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Q9JHH6 (CBPB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:Tafi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

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 Ref.2.

Tissue specificity

Plasma; synthesized in the liver. Ref.2

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_0000004379
Chain114 – 422309Carboxypeptidase B2
PRO_0000004380

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...) Ref.6
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

Experimental info

Sequence conflict1351I → L in AAF00528. Ref.3
Sequence conflict2771Y → C in AAH89577. Ref.5
Sequence conflict344 – 3463ESI → GSF in AAF00528. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9JHH6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 99113755669D55CB

FASTA42248,871
        10         20         30         40         50         60 
MKLHGLGILV AIILYEQHGF AFQSGQVLSA LPRTSRQVQL LQNLTTTYEV VLWQPVTAEF 

        70         80         90        100        110        120 
IEKKKEVHFF VNASDVDSVK AHLNVSRIPF NVLMNNVEDL IEQQTFNDTV SPRASASYYE 

       130        140        150        160        170        180 
QYHSLNEIYS WIEVITEQHP DMLQKIYIGS SFEKYPLYVL KVSGKEQRIK NAIWIDCGIH 

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

       250        260        270        280        290        300 
RSAHKNNRCV GTDLNRNFAS KHWCEKGASS SSCSETYCGL YPESEPEVKA VADFLRRNID 

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

       370        380        390        400        410        420 
LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERYI KPTCAEALAA ISKIVWHVIR 


NT

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00310049.
RefSeqNP_062749.2. NM_019775.3.
UniGeneMm.24242.

3D structure databases

ProteinModelPortalQ9JHH6.
SMRQ9JHH6. Positions 23-421.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000022576.

Protein family/group databases

MEROPSM14.009.

PTM databases

PhosphoSiteQ9JHH6.

Proteomic databases

PaxDbQ9JHH6.
PRIDEQ9JHH6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022576; ENSMUSP00000022576; ENSMUSG00000021999.
GeneID56373.
KEGGmmu:56373.
UCSCuc007uqq.2. mouse.

Organism-specific databases

CTD1361.
MGIMGI:1891837. Cpb2.

Phylogenomic databases

eggNOGCOG2866.
GeneTreeENSGT00670000097950.
HOGENOMHOG000252968.
HOVERGENHBG050815.
InParanoidQ9JHH6.
KOK01300.
OMALYPESEP.
OrthoDBEOG4NKBVH.

Enzyme and pathway databases

BRENDA3.4.17.20. 3474.

Gene expression databases

BgeeQ9JHH6.
CleanExMM_CPB2.
GenevestigatorQ9JHH6.
GermOnlineENSMUSG00000021999. Mus musculus.

Family and domain databases

Gene3D3.30.70.340. 1 hit.
InterProIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
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

NextBio312432.
SOURCESearch...

Entry information

Entry nameCBPB2_MOUSE
AccessionPrimary (citable) accession number: Q9JHH6
Secondary accession number(s): Q5EBI3, Q9QZF0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: October 1, 2000
Last modified: April 3, 2013
This is version 93 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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