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Protein

Carboxypeptidase B

Gene

CPB1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential release of a C-terminal lysine or arginine amino acid.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi176 – 1761Zinc; catalyticBy similarity
Metal bindingi179 – 1791Zinc; catalyticBy similarity
Binding sitei234 – 2341SubstrateBy similarity
Metal bindingi304 – 3041Zinc; catalyticBy similarity
Binding sitei356 – 3561SubstrateBy similarity
Active sitei378 – 3781Proton donor/acceptor1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM14.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase B (EC:3.4.17.21 Publication)
Gene namesi
Name:CPB1
Synonyms:CPB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Propeptidei17 – 11094Activation peptideBy similarityPRO_0000280813Add
BLAST
Chaini111 – 417307Carboxypeptidase BPRO_0000212782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi173 ↔ 1862 Publications
Disulfide bondi245 ↔ 2682 Publications
Disulfide bondi259 ↔ 2732 Publications

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP00732.
PRIDEiP00732.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000580.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPBX-ray2.80A111-192[»]
B200-416[»]
ProteinModelPortaliP00732.
SMRiP00732. Positions 22-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00732.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 1794Substrate bindingBy similarity
Regioni251 – 2522Substrate bindingBy similarity
Regioni305 – 3062Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiP00732.
OMAiDVEDESH.
OrthoDBiEOG7RZ5Q9.
TreeFamiTF317197.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR003146. M14A_act_pep.
IPR000834. Peptidase_M14.
IPR009020. Propept_inh.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54897. SSF54897. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAFLILVTV TLASAHHSGE HFEGDKVFRV HVEDENHISL LHELASTRQM
60 70 80 90 100
DFWKPDSVTQ VKPHSTVDFR VKAEDTVAVE DFLGQNGLRY EVLISNLRSM
110 120 130 140 150
LEAQFDSRVR TTGHSYEKYN NWETIEAWTE QVASENPDLI SRSAIGTTFL
160 170 180 190 200
GNTIYLLKVG KPGSNKPAVF MDCGFHAREW ISPAFCQWFV REAVRTYGRE
210 220 230 240 250
IHMTEFLDKL DFYVLPVVNI DGYIYTWTTN RMWRKTRSTR AGSSCTGTDL
260 270 280 290 300
NRNFDAGWCS IGASNNPCSE TYCGSAAESE KESKAVADFI RNHLSSIKAY
310 320 330 340 350
LTIHSYSQMM LYPYSYDYKL PKNNVELNTL AKGAVKKLAS LHGTTYTYGP
360 370 380 390 400
GASTIYPASG GSDDWAYDQG IKYSFTFELR DKGRYGFVLP ESQIQPTCEE
410
TMLAIKYVTS YVLEHLY
Length:417
Mass (Da):47,348
Last modified:March 20, 2007 - v2
Checksum:i923DABC54214CB27
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471T → S AA sequence (PubMed:1057162).Curated
Sequence conflicti353 – 3531S → T AA sequence (PubMed:1057162).Curated

Sequence databases

PIRiA93797. CPBOB.
UniGeneiBt.28370.

Genome annotation databases

EnsembliENSBTAT00000000580; ENSBTAP00000000580; ENSBTAG00000000456.

Cross-referencesi

Sequence databases

PIRiA93797. CPBOB.
UniGeneiBt.28370.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPBX-ray2.80A111-192[»]
B200-416[»]
ProteinModelPortaliP00732.
SMRiP00732. Positions 22-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000580.

Protein family/group databases

MEROPSiM14.003.

Proteomic databases

PaxDbiP00732.
PRIDEiP00732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000580; ENSBTAP00000000580; ENSBTAG00000000456.

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiP00732.
OMAiDVEDESH.
OrthoDBiEOG7RZ5Q9.
TreeFamiTF317197.

Miscellaneous databases

EvolutionaryTraceiP00732.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR003146. M14A_act_pep.
IPR000834. Peptidase_M14.
IPR009020. Propept_inh.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54897. SSF54897. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of taurine cattle: a window to ruminant biology and evolution."
    The bovine genome sequencing and analysis consortium
    Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  2. Cited for: PROTEIN SEQUENCE OF 111-416.
  3. "Primary structure of bovine carboxypeptidase B. Inferences from the locations of the half-cystines and identification of the active site arginine."
    Schmidt J.J., Hirs C.H.W.
    J. Biol. Chem. 249:3756-3764(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 141-203; 241-291; 373-375 AND 402-416.
  4. "Structure of carboxypeptidase B at 2.8-A resolution."
    Schmid M.F., Herriott J.R.
    J. Mol. Biol. 103:175-190(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS.
  5. "Isolation and sequence of peptides at the active center of bovine carboxypeptidase B."
    Plummer T.H. Jr.
    J. Biol. Chem. 244:5246-5253(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SITE, PARTIAL PROTEIN SEQUENCE.
  6. "Identification of a glutamic acid at the active center of bovine carboxypeptidase B."
    Kimmel M.T., Plummer T.H. Jr.
    J. Biol. Chem. 247:7864-7869(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiCBPB1_BOVIN
AccessioniPrimary (citable) accession number: P00732
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 20, 2007
Last modified: July 6, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Chemical modification of Tyr-356 leads to loss of enzyme activity (PubMed:5344132). Chemical modification of Glu-378 leads to loss of enzyme activity (PubMed:4565668).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.