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P00730

- CBPA1_BOVIN

UniProt

P00730 - CBPA1_BOVIN

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Protein

Carboxypeptidase A1

Gene
CPA1, CPA
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi179 – 1791Zinc; catalytic
Metal bindingi182 – 1821Zinc; catalytic
Binding sitei237 – 2371Substrate
Metal bindingi306 – 3061Zinc; catalytic
Active sitei380 – 3801Nucleophile

GO - Molecular functioni

  1. metallocarboxypeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP00730.

Protein family/group databases

MEROPSiM14.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase A1 (EC:3.4.17.1)
Gene namesi
Name:CPA1
Synonyms:CPA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Propeptidei17 – 11094Activation peptidePRO_0000004343Add
BLAST
Chaini111 – 419309Carboxypeptidase A1PRO_0000004344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi248 ↔ 271

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP00730.

Expressioni

Tissue specificityi

Pancreas.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-44716N.
MINTiMINT-1505101.
STRINGi9913.ENSBTAP00000017727.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 296
Helixi33 – 408
Turni41 – 433
Helixi46 – 483
Beta strandi51 – 544
Beta strandi63 – 675
Helixi69 – 8113
Beta strandi85 – 917
Helixi93 – 10614
Turni114 – 1163
Beta strandi119 – 1213
Helixi125 – 13814
Turni140 – 1423
Beta strandi143 – 1508
Beta strandi156 – 1627
Beta strandi164 – 1685
Beta strandi171 – 1766
Helixi183 – 19917
Turni200 – 2023
Helixi204 – 2129
Beta strandi214 – 2196
Helixi223 – 2319
Beta strandi244 – 2474
Helixi253 – 2553
Beta strandi257 – 2604
Beta strandi263 – 2675
Beta strandi273 – 2753
Helixi284 – 29613
Beta strandi299 – 3068
Beta strandi311 – 3155
Helixi326 – 34116
Turni342 – 3443
Beta strandi349 – 3524
Helixi353 – 3564
Helixi364 – 3707
Beta strandi375 – 3806
Beta strandi384 – 3874
Helixi388 – 3903
Helixi393 – 3953
Helixi396 – 41621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/E111-414[»]
1HEEX-ray1.75A/B/D/E111-414[»]
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[»]
ProteinModelPortaliP00730.
SMRiP00730. Positions 17-419.

Miscellaneous databases

EvolutionaryTraceiP00730.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 1824Substrate binding
Regioni254 – 2552Substrate binding
Regioni307 – 3082Substrate binding

Sequence similaritiesi

Belongs to the peptidase M14 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
KOiK08779.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[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.

P00730-1 [UniParc]FASTAAdd to Basket

« Hide

MQGLLILSVL LGAALGKEDF VGHQVLRITA ADEAEVQTVK ELEDLEHLQL    50
DFWRGPGQPG SPIDVRVPFP SLQAVKVFLE AHGIRYRIMI EDVQSLLDEE 100
QEQMFASQSR ARSTNTFNYA TYHTLDEIYD FMDLLVAEHP QLVSKLQIGR 150
SYEGRPIYVL KFSTGGSNRP AIWIDLGIHS REWITQATGV WFAKKFTEDY 200
GQDPSFTAIL DSMDIFLEIV TNPDGFAFTH SQNRLWRKTR SVTSSSLCVG 250
VDANRNWDAG FGKAGASSSP CSETYHGKYA NSEVEVKSIV DFVKDHGNFK 300
AFLSIHSYSQ LLLYPYGYTT QSIPDKTELN QVAKSAVEAL KSLYGTSYKY 350
GSIITTIYQA SGGSIDWSYN QGIKYSFTFE LRDTGRYGFL LPASQIIPTA 400
QETWLGVLTI MEHTLNNLY 419
Length:419
Mass (Da):47,082
Last modified:November 1, 1991 - v3
Checksum:i21B86407B3BFC452
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti289 – 2891I → V in allelic variant. 1 Publication
Natural varianti338 – 3381E → A in allelic variant. 1 Publication
Natural varianti415 – 4151L → V in allelic variant. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951S → L AA sequence 1 Publication
Sequence conflicti199 – 1991D → N AA sequence 1 Publication
Sequence conflicti203 – 2031D → N AA sequence 1 Publication
Sequence conflicti224 – 2241D → N AA sequence 1 Publication
Sequence conflicti232 – 2321Q → E AA sequence 1 Publication
Sequence conflicti295 – 2951D → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M61851 mRNA. Translation: AAA30426.1.
Z33906 mRNA. Translation: CAA83955.1.
PIRiJN0126. CPBOA.
RefSeqiNP_777175.1. NM_174750.2.
UniGeneiBt.4052.

Genome annotation databases

GeneIDi286762.
KEGGibta:286762.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M61851 mRNA. Translation: AAA30426.1 .
Z33906 mRNA. Translation: CAA83955.1 .
PIRi JN0126. CPBOA.
RefSeqi NP_777175.1. NM_174750.2.
UniGenei Bt.4052.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ARL X-ray 1.88 A 111-417 [» ]
1ARM X-ray 1.76 A 111-419 [» ]
1BAV X-ray 1.60 A/B/C/D 111-419 [» ]
1CBX X-ray 2.00 A 111-417 [» ]
1CPS X-ray 2.25 A 111-417 [» ]
1CPX X-ray 2.00 A 111-417 [» ]
1EE3 X-ray 1.70 P 111-419 [» ]
1ELL X-ray 1.76 P 111-419 [» ]
1ELM X-ray 2.00 P 111-419 [» ]
1F57 X-ray 1.75 A 111-417 [» ]
1HDQ X-ray 2.30 A 111-417 [» ]
1HDU X-ray 1.75 A/B/D/E 111-414 [» ]
1HEE X-ray 1.75 A/B/D/E 111-414 [» ]
1IY7 X-ray 2.00 A 111-417 [» ]
1M4L X-ray 1.25 A 111-417 [» ]
1PYT X-ray 2.35 A 17-110 [» ]
B 111-419 [» ]
1YME X-ray 1.53 A 111-419 [» ]
1ZLH X-ray 1.70 A 111-419 [» ]
2ABZ X-ray 2.16 A/B 111-419 [» ]
2CTB X-ray 1.50 A 111-417 [» ]
2CTC X-ray 1.40 A 111-417 [» ]
2RFH X-ray 1.70 A 111-417 [» ]
3CPA X-ray 2.00 A 111-417 [» ]
3FVL X-ray 1.85 A/C/E 111-417 [» ]
3FX6 X-ray 1.85 A/C/E 111-417 [» ]
3I1U X-ray 1.39 A 111-419 [» ]
3KGQ X-ray 1.70 A 111-419 [» ]
4CPA X-ray 2.50 A/B 111-417 [» ]
5CPA X-ray 1.54 A 111-417 [» ]
6CPA X-ray 2.00 A 111-417 [» ]
7CPA X-ray 2.00 A 111-417 [» ]
8CPA X-ray 2.00 A 111-417 [» ]
ProteinModelPortali P00730.
SMRi P00730. Positions 17-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-44716N.
MINTi MINT-1505101.
STRINGi 9913.ENSBTAP00000017727.

Chemistry

BindingDBi P00730.
ChEMBLi CHEMBL3481.

Protein family/group databases

MEROPSi M14.001.

Proteomic databases

PRIDEi P00730.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 286762.
KEGGi bta:286762.

Organism-specific databases

CTDi 1357.

Phylogenomic databases

eggNOGi COG2866.
HOGENOMi HOG000252967.
HOVERGENi HBG050815.
KOi K08779.

Enzyme and pathway databases

SABIO-RK P00730.

Miscellaneous databases

EvolutionaryTracei P00730.
NextBioi 20806424.

Family and domain databases

Gene3Di 3.30.70.340. 1 hit.
InterProi IPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view ]
Pfami PF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view ]
PRINTSi PR00765. CRBOXYPTASEA.
SMARTi SM00631. Zn_pept. 1 hit.
[Graphical view ]
SUPFAMi SSF54897. SSF54897. 1 hit.
PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCBPA1_BOVIN
AccessioniPrimary (citable) accession number: P00730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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