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P09955

- CBPB1_PIG

UniProt

P09955 - CBPB1_PIG

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Protein

Carboxypeptidase B

Gene

CPB1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: 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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP09955.
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

        10         20         30         40         50
MLAFLILVTV TLASAHHSGE HFEGEKVFRV NVEDENDISL LHELASTRQI
60 70 80 90 100
DFWKPDSVTQ IKPHSTVDFR VKAEDILAVE DFLEQNELQY EVLINNLRSV
110 120 130 140 150
LEAQFDSRVR TTGHSYEKYN NWETIEAWTK QVTSENPDLI SRTAIGTTFL
160 170 180 190 200
GNNIYLLKVG KPGPNKPAIF MDCGFHAREW ISHAFCQWFV REAVLTYGYE
210 220 230 240 250
SHMTEFLNKL DFYVLPVLNI DGYIYTWTKN RMWRKTRSTN AGTTCIGTDP
260 270 280 290 300
NRNFDAGWCT TGASTDPCDE TYCGSAAESE KETKALADFI RNNLSSIKAY
310 320 330 340 350
LTIHSYSQMI LYPYSYDYKL PENNAELNNL AKAAVKELAT LYGTKYTYGP
360 370 380 390 400
GATTIYPAAG GSDDWAYDQG IKYSFTFELR DKGRYGFILP ESQIQATCEE
410
TMLAIKYVTN YVLGHL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P09955.
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: November 26, 2014
This is version 126 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