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Q9JHH6

- CBPB2_MOUSE

UniProt

Q9JHH6 - CBPB2_MOUSE

Protein

Carboxypeptidase B2

Gene

Cpb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    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

    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

    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.
    GeneTreeiENSGT00670000097950.
    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

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    MKLHGLGILV AIILYEQHGF AFQSGQVLSA LPRTSRQVQL LQNLTTTYEV    50
    VLWQPVTAEF IEKKKEVHFF VNASDVDSVK AHLNVSRIPF NVLMNNVEDL 100
    IEQQTFNDTV SPRASASYYE QYHSLNEIYS WIEVITEQHP DMLQKIYIGS 150
    SFEKYPLYVL KVSGKEQRIK NAIWIDCGIH AREWISPAFC LWFIGYVTQF 200
    HGKENLYTRL LRHVDFYIMP VMNVDGYDYT WKKNRMWRKN RSAHKNNRCV 250
    GTDLNRNFAS KHWCEKGASS SSCSETYCGL YPESEPEVKA VADFLRRNID 300
    HIKAYISMHS YSQQILFPYS YNRSKSKDHE ELSLVASEAV RAIESINKNT 350
    RYTHGSGSES LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERYI 400
    KPTCAEALAA ISKIVWHVIR NT 422
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00670000097950.
    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

    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: October 1, 2014
    This is version 103 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