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P00730

- CBPA1_BOVIN

UniProt

P00730 - CBPA1_BOVIN

Protein

Carboxypeptidase A1

Gene

CPA1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (01 Nov 1991)
      Previous versions | rss
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    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

    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

    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 – 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.
    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.
    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

    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:
    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: October 1, 2014
    This is version 142 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