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P00730

- CBPA1_BOVIN

UniProt

P00730 - CBPA1_BOVIN

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Protein

Carboxypeptidase A1

Gene

CPA1

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

Zn2+Note: 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 region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Propeptidei17 – 11094Activation peptide1 PublicationPRO_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.6 Publications

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
InParanoidiP00730.
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

        10         20         30         40         50
MQGLLILSVL LGAALGKEDF VGHQVLRITA ADEAEVQTVK ELEDLEHLQL
60 70 80 90 100
DFWRGPGQPG SPIDVRVPFP SLQAVKVFLE AHGIRYRIMI EDVQSLLDEE
110 120 130 140 150
QEQMFASQSR ARSTNTFNYA TYHTLDEIYD FMDLLVAEHP QLVSKLQIGR
160 170 180 190 200
SYEGRPIYVL KFSTGGSNRP AIWIDLGIHS REWITQATGV WFAKKFTEDY
210 220 230 240 250
GQDPSFTAIL DSMDIFLEIV TNPDGFAFTH SQNRLWRKTR SVTSSSLCVG
260 270 280 290 300
VDANRNWDAG FGKAGASSSP CSETYHGKYA NSEVEVKSIV DFVKDHGNFK
310 320 330 340 350
AFLSIHSYSQ LLLYPYGYTT QSIPDKTELN QVAKSAVEAL KSLYGTSYKY
360 370 380 390 400
GSIITTIYQA SGGSIDWSYN QGIKYSFTFE LRDTGRYGFL LPASQIIPTA
410
QETWLGVLTI MEHTLNNLY
Length:419
Mass (Da):47,082
Last modified:November 1, 1991 - v3
Checksum:i21B86407B3BFC452
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951S → L AA sequence (PubMed:3147705)Curated
Sequence conflicti199 – 1991D → N AA sequence (PubMed:5102489)Curated
Sequence conflicti203 – 2031D → N AA sequence (PubMed:5102489)Curated
Sequence conflicti224 – 2241D → N AA sequence (PubMed:5102489)Curated
Sequence conflicti232 – 2321Q → E AA sequence (PubMed:5102489)Curated
Sequence conflicti295 – 2951D → N AA sequence (PubMed:5102489)Curated

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P00730.
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: November 26, 2014
This is version 144 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