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P09955

- CBPB1_PIG

UniProt

P09955 - CBPB1_PIG

Protein

Carboxypeptidase B

Gene

CPB1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 5 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi176 – 1761Zinc
    Metal bindingi179 – 1791Zinc
    Metal bindingi304 – 3041Zinc
    Active sitei356 – 3561
    Active sitei378 – 3781Nucleophile

    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

    Protein family/group databases

    MEROPSiM14.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase B (EC:3.4.17.2)
    Gene namesi
    Name:CPB1
    Synonyms:CPB
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15152 PublicationsAdd
    BLAST
    Propeptidei16 – 11095Activation peptidePRO_0000004373Add
    BLAST
    Chaini111 – 416306Carboxypeptidase BPRO_0000004374Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi173 ↔ 186
    Disulfide bondi245 ↔ 268
    Disulfide bondi259 ↔ 273

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP09955.

    Miscellaneous databases

    PMAP-CutDBP09955.

    Interactioni

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000012464.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 214
    Beta strandi26 – 327
    Helixi35 – 4713
    Beta strandi50 – 578
    Helixi58 – 603
    Beta strandi63 – 719
    Helixi73 – 753
    Helixi76 – 8510
    Beta strandi90 – 956
    Helixi97 – 1037
    Beta strandi116 – 1183
    Helixi122 – 13514
    Turni137 – 1393
    Beta strandi140 – 1478
    Beta strandi153 – 1608
    Beta strandi168 – 1725
    Helixi180 – 19617
    Turni197 – 1993
    Helixi201 – 2099
    Beta strandi211 – 2166
    Helixi220 – 2289
    Beta strandi241 – 2444
    Helixi250 – 2523
    Beta strandi254 – 2574
    Beta strandi260 – 2623
    Beta strandi263 – 2653
    Helixi281 – 29212
    Turni293 – 2964
    Beta strandi297 – 3048
    Beta strandi306 – 3138
    Beta strandi315 – 3184
    Helixi324 – 33916
    Turni340 – 3423
    Beta strandi347 – 3504
    Helixi351 – 3544
    Helixi362 – 3687
    Beta strandi372 – 3787
    Beta strandi382 – 3854
    Helixi391 – 3933
    Helixi394 – 41320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NSAX-ray2.30A41-416[»]
    1PBANMR-A16-96[»]
    1Z5RX-ray1.40A/B/C111-416[»]
    1ZG7X-ray1.75A/B/C111-416[»]
    1ZG8X-ray2.00A/B/C111-416[»]
    1ZG9X-ray2.00A/B/C111-416[»]
    2JEWX-ray1.40A111-416[»]
    2PIYX-ray1.43A/B/C111-416[»]
    2PIZX-ray1.60A/B/C111-416[»]
    2PJ0X-ray1.65A/B/C111-416[»]
    2PJ1X-ray1.64A/B/C111-416[»]
    2PJ2X-ray1.95A/B/C111-416[»]
    2PJ3X-ray1.64A/B/C111-416[»]
    2PJ4X-ray2.00A/B111-416[»]
    2PJ5X-ray1.65A/B/C111-416[»]
    2PJ6X-ray1.60A111-416[»]
    2PJ7X-ray1.77A/B/C111-416[»]
    2PJ8X-ray1.70A/B/C111-416[»]
    2PJ9X-ray1.56A111-416[»]
    2PJAX-ray1.70A/B/C111-416[»]
    2PJBX-ray1.70A/B/C111-416[»]
    2PJCX-ray1.74A/B/C111-416[»]
    3GLJX-ray1.89A16-416[»]
    3WABX-ray2.15A111-416[»]
    3WC5X-ray1.70A111-416[»]
    3WC6X-ray1.65A111-416[»]
    3WC7X-ray1.90A111-416[»]
    ProteinModelPortaliP09955.
    SMRiP09955. Positions 22-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09955.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOGENOMiHOG000252968.
    HOVERGENiHBG050815.
    KOiK01291.

    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.

    P09955-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLAFLILVTV TLASAHHSGE HFEGEKVFRV NVEDENDISL LHELASTRQI    50
    DFWKPDSVTQ IKPHSTVDFR VKAEDILAVE DFLEQNELQY EVLINNLRSV 100
    LEAQFDSRVR TTGHSYEKYN NWETIEAWTK QVTSENPDLI SRTAIGTTFL 150
    GNNIYLLKVG KPGPNKPAIF MDCGFHAREW ISHAFCQWFV REAVLTYGYE 200
    SHMTEFLNKL DFYVLPVLNI DGYIYTWTKN RMWRKTRSTN AGTTCIGTDP 250
    NRNFDAGWCT TGASTDPCDE TYCGSAAESE KETKALADFI RNNLSSIKAY 300
    LTIHSYSQMI LYPYSYDYKL PENNAELNNL AKAAVKELAT LYGTKYTYGP 350
    GATTIYPAAG GSDDWAYDQG IKYSFTFELR DKGRYGFILP ESQIQATCEE 400
    TMLAIKYVTN YVLGHL 416
    Length:416
    Mass (Da):47,381
    Last modified:April 26, 2005 - v5
    Checksum:i5FA7FCED7B45AE6A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401L → E AA sequence (PubMed:2018774)Curated
    Sequence conflicti40 – 401L → E AA sequence (PubMed:4026847)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133775 mRNA. Translation: CAB46991.1.
    PIRiA38354.
    RefSeqiNP_999334.1. NM_214169.1.
    UniGeneiSsc.16048.

    Genome annotation databases

    GeneIDi397341.
    KEGGissc:397341.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133775 mRNA. Translation: CAB46991.1 .
    PIRi A38354.
    RefSeqi NP_999334.1. NM_214169.1.
    UniGenei Ssc.16048.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NSA X-ray 2.30 A 41-416 [» ]
    1PBA NMR - A 16-96 [» ]
    1Z5R X-ray 1.40 A/B/C 111-416 [» ]
    1ZG7 X-ray 1.75 A/B/C 111-416 [» ]
    1ZG8 X-ray 2.00 A/B/C 111-416 [» ]
    1ZG9 X-ray 2.00 A/B/C 111-416 [» ]
    2JEW X-ray 1.40 A 111-416 [» ]
    2PIY X-ray 1.43 A/B/C 111-416 [» ]
    2PIZ X-ray 1.60 A/B/C 111-416 [» ]
    2PJ0 X-ray 1.65 A/B/C 111-416 [» ]
    2PJ1 X-ray 1.64 A/B/C 111-416 [» ]
    2PJ2 X-ray 1.95 A/B/C 111-416 [» ]
    2PJ3 X-ray 1.64 A/B/C 111-416 [» ]
    2PJ4 X-ray 2.00 A/B 111-416 [» ]
    2PJ5 X-ray 1.65 A/B/C 111-416 [» ]
    2PJ6 X-ray 1.60 A 111-416 [» ]
    2PJ7 X-ray 1.77 A/B/C 111-416 [» ]
    2PJ8 X-ray 1.70 A/B/C 111-416 [» ]
    2PJ9 X-ray 1.56 A 111-416 [» ]
    2PJA X-ray 1.70 A/B/C 111-416 [» ]
    2PJB X-ray 1.70 A/B/C 111-416 [» ]
    2PJC X-ray 1.74 A/B/C 111-416 [» ]
    3GLJ X-ray 1.89 A 16-416 [» ]
    3WAB X-ray 2.15 A 111-416 [» ]
    3WC5 X-ray 1.70 A 111-416 [» ]
    3WC6 X-ray 1.65 A 111-416 [» ]
    3WC7 X-ray 1.90 A 111-416 [» ]
    ProteinModelPortali P09955.
    SMRi P09955. Positions 22-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000012464.

    Chemistry

    BindingDBi P09955.
    ChEMBLi CHEMBL4065.

    Protein family/group databases

    MEROPSi M14.003.

    Proteomic databases

    PaxDbi P09955.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397341.
    KEGGi ssc:397341.

    Organism-specific databases

    CTDi 1360.

    Phylogenomic databases

    eggNOGi COG2866.
    HOGENOMi HOG000252968.
    HOVERGENi HBG050815.
    KOi K01291.

    Miscellaneous databases

    EvolutionaryTracei P09955.
    PMAP-CutDB P09955.

    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. "Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme."
      Ventura S., Villegas V., Sterner J., Larson J., Vendrell J., Hershberger C., Aviles F.X.
      J. Biol. Chem. 274:19925-19933(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    2. "Analysis of the activation process of porcine procarboxypeptidase B and determination of the sequence of its activation segment."
      Burgos F.J., Salva M., Villegas V., Soriano F., Mendez E., Aviles F.X.
      Biochemistry 30:4082-4089(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-118.
    3. "Sequential homologies between procarboxypeptidases A and B from porcine pancreas."
      Aviles F.X., Vendrell J., Burgos F.J., Soriano F., Mendez E.
      Biochem. Biophys. Res. Commun. 130:97-103(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 16-53.
    4. "Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity."
      Coll M., Guasch A., Aviles F.X., Huber R.
      EMBO J. 10:1-9(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 16-416.
    5. "Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B."
      Vendrell J., Wider G., Aviles F.X., Wuethrich K.
      Biochemistry 29:7515-7522(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF ACTIVATION PEPTIDE, PROTEIN SEQUENCE OF 16-96.
    6. "The NMR structure of the activation domain isolated from porcine procarboxypeptidase B."
      Vendrell J., Billeter M., Wider G., Aviles F.X., Wuethrich K.
      EMBO J. 10:11-15(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF ACTIVATION PEPTIDE.
    7. "Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B."
      Billeter M., Vendrell J., Wider G., Aviles F.X., Coll M., Guasch A., Huber R., Wuethrich K.
      J. Biomol. NMR 2:1-10(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF ACTIVATION PEPTIDE.

    Entry informationi

    Entry nameiCBPB1_PIG
    AccessioniPrimary (citable) accession number: P09955
    Secondary accession number(s): Q9XSP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 124 of the entry and version 5 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