.17.2
Gene names
Name:CPB1
Synonyms:CPB
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length416 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 lysine or arginine amino acid.

Cofactor

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetallocarboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.2 Ref.3 Ref.5
Propeptide16 – 11095Activation peptide
PRO_0000004373
Chain111 – 416306Carboxypeptidase B
PRO_0000004374

Sites

Active site3561
Active site3781Nucleophile
Metal binding1761Zinc
Metal binding1791Zinc
Metal binding3041Zinc

Amino acid modifications

Disulfide bond173 ↔ 186
Disulfide bond245 ↔ 268
Disulfide bond259 ↔ 273

Experimental info

Sequence conflict401L → E AA sequence Ref.2
Sequence conflict401L → E AA sequence Ref.3

Secondary structure

....................................................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09955 [UniParc].

Last modified April 26, 2005. Version 5.
Checksum: 5FA7FCED7B45AE6A

FASTA41647,381
        10         20         30         40         50         60 
MLAFLILVTV TLASAHHSGE HFEGEKVFRV NVEDENDISL LHELASTRQI DFWKPDSVTQ 

        70         80         90        100        110        120 
IKPHSTVDFR VKAEDILAVE DFLEQNELQY EVLINNLRSV LEAQFDSRVR TTGHSYEKYN 

       130        140        150        160        170        180 
NWETIEAWTK QVTSENPDLI SRTAIGTTFL GNNIYLLKVG KPGPNKPAIF MDCGFHAREW 

       190        200        210        220        230        240 
ISHAFCQWFV REAVLTYGYE SHMTEFLNKL DFYVLPVLNI DGYIYTWTKN RMWRKTRSTN 

       250        260        270        280        290        300 
AGTTCIGTDP NRNFDAGWCT TGASTDPCDE TYCGSAAESE KETKALADFI RNNLSSIKAY 

       310        320        330        340        350        360 
LTIHSYSQMI LYPYSYDYKL PENNAELNNL AKAAVKELAT LYGTKYTYGP GATTIYPAAG 

       370        380        390        400        410 
GSDDWAYDQG IKYSFTFELR DKGRYGFILP ESQIQATCEE TMLAIKYVTN YVLGHL 

« Hide

References

[1]"Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme."
Ventura S., Villegas V., Sterner J., Larson J., Vendrell J., Hershberger C., Aviles F.X.
J. Biol. Chem. 274:19925-19933(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Analysis of the activation process of porcine procarboxypeptidase B and determination of the sequence of its activation segment."
Burgos F.J., Salva M., Villegas V., Soriano F., Mendez E., Aviles F.X.
Biochemistry 30:4082-4089(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-118.
[3]"Sequential homologies between procarboxypeptidases A and B from porcine pancreas."
Aviles F.X., Vendrell J., Burgos F.J., Soriano F., Mendez E.
Biochem. Biophys. Res. Commun. 130:97-103(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 16-53.
[4]"Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity."
Coll M., Guasch A., Aviles F.X., Huber R.
EMBO J. 10:1-9(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 16-416.
[5]"Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B."
Vendrell J., Wider G., Aviles F.X., Wuethrich K.
Biochemistry 29:7515-7522(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF ACTIVATION PEPTIDE, PROTEIN SEQUENCE OF 16-96.
[6]"The NMR structure of the activation domain isolated from porcine procarboxypeptidase B."
Vendrell J., Billeter M., Wider G., Aviles F.X., Wuethrich K.
EMBO J. 10:11-15(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF ACTIVATION PEPTIDE.
[7]"Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B."
Billeter M., Vendrell J., Wider G., Aviles F.X., Coll M., Guasch A., Huber R., Wuethrich K.
J. Biomol. NMR 2:1-10(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF ACTIVATION PEPTIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ133775 mRNA. Translation: CAB46991.1.
PIRA38354.
RefSeqNP_999334.1. NM_214169.1.
UniGeneSsc.16048.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NSAX-ray2.30A22-416[»]
1PBANMR-A16-96[»]
1Z5RX-ray1.40A/B/C111-416[»]
1ZG7X-ray1.75A/B/C111-416[»]
1ZG8X-ray2.00A/B/C111-416[»]
1ZG9X-ray2.00A/B/C111-416[»]
2JEWX-ray1.40A111-416[»]
2PIYX-ray1.43A/B/C111-416[»]
2PIZX-ray1.60A/B/C111-416[»]
2PJ0X-ray1.65A/B/C111-416[»]
2PJ1X-ray1.64A/B/C111-416[»]
2PJ2X-ray1.95A/B/C111-416[»]
2PJ3X-ray1.64A/B/C111-416[»]
2PJ4X-ray2.00A/B111-416[»]
2PJ5X-ray1.65A/B/C111-416[»]
2PJ6X-ray1.60A111-416[»]
2PJ7X-ray1.77A/B/C111-416[»]
2PJ8X-ray1.70A/B/C111-416[»]
2PJ9X-ray1.56A111-416[»]
2PJAX-ray1.70A/B/C111-416[»]
2PJBX-ray1.70A/B/C111-416[»]
2PJCX-ray1.74A/B/C111-416[»]
3GLJX-ray1.89A16-416[»]
3WABX-ray2.15A111-416[»]
3WC5X-ray1.70A111-416[»]
3WC6X-ray1.65A111-416[»]
3WC7X-ray1.90A111-416[»]
ProteinModelPortalP09955.
SMRP09955. Positions 22-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000012464.

Chemistry

BindingDBP09955.
ChEMBLCHEMBL4065.

Protein family/group databases

MEROPSM14.003.

Proteomic databases

PaxDbP09955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397341.
KEGGssc:397341.

Organism-specific databases

CTD1360.

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000252968.
HOVERGENHBG050815.
KOK01291.

Family and domain databases

Gene3D3.30.70.340. 1 hit.
InterProIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMSSF54897. SSF54897. 1 hit.
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09955.
PMAP-CutDBP09955.

Entry information

Entry nameCBPB1_PIG
AccessionPrimary (citable) accession number: P09955
Secondary accession number(s): Q9XSP3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 26, 2005
Last modified: December 11, 2013
This is version 121 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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