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Protein

Carboxypeptidase B2

Gene

Cpb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi180Zinc; catalyticBy similarity1
Metal bindingi183Zinc; catalyticBy similarity1
Binding sitei238SubstrateBy similarity1
Metal bindingi309Zinc; catalyticBy similarity1
Binding sitei362SubstrateBy similarity1
Active sitei384Proton donor/acceptorBy similarity1

GO - Molecular functioni

  • carboxypeptidase activity Source: RGD
  • metallocarboxypeptidase activity Source: GO_Central
  • 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

Keywordsi

Molecular functionCarboxypeptidase, Hydrolase, Metalloprotease, Protease
Biological processBlood coagulation, Fibrinolysis, Hemostasis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.20 5301
ReactomeiR-RNO-2022377 Metabolism of Angiotensinogen to Angiotensins
R-RNO-977606 Regulation of Complement cascade

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi71035 Cpb2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000000438122 – 113Activation peptideBy similarityAdd BLAST92
ChainiPRO_0000004382114 – 422Carboxypeptidase B2Add BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi43N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi84N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi107N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi177 ↔ 190By similarity
Glycosylationi240N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi249 ↔ 273By similarity
Disulfide bondi264 ↔ 278By similarity
Glycosylationi322N-linked (GlcNAc...) asparagineSequence analysis1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei323 – 324Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9EQV9
PRIDEiQ9EQV9

PTM databases

PhosphoSitePlusiQ9EQV9

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

BgeeiENSRNOG00000010935
GenevisibleiQ9EQV9 RN

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014909

Structurei

3D structure databases

ProteinModelPortaliQ9EQV9
SMRiQ9EQV9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 183Substrate bindingBy similarity4
Regioni255 – 256Substrate bindingBy similarity2
Regioni310 – 311Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2650 Eukaryota
COG2866 LUCA
GeneTreeiENSGT00760000119103
HOGENOMiHOG000252968
HOVERGENiHBG050815
InParanoidiQ9EQV9
KOiK01300
OMAiEIYSWIE
OrthoDBiEOG091G0HUI
PhylomeDBiQ9EQV9
TreeFamiTF317197

Family and domain databases

CDDicd06246 M14_CPB2, 1 hit
Gene3Di3.30.70.340, 1 hit
InterProiView protein in InterPro
IPR033849 CPB2
IPR036990 M14A-like_propep
IPR003146 M14A_act_pep
IPR000834 Peptidase_M14
PfamiView protein in Pfam
PF00246 Peptidase_M14, 1 hit
PF02244 Propep_M14, 1 hit
PRINTSiPR00765 CRBOXYPTASEA
SMARTiView protein in SMART
SM00631 Zn_pept, 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

Similar proteinsi

Entry informationi

Entry nameiCBPB2_RAT
AccessioniPrimary (citable) accession number: Q9EQV9
Secondary accession number(s): Q3B7V3, Q5BKB8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 112 of the entry and version 1 of the sequence. See 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

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