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Q9JHH6

- CBPB2_MOUSE

UniProt

Q9JHH6 - CBPB2_MOUSE

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Protein

Carboxypeptidase B2

Gene

Cpb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.

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
Metal bindingi309 – 3091Zinc; catalyticBy similarity
Sitei323 – 3242Cleavage; by thrombinBy similarity
Active sitei384 – 3841NucleophileBy similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: MGI
  2. metallocarboxypeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. cellular response to glucose stimulus Source: Ensembl
  3. fibrinolysis Source: UniProtKB-KW
  4. liver regeneration Source: Ensembl
  5. negative regulation of fibrinolysis Source: Ensembl
  6. negative regulation of hepatocyte proliferation Source: Ensembl
  7. negative regulation of plasminogen activation Source: Ensembl
  8. positive regulation of extracellular matrix constituent secretion Source: Ensembl
  9. response to drug Source: Ensembl
  10. response to heat Source: Ensembl
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. 3474.

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
Synonyms:Tafi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1891837. Cpb2.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular space Source: Ensembl
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_0000004379Add
BLAST
Chaini114 – 422309Carboxypeptidase B2PRO_0000004380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi72 – 721N-linked (GlcNAc...)1 Publication
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

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9JHH6.
PRIDEiQ9JHH6.

PTM databases

PhosphoSiteiQ9JHH6.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.1 Publication

Gene expression databases

BgeeiQ9JHH6.
CleanExiMM_CPB2.
GenevestigatoriQ9JHH6.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022576.

Structurei

3D structure databases

ProteinModelPortaliQ9JHH6.
SMRiQ9JHH6. Positions 23-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiQ9JHH6.
KOiK01300.
OMAiEIYSWIE.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiQ9JHH6.
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.

Q9JHH6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLHGLGILV AIILYEQHGF AFQSGQVLSA LPRTSRQVQL LQNLTTTYEV
60 70 80 90 100
VLWQPVTAEF IEKKKEVHFF VNASDVDSVK AHLNVSRIPF NVLMNNVEDL
110 120 130 140 150
IEQQTFNDTV SPRASASYYE QYHSLNEIYS WIEVITEQHP DMLQKIYIGS
160 170 180 190 200
SFEKYPLYVL KVSGKEQRIK NAIWIDCGIH AREWISPAFC LWFIGYVTQF
210 220 230 240 250
HGKENLYTRL LRHVDFYIMP VMNVDGYDYT WKKNRMWRKN RSAHKNNRCV
260 270 280 290 300
GTDLNRNFAS KHWCEKGASS SSCSETYCGL YPESEPEVKA VADFLRRNID
310 320 330 340 350
HIKAYISMHS YSQQILFPYS YNRSKSKDHE ELSLVASEAV RAIESINKNT
360 370 380 390 400
RYTHGSGSES LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERYI
410 420
KPTCAEALAA ISKIVWHVIR NT
Length:422
Mass (Da):48,871
Last modified:October 1, 2000 - v1
Checksum:i99113755669D55CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351I → L in AAF00528. 1 PublicationCurated
Sequence conflicti277 – 2771Y → C in AAH89577. (PubMed:15489334)Curated
Sequence conflicti344 – 3463ESI → GSF in AAF00528. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021968 mRNA. Translation: BAB03402.1.
AF164524 mRNA. Translation: AAF62385.1.
AF186188 mRNA. Translation: AAF00528.1.
AK004045 mRNA. Translation: BAB23141.1.
BC089577 mRNA. Translation: AAH89577.1.
CCDSiCCDS27277.1.
RefSeqiNP_062749.2. NM_019775.3.
UniGeneiMm.24242.

Genome annotation databases

EnsembliENSMUST00000022576; ENSMUSP00000022576; ENSMUSG00000021999.
GeneIDi56373.
KEGGimmu:56373.
UCSCiuc007uqq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021968 mRNA. Translation: BAB03402.1 .
AF164524 mRNA. Translation: AAF62385.1 .
AF186188 mRNA. Translation: AAF00528.1 .
AK004045 mRNA. Translation: BAB23141.1 .
BC089577 mRNA. Translation: AAH89577.1 .
CCDSi CCDS27277.1.
RefSeqi NP_062749.2. NM_019775.3.
UniGenei Mm.24242.

3D structure databases

ProteinModelPortali Q9JHH6.
SMRi Q9JHH6. Positions 23-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000022576.

Protein family/group databases

MEROPSi M14.009.

PTM databases

PhosphoSitei Q9JHH6.

Proteomic databases

PaxDbi Q9JHH6.
PRIDEi Q9JHH6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022576 ; ENSMUSP00000022576 ; ENSMUSG00000021999 .
GeneIDi 56373.
KEGGi mmu:56373.
UCSCi uc007uqq.2. mouse.

Organism-specific databases

CTDi 1361.
MGIi MGI:1891837. Cpb2.

Phylogenomic databases

eggNOGi COG2866.
GeneTreei ENSGT00760000119103.
HOGENOMi HOG000252968.
HOVERGENi HBG050815.
InParanoidi Q9JHH6.
KOi K01300.
OMAi EIYSWIE.
OrthoDBi EOG7RZ5Q9.
PhylomeDBi Q9JHH6.
TreeFami TF317197.

Enzyme and pathway databases

BRENDAi 3.4.17.20. 3474.

Miscellaneous databases

NextBioi 312432.
PROi Q9JHH6.
SOURCEi Search...

Gene expression databases

Bgeei Q9JHH6.
CleanExi MM_CPB2.
Genevestigatori Q9JHH6.

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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not."
    Sato T., Miwa T., Akatsu H., Matsukawa N., Obata K., Okada N., Campbell W., Okada H.
    J. Immunol. 165:1053-1058(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of mouse thrombin-activatable fibrinolysis inhibitor."
    Marx P.F., Wagenaar G.T.M., Reijerkerk A., Tiekstra M.J., van Rossum A.G.S.H., Gebbink M.F.G.B., Meijers J.C.M.
    Thromb. Haemost. 83:297-303(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Isolation and characterization of mouse liver carboxypeptidase B gene."
    He Y.C., Broze G.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  5. "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.
  6. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-72.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiCBPB2_MOUSE
AccessioniPrimary (citable) accession number: Q9JHH6
Secondary accession number(s): Q5EBI3, Q9QZF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 105 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3