Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9EQV9 (CBPB2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase B2
EC=3.4.17.20
Alternative name(s):
Carboxypeptidase R
Short name=CPR
Carboxypeptidase U
Short name=CPU
Thrombin-activable fibrinolysis inhibitor
Short name=TAFI
Gene names
Name:Cpb2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. Ref.1

Catalytic activity

Release of C-terminal Arg and Lys from a polypeptide.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

TAFI/CPB2 is unique among carboxypeptidases in that it spontaneously inactivates with a short half-life, a property that is crucial for its role in controlling blood clot lysis. The zymogen is stabilized by interactions with the activation peptide. Release of the activation peptide increases a dynamic flap mobility and in time this leads to conformational changes that disrupt the catalytic site and expose a cryptic thrombin-cleavage site present at Arg-323 By similarity.

Subcellular location

Secreted.

Tissue specificity

Plasma; synthesized in the liver.

Sequence similarities

Belongs to the peptidase M14 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 11392Activation peptide By similarity
PRO_0000004381
Chain114 – 422309Carboxypeptidase B2
PRO_0000004382

Sites

Active site3841Nucleophile By similarity
Metal binding1801Zinc; catalytic By similarity
Metal binding1831Zinc; catalytic By similarity
Metal binding3091Zinc; catalytic By similarity
Site323 – 3242Cleavage; by thrombin By similarity

Amino acid modifications

Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 190 By similarity
Disulfide bond249 ↔ 273 By similarity
Disulfide bond264 ↔ 278 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9EQV9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: FFFD32A51A9366C8

FASTA42248,827
        10         20         30         40         50         60 
MKLYGLGVLV AIILYEKHGL AFQSGHVLSA LPRTSRQVQL LQNLTTTYEV VLWQPVTAEF 

        70         80         90        100        110        120 
IEKKKEVHFF VNASDVNSVK AYLNASRIPF NVLMNNVEDL IQQQTSNDTV SPRASSSYYE 

       130        140        150        160        170        180 
QYHSLNEIYS WIEVITEQHP DMLQKIYIGS SYEKYPLYVL KVSGKEHRVK NAIWIDCGIH 

       190        200        210        220        230        240 
AREWISPAFC LWFIGYVTQF HGKENTYTRL LRHVDFYIMP VMNVDGYDYT WKKNRMWRKN 

       250        260        270        280        290        300 
RSVHMNNRCV GTDLNRNFAS KHWCEKGASS FSCSETYCGL YPESEPEVKA VADFLRRNIN 

       310        320        330        340        350        360 
HIKAYISMHS YSQQILFPYS YNRSKSKDHE ELSLVASEAV RAIESINKNT RYTHGSGSES 

       370        380        390        400        410        420 
LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERFI KPTCAEALAA VSKIAWHVIR 


NS

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N."
Kato T., Sato T., Matsuo S., Yamamoto T., Campbell W., Hotta N., Okada N., Okada H.
Microbiol. Immunol. 44:719-728(2000) [PubMed: 11021404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB042598 mRNA. Translation: BAB18617.1.
BC091133 mRNA. Translation: AAH91133.1.
BC107447 mRNA. Translation: AAI07448.1.
IPIIPI00190501.
RefSeqNP_446069.1. NM_053617.2.
UniGeneRn.12572.

3D structure databases

ProteinModelPortalQ9EQV9.
SMRQ9EQV9. Positions 23-421.
ModBaseSearch...

Protein family/group databases

MEROPSM14.009.

Proteomic databases

PRIDEQ9EQV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014909; ENSRNOP00000014909; ENSRNOG00000010935.
GeneID113936.
KEGGrno:113936.
UCSCNM_053617. rat.

Organism-specific databases

CTD1361.
RGD71035. Cpb2.

Phylogenomic databases

eggNOGroNOG05617.
GeneTreeENSGT00560000077118.
HOVERGENHBG050815.
InParanoidQ9EQV9.
OMAEIYSWIE.
OrthoDBEOG4NKBVH.
PhylomeDBQ9EQV9.

Gene expression databases

ArrayExpressQ9EQV9.
GenevestigatorQ9EQV9.
GermOnlineENSRNOG00000010935. Rattus norvegicus.

Family and domain databases

InterProIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
Gene3DG3DSA:3.30.70.340. G3DSA:3.30.70.340. 1 hit.
KOK01300.
PfamPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMSSF54897. Prot_inh_propept. 1 hit.
PROSITEPS00132. CARBOXYPEPT_ZN_1. False negative.
PS00133. CARBOXYPEPT_ZN_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio618052.

Entry information

Entry nameCBPB2_RAT
AccessionPrimary (citable) accession number: Q9EQV9
Secondary accession number(s): Q3B7V3, Q5BKB8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents