Reviewed, UniProtKB/Swiss-Prot Q9JHH6 (CBPB2_MOUSE)

Names and origin

Protein names

Recommended name:
    Carboxypeptidase B2
    EC=3.4.17.20
Alternative name(s):
    Carboxypeptidase U
      Short name=CPU
    Thrombin-activable fibrinolysis inhibitor
      Short name=TAFI
    Carboxypeptidase R
      Short name=CPR

Gene names

Name:	Cpb2
Synonyms:	Tafi

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Catalytic activity	Release of C-terminal Arg and Lys from a polypeptide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted. Ref.2
Tissue specificity	Plasma; synthesized in the liver. Ref.2
Sequence similarities	Belongs to the peptidase M14 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 113	92	Activation peptide By similarity		PRO_0000004379
	Chain	114 – 422	309	Carboxypeptidase B2		PRO_0000004380
Sites
	Active site	384	1	Nucleophile By similarity
	Metal binding	180	1	Zinc By similarity
	Metal binding	183	1	Zinc By similarity
	Metal binding	309	1	Zinc By similarity
Amino acid modifications
	Glycosylation	43	1	N-linked (GlcNAc...) Potential
	Glycosylation	72	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	84	1	N-linked (GlcNAc...) Potential
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Glycosylation	240	1	N-linked (GlcNAc...) Potential
	Glycosylation	322	1	N-linked (GlcNAc...) Potential
	Disulfide bond	177 ↔ 190		By similarity
	Disulfide bond	249 ↔ 273		By similarity
	Disulfide bond	264 ↔ 278		By similarity
Experimental info
	Sequence conflict	135	1	I → L in AAF00528. Ref.3
	Sequence conflict	277	1	Y → C in AAH89577. Ref.5
	Sequence conflict	344 – 346	3	ESI → GSF in AAF00528. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9JHH6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 99113755669D55CB	FASTA	422	48,871
	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

References

	« Hide 'large scale' referencesShow '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: 10878383] [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: 10739389] [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: 16141072] [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: 15489334] [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: 16944957] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-72, MASS SPECTROMETRY. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00310049.
RefSeq	NP_062749.2.
UniGene	Mm.24242
3D structure databases
HSSP	HSSP built from PDB template 1DTD based on UniProtKB P48052.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JHH6.
Protein family/group databases
MEROPS	M14.009.
PTM databases
PhosphoSite	Q9JHH6.
Proteomic databases
PRIDE	Q9JHH6.
Genome annotation databases
Ensembl	ENSMUST00000022576; ENSMUSP00000022576; ENSMUSG00000021999; Mus musculus. [Genome view]
GeneID	56373.
KEGG	mmu:56373.
UCSC	uc007uqq.1. mouse.
Organism-specific databases
CTD	56373.
MGI	MGI:1891837. Cpb2.
Phylogenomic databases
HOGENOM	Q9JHH6.
HOVERGEN	Q9JHH6.
OMA	IGSSYEK.
Enzyme and pathway databases
BRENDA	3.4.17.20. 244.
Gene expression databases
ArrayExpress	Q9JHH6.
Bgee	Q9JHH6.
CleanEx	MM_CPB2.
Genevestigator	Q9JHH6.
GermOnline	ENSMUSG00000021999. Mus musculus.
Family and domain databases
InterPro	IPR000834. Peptidase_M14. IPR003146. Prot_inh_M14A. [Graphical view]
Pfam	PF00246. Peptidase_M14. 1 hit. PF02244. Propep_M14. 1 hit. [Graphical view]
PRINTS	PR00765. CRBOXYPTASEA.
SMART	SM00631. Zn_pept. 1 hit. [Graphical view]
PROSITE	PS00132. CARBOXYPEPT_ZN_1. False negative. PS00133. CARBOXYPEPT_ZN_2. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	312432.
SOURCE	Search...

Entry information

Entry name

CBPB2_MOUSE

Accession

Primary (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:	November 3, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)