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P00730 (CBPA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 139. 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 A1

EC=3.4.17.1
Gene names
Name:CPA1
Synonyms:CPA
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro By similarity.

Catalytic activity

Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Monomer. The zymogen is secreted as a ternary complex composed of procarboxypeptidase A, chymotrypsinogen C and proproteinase E.

Subcellular location

Secretedextracellular space.

Tissue specificity

Pancreas. Ref.8

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   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 space

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 – 1616 Ref.5
Propeptide17 – 11094Activation peptide
PRO_0000004343
Chain111 – 419309Carboxypeptidase A1
PRO_0000004344

Regions

Region179 – 1824Substrate binding
Region254 – 2552Substrate binding
Region307 – 3082Substrate binding

Sites

Active site3801Nucleophile
Metal binding1791Zinc; catalytic
Metal binding1821Zinc; catalytic
Metal binding3061Zinc; catalytic
Binding site2371Substrate

Amino acid modifications

Disulfide bond248 ↔ 271

Natural variations

Natural variant2891I → V in allelic variant. Ref.14
Natural variant3381E → A in allelic variant. Ref.14
Natural variant4151L → V in allelic variant. Ref.14

Experimental info

Sequence conflict951S → L AA sequence Ref.5
Sequence conflict1991D → N AA sequence Ref.3
Sequence conflict2031D → N AA sequence Ref.3
Sequence conflict2241D → N AA sequence Ref.3
Sequence conflict2321Q → E AA sequence Ref.3
Sequence conflict2951D → N AA sequence Ref.3

Secondary structure

.......................................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00730 [UniParc].

Last modified November 1, 1991. Version 3.
Checksum: 21B86407B3BFC452

FASTA41947,082
        10         20         30         40         50         60 
MQGLLILSVL LGAALGKEDF VGHQVLRITA ADEAEVQTVK ELEDLEHLQL DFWRGPGQPG 

        70         80         90        100        110        120 
SPIDVRVPFP SLQAVKVFLE AHGIRYRIMI EDVQSLLDEE QEQMFASQSR ARSTNTFNYA 

       130        140        150        160        170        180 
TYHTLDEIYD FMDLLVAEHP QLVSKLQIGR SYEGRPIYVL KFSTGGSNRP AIWIDLGIHS 

       190        200        210        220        230        240 
REWITQATGV WFAKKFTEDY GQDPSFTAIL DSMDIFLEIV TNPDGFAFTH SQNRLWRKTR 

       250        260        270        280        290        300 
SVTSSSLCVG VDANRNWDAG FGKAGASSSP CSETYHGKYA NSEVEVKSIV DFVKDHGNFK 

       310        320        330        340        350        360 
AFLSIHSYSQ LLLYPYGYTT QSIPDKTELN QVAKSAVEAL KSLYGTSYKY GSIITTIYQA 

       370        380        390        400        410 
SGGSIDWSYN QGIKYSFTFE LRDTGRYGFL LPASQIIPTA QETWLGVLTI MEHTLNNLY 

« Hide

References

[1]"Cloning and nucleotide sequence of a bovine pancreatic preprocarboxypeptidase A cDNA."
le Hueerou I., Guilloteau P., Toullec R., Puigserver A., Wicker C.
Biochem. Biophys. Res. Commun. 175:110-116(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Cloning, sequencing and expression of the gene encoding a major allotypic preprocarboxypeptidase A from bovine pancreas."
Goo J.H., Kim K.H., Choi K.Y.
Gene 165:333-334(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[3]"Amino acid sequence of bovine carboxypeptidase A. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F-I."
Bradshaw R.A., Walsh K.A., Neurath H.
Biochemistry 10:938-950(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 111-417.
[4]"Characterization of bovine carboxypeptidase A (Allan)."
Petra P.H., Hermodson M.A., Walsh K.A., Neurath H.
Biochemistry 10:4023-4025(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 138 AND 141.
[5]"The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A."
Wade R.D., Hass G.M., Kumar S., Walsh K.A., Neurath H.
Biochimie 70:1137-1142(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-120.
[6]"Refined crystal structure of carboxypeptidase A at 1.54-A resolution."
Rees D.C., Lewis M., Lipscomb W.N.
J. Mol. Biol. 168:367-387(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
[7]"High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate."
Teplyakov A., Wilson K.S., Orioli P., Mangani S.
Acta Crystallogr. D 49:534-540(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 111-417 IN COMPLEX WITH ZINC IONS AND SUBSTRATE ANALOG.
[8]"The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C."
Gomis-Rueth F.-X., Gomez M., Bode W., Huber R., Aviles F.X.
EMBO J. 14:4387-4394(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH CPA1 AND CTRC, TISSUE SPECIFICITY.
[9]"Carboxypeptidase A: native, zinc-removed and mercury-replaced forms."
Greenblatt H.M., Feinberg H., Tucker P.A., Shoham G.
Acta Crystallogr. D 54:289-305(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 111-419 OF APOENZYME AND IN COMPLEX WITH ZINC IONS.
[10]"Crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 A -- inhibitor-induced conformational changes."
van Aalten D.M.F., Chong C.R., Joshua-Tor L.
Biochemistry 39:10082-10089(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 111-417 IN COMPLEX WITH ZINC IONS AND INHIBITOR.
[11]"Insight into the stereochemistry in the inhibition of carboxypeptidase A with N-(hydroxyaminocarbonyl)phenylalanine: binding modes of an enantiomeric pair of the inhibitor to carboxypeptidase A."
Cho J.H., Kim D.H., Chung S.J., Ha N.-C., Oh B.-H., Yong Choi K.
Bioorg. Med. Chem. 10:2015-2022(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 111-417 IN COMPLEX WITH ZINC IONS AND SUBSTRATE ANALOG.
[12]"Sulfamide-based inhibitors for carboxypeptidase A. Novel type transition state analogue inhibitors for zinc proteases."
Park J.D., Kim D.H., Kim S.-J., Woo J.-R., Ryu S.E.
J. Med. Chem. 45:5295-5302(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 111-417 IN COMPLEX WITH ZINC IONS AND SUBSTRATE ANALOG.
[13]"Refined structure of bovine carboxypeptidase A at 1.25 A resolution."
Kilshtain-Vardi A., Glick M., Greenblatt H.M., Goldblum A., Shoham G.
Acta Crystallogr. D 59:323-333(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 111-417 IN COMPLEX WITH ZINC IONS.
[14]"Identification of the amino acid replacements characterizing the allotypic forms of bovine carboxypeptidase A."
Petra P.H., Bradshaw R.A., Walsh K.A., Neurath H.
Biochemistry 8:2762-2768(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALLELIC VAL-289; ALA-338 AND VAL-415.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61851 mRNA. Translation: AAA30426.1.
Z33906 mRNA. Translation: CAA83955.1.
PIRCPBOA. JN0126.
RefSeqNP_777175.1. NM_174750.2.
UniGeneBt.4052.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ARLX-ray1.88A111-417[»]
1ARMX-ray1.76A111-419[»]
1BAVX-ray1.60A/B/C/D111-419[»]
1CBXX-ray2.00A111-417[»]
1CPSX-ray2.25A111-417[»]
1CPXX-ray2.00A111-417[»]
1EE3X-ray1.70P111-419[»]
1ELLX-ray1.76P111-419[»]
1ELMX-ray2.00P111-419[»]
1F57X-ray1.75A111-417[»]
1HDQX-ray2.30A111-417[»]
1HDUX-ray1.75A/B/D/E111-417[»]
1HEEX-ray1.75A/B/D/E111-417[»]
1IY7X-ray2.00A111-417[»]
1M4LX-ray1.25A111-417[»]
1PYTX-ray2.35A17-110[»]
B111-419[»]
1YMEX-ray1.53A111-419[»]
1ZLHX-ray1.70A111-419[»]
2ABZX-ray2.16A/B111-419[»]
2CTBX-ray1.50A111-417[»]
2CTCX-ray1.40A111-417[»]
2RFHX-ray1.70A111-417[»]
3CPAX-ray2.00A111-417[»]
3FVLX-ray1.85A/C/E111-417[»]
3FX6X-ray1.85A/C/E111-417[»]
3I1UX-ray1.39A111-419[»]
3KGQX-ray1.70A111-419[»]
4CPAX-ray2.50A/B111-417[»]
5CPAX-ray1.54A111-417[»]
6CPAX-ray2.00A111-417[»]
7CPAX-ray2.00A111-417[»]
8CPAX-ray2.00A111-417[»]
ProteinModelPortalP00730.
SMRP00730. Positions 17-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-44716N.
MINTMINT-1505101.
STRING9913.ENSBTAP00000017727.

Chemistry

BindingDBP00730.
ChEMBLCHEMBL3481.

Protein family/group databases

MEROPSM14.001.

Proteomic databases

PRIDEP00730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID286762.
KEGGbta:286762.

Organism-specific databases

CTD1357.

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000252967.
HOVERGENHBG050815.
KOK08779.

Enzyme and pathway databases

SABIO-RKP00730.

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

EvolutionaryTraceP00730.
NextBio20806424.

Entry information

Entry nameCBPA1_BOVIN
AccessionPrimary (citable) accession number: P00730
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: February 19, 2014
This is version 139 of the entry and version 3 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