LOCUS       NP_062749                422 aa            linear   ROD 03-JUN-2024
DEFINITION  carboxypeptidase B2 preproprotein [Mus musculus].
ACCESSION   NP_062749
VERSION     NP_062749.2
DBSOURCE    REFSEQ: accession NM_019775.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Meijers,J.C.M., van der Harst,J., Marx,P.F., Sahbaie,P., Clark,D.J.
            and Morser,J.
  TITLE     Brain Expression of CPB2 and Effects of Cpb2 Deficiency in Mouse
            Models of Behavior
  JOURNAL   Thromb Haemost 124 (1), 4-19 (2024)
   PUBMED   37532120
  REMARK    GeneRIF: Brain Expression of CPB2 and Effects of Cpb2 Deficiency in
            Mouse Models of Behavior.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Zhou,Q., Zhao,L., Shao,Z., Declerck,P., Leung,L.L.K. and Morser,J.
  TITLE     Both plasma basic carboxypeptidases, carboxypeptidase B2 and
            carboxypeptidase N, regulate vascular leakage activity in mice
  JOURNAL   J Thromb Haemost 20 (1), 238-244 (2022)
   PUBMED   34626062
  REMARK    GeneRIF: Both plasma basic carboxypeptidases, carboxypeptidase B2
            and carboxypeptidase N, regulate vascular leakage activity in mice.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Ni,R., Neves,M.A.D., Wu,C., Cerroni,S.E., Flick,M.J., Ni,H.,
            Weitz,J.I., Gross,P.L. and Kim,P.Y.
  TITLE     Activated thrombin-activatable fibrinolysis inhibitor (TAFIa)
            attenuates fibrin-dependent plasmin generation on
            thrombin-activated platelets
  JOURNAL   J Thromb Haemost 18 (9), 2364-2376 (2020)
   PUBMED   32506822
  REMARK    GeneRIF: Activated thrombin-activatable fibrinolysis inhibitor
            (TAFIa) attenuates fibrin-dependent plasmin generation on
            thrombin-activated platelets.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Basu,S., Liang,H.P.H., Hernandez,I., Zogg,M., Fields,B., May,J.,
            Ogoti,Y., Wyseure,T., Mosnier,L.O., Burns,R.T., Carlson,K. and
            Weiler,H.
  TITLE     Role of thrombomodulin expression on hematopoietic stem cells
  JOURNAL   J Thromb Haemost 18 (1), 123-135 (2020)
   PUBMED   31628891
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Wyseure,T., Yang,T., Zhou,J.Y., Cooke,E.J., Wanko,B., Olmer,M.,
            Agashe,R., Morodomi,Y., Behrendt,N., Lotz,M., Morser,J., von
            Drygalski,A. and Mosnier,L.O.
  TITLE     TAFI deficiency causes maladaptive vascular remodeling after
            hemophilic joint bleeding
  JOURNAL   JCI Insight 4 (19), 128379 (2019)
   PUBMED   31465300
  REMARK    GeneRIF: TAFI deficiency causes maladaptive vascular remodeling
            after hemophilic joint bleeding.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Swaisgood,C.M., Schmitt,D., Eaton,D. and Plow,E.F.
  TITLE     In vivo regulation of plasminogen function by plasma
            carboxypeptidase B
  JOURNAL   J Clin Invest 110 (9), 1275-1282 (2002)
   PUBMED   12417566
  REMARK    GeneRIF: role of pCPB as a modulator of the pivotal functions of
            plasminogen in fibrinolysis and cell migration in vivo.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Nagashima,M., Yin,Z.F., Zhao,L., White,K., Zhu,Y., Lasky,N.,
            Halks-Miller,M., Broze,G.J. Jr., Fay,W.P. and Morser,J.
  TITLE     Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is
            compatible with murine life
  JOURNAL   J Clin Invest 109 (1), 101-110 (2002)
   PUBMED   11781355
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Ong,K., Horsfall,W., Conway,E.M. and Schuh,A.C.
  TITLE     Early embryonic expression of murine coagulation system components
  JOURNAL   Thromb Haemost 84 (6), 1023-1030 (2000)
   PUBMED   11154109
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Sato,T., Miwa,T., Akatsu,H., Matsukawa,N., Obata,K., Okada,N.,
            Campbell,W. and Okada,H.
  TITLE     Pro-carboxypeptidase R is an acute phase protein in the mouse,
            whereas carboxypeptidase N is not
  JOURNAL   J Immunol 165 (2), 1053-1058 (2000)
   PUBMED   10878383
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Marx,P.F., Wagenaar,G.T., Reijerkerk,A., Tiekstra,M.J., van
            Rossum,A.G., Gebbink,M.F. and Meijers,J.C.
  TITLE     Characterization of mouse thrombin-activatable fibrinolysis
            inhibitor
  JOURNAL   Thromb Haemost 83 (2), 297-303 (2000)
   PUBMED   10739389
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA048136.1, AK004045.1 and
            CO807338.1.
            
            On Jun 19, 2003 this sequence version replaced NP_062749.1.
            
            Summary: This gene encodes carboxypeptidase B, a zinc-dependent
            metalloprotease that cleaves peptide bonds at the C-terminus of
            protein substrates. The encoded preproprotein undergoes proteolytic
            activation to generate a mature, functional enzyme, and secreted
            into plasma. [provided by RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF164524.1, BC089577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849385, SAMN00849386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 39.73 cM"
     Protein         1..422
                     /product="carboxypeptidase B2 preproprotein"
                     /EC_number="3.4.17.20"
                     /note="carboxypeptidase R; carboxypeptidase B2 (plasma);
                     carboxypeptidase U; thrombin-activable fibrinolysis
                     inhibitor; thrombin-activatable fibrinolysis inhibitor"
                     /calculated_mol_wt=46565
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2324
     Region          28..104
                     /region_name="Propep_M14"
                     /note="Carboxypeptidase activation peptide; pfam02244"
                     /db_xref="CDD:460505"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHH6.1)"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16944957; propagated from
                     UniProtKB/Swiss-Prot (Q9JHH6.1)"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHH6.1)"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHH6.1)"
     mat_peptide     114..422
                     /product="Carboxypeptidase B2. /id=PRO_0000004380"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHH6.1)"
                     /calculated_mol_wt=36037
     Region          118..419
                     /region_name="M14_CPB2"
                     /note="Peptidase M14 carboxypeptidase subfamily A/B-like;
                     Carboxypeptidase B2 subgroup; cd06246"
                     /db_xref="CDD:349465"
     Site            order(180,183,238,255..256,309..310,316,384)
                     /site_type="active"
                     /db_xref="CDD:349465"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHH6.1)"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHH6.1)"
     Site            323..324
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9JHH6.1)"
     CDS             1..422
                     /gene="Cpb2"
                     /gene_synonym="1110032P04Rik; 4930405E17Rik; CPR; Cpu;
                     TAFI"
                     /coded_by="NM_019775.3:69..1337"
                     /db_xref="CCDS:CCDS27277.1"
                     /db_xref="GeneID:56373"
                     /db_xref="MGI:MGI:1891837"
ORIGIN      
        1 mklhglgilv aiilyeqhgf afqsgqvlsa lprtsrqvql lqnltttyev vlwqpvtaef
       61 iekkkevhff vnasdvdsvk ahlnvsripf nvlmnnvedl ieqqtfndtv sprasasyye
      121 qyhslneiys wieviteqhp dmlqkiyigs sfekyplyvl kvsgkeqrik naiwidcgih
      181 arewispafc lwfigyvtqf hgkenlytrl lrhvdfyimp vmnvdgydyt wkknrmwrkn
      241 rsahknnrcv gtdlnrnfas khwcekgass sscsetycgl ypesepevka vadflrrnid
      301 hikayismhs ysqqilfpys ynrskskdhe elslvaseav raiesinknt rythgsgses
      361 lylapggsdd wiydlgikys ftielrdtgr ygfllperyi kptcaealaa iskivwhvir
      421 nt
//
