Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carboxypeptidase B2

Gene

Cpb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi180 – 1801Zinc; catalyticBy similarity
Metal bindingi183 – 1831Zinc; catalyticBy similarity
Binding sitei238 – 2381SubstrateBy similarity
Metal bindingi309 – 3091Zinc; catalyticBy similarity
Binding sitei362 – 3621SubstrateBy similarity
Active sitei384 – 3841Proton donor/acceptorBy similarity

GO - Molecular functioni

  • carboxypeptidase activity Source: RGD
  • metallocarboxypeptidase activity Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • cellular response to glucose stimulus Source: RGD
  • fibrinolysis Source: RGD
  • liver regeneration Source: RGD
  • negative regulation of fibrinolysis Source: RGD
  • negative regulation of hepatocyte proliferation Source: RGD
  • negative regulation of plasminogen activation Source: RGD
  • positive regulation of extracellular matrix constituent secretion Source: RGD
  • proteolysis Source: RGD
  • response to drug Source: RGD
  • response to heat Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.20. 5301.

Protein family/group databases

MEROPSiM14.009.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Cpb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi71035. Cpb2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 11392Activation peptideBy similarityPRO_0000004381Add
BLAST
Chaini114 – 422309Carboxypeptidase B2PRO_0000004382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence analysis
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi177 ↔ 190By similarity
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi249 ↔ 273By similarity
Disulfide bondi264 ↔ 278By similarity
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence analysis

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei323 – 3242Cleavage; by thrombinBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9EQV9.
PRIDEiQ9EQV9.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

GenevisibleiQ9EQV9. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014909.

Structurei

3D structure databases

ProteinModelPortaliQ9EQV9.
SMRiQ9EQV9. Positions 23-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni180 – 1834Substrate bindingBy similarity
Regioni255 – 2562Substrate bindingBy similarity
Regioni310 – 3112Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiQ9EQV9.
KOiK01300.
OMAiLRRNINH.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiQ9EQV9.
TreeFamiTF317197.

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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EQV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYGLGVLV AIILYEKHGL AFQSGHVLSA LPRTSRQVQL LQNLTTTYEV
60 70 80 90 100
VLWQPVTAEF IEKKKEVHFF VNASDVNSVK AYLNASRIPF NVLMNNVEDL
110 120 130 140 150
IQQQTSNDTV SPRASSSYYE QYHSLNEIYS WIEVITEQHP DMLQKIYIGS
160 170 180 190 200
SYEKYPLYVL KVSGKEHRVK NAIWIDCGIH AREWISPAFC LWFIGYVTQF
210 220 230 240 250
HGKENTYTRL LRHVDFYIMP VMNVDGYDYT WKKNRMWRKN RSVHMNNRCV
260 270 280 290 300
GTDLNRNFAS KHWCEKGASS FSCSETYCGL YPESEPEVKA VADFLRRNIN
310 320 330 340 350
HIKAYISMHS YSQQILFPYS YNRSKSKDHE ELSLVASEAV RAIESINKNT
360 370 380 390 400
RYTHGSGSES LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERFI
410 420
KPTCAEALAA VSKIAWHVIR NS
Length:422
Mass (Da):48,827
Last modified:March 1, 2001 - v1
Checksum:iFFFD32A51A9366C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042598 mRNA. Translation: BAB18617.1.
BC091133 mRNA. Translation: AAH91133.1.
BC107447 mRNA. Translation: AAI07448.1.
RefSeqiNP_446069.1. NM_053617.2.
UniGeneiRn.12572.

Genome annotation databases

EnsembliENSRNOT00000014909; ENSRNOP00000014909; ENSRNOG00000010935.
GeneIDi113936.
KEGGirno:113936.
UCSCiRGD:71035. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042598 mRNA. Translation: BAB18617.1.
BC091133 mRNA. Translation: AAH91133.1.
BC107447 mRNA. Translation: AAI07448.1.
RefSeqiNP_446069.1. NM_053617.2.
UniGeneiRn.12572.

3D structure databases

ProteinModelPortaliQ9EQV9.
SMRiQ9EQV9. Positions 23-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014909.

Protein family/group databases

MEROPSiM14.009.

Proteomic databases

PaxDbiQ9EQV9.
PRIDEiQ9EQV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014909; ENSRNOP00000014909; ENSRNOG00000010935.
GeneIDi113936.
KEGGirno:113936.
UCSCiRGD:71035. rat.

Organism-specific databases

CTDi1361.
RGDi71035. Cpb2.

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiQ9EQV9.
KOiK01300.
OMAiLRRNINH.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiQ9EQV9.
TreeFamiTF317197.

Enzyme and pathway databases

BRENDAi3.4.17.20. 5301.

Miscellaneous databases

NextBioi618052.
PROiQ9EQV9.

Gene expression databases

GenevisibleiQ9EQV9. RN.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiCBPB2_RAT
AccessioniPrimary (citable) accession number: Q9EQV9
Secondary accession number(s): Q3B7V3, Q5BKB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.