| Tag | Content |
|---|
| CPLM ID | CPLM-021710 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Carboxypeptidase B2 |
Protein Synonyms/Alias | Carboxypeptidase R; CPR; Carboxypeptidase U; CPU; Thrombin-activable fibrinolysis inhibitor; TAFI |
Gene Name | Cpb2 |
Gene Synonyms/Alias | Tafi |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 348 | RAIESINKNTRYTHG | ubiquitination | [1] | | 401 | LLPERYIKPTCAEAL | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | ACT_SITE 384 384 Nucleophile (By similarity).
METAL 180 180 Zinc; catalytic (By similarity).
METAL 183 183 Zinc; catalytic (By similarity).
METAL 309 309 Zinc; catalytic (By similarity).
CARBOHYD 43 43 N-linked (GlcNAc...) (Potential).
CARBOHYD 72 72 N-linked (GlcNAc...).
CARBOHYD 84 84 N-linked (GlcNAc...) (Potential).
CARBOHYD 107 107 N-linked (GlcNAc...) (Potential).
CARBOHYD 240 240 N-linked (GlcNAc...) (Potential).
CARBOHYD 322 322 N-linked (GlcNAc...) (Potential).
DISULFID 177 190 By similarity.
DISULFID 249 273 By similarity.
DISULFID 264 278 By similarity. |
Keyword | Blood coagulation; Carboxypeptidase; Complete proteome; Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 422 AA |
Protein Sequence | MKLHGLGILV AIILYEQHGF AFQSGQVLSA LPRTSRQVQL LQNLTTTYEV VLWQPVTAEF 60
IEKKKEVHFF VNASDVDSVK AHLNVSRIPF NVLMNNVEDL IEQQTFNDTV SPRASASYYE 120
QYHSLNEIYS WIEVITEQHP DMLQKIYIGS SFEKYPLYVL KVSGKEQRIK NAIWIDCGIH 180
AREWISPAFC LWFIGYVTQF HGKENLYTRL LRHVDFYIMP VMNVDGYDYT WKKNRMWRKN 240
RSAHKNNRCV GTDLNRNFAS KHWCEKGASS SSCSETYCGL YPESEPEVKA VADFLRRNID 300
HIKAYISMHS YSQQILFPYS YNRSKSKDHE ELSLVASEAV RAIESINKNT RYTHGSGSES 360
LYLAPGGSDD WIYDLGIKYS FTIELRDTGR YGFLLPERYI KPTCAEALAA ISKIVWHVIR 420
NT 422 |
Gene Ontology | GO:0005615; C:extracellular space; IEA:Compara. GO:0004180; F:carboxypeptidase activity; IDA:MGI. GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW. GO:0051918; P:negative regulation of fibrinolysis; IEA:Compara. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. GO:0042493; P:response to drug; IEA:Compara. GO:0009408; P:response to heat; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |