CBPN_MOUSE
ID CBPN_MOUSE Reviewed; 457 AA.
AC Q9JJN5; Q91WM9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Carboxypeptidase N catalytic chain;
DE Short=CPN;
DE EC=3.4.17.3;
DE AltName: Full=Carboxypeptidase N polypeptide 1;
DE AltName: Full=Carboxypeptidase N small subunit;
DE Flags: Precursor;
GN Name=Cpn1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=10878383; DOI=10.4049/jimmunol.165.2.1053;
RA Sato T., Miwa T., Akatsu H., Matsukawa N., Obata K., Okada N., Campbell W.,
RA Okada H.;
RT "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas
RT carboxypeptidase N is not.";
RL J. Immunol. 165:1053-1058(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11342641; DOI=10.4049/jimmunol.166.10.6196;
RA Matthews K.W., Wetsel R.A.;
RT "Characterization of mouse carboxypeptidase N small active subunit gene
RT structure.";
RL J. Immunol. 166:6196-6202(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protects the body from potent vasoactive and inflammatory
CC peptides containing C-terminal Arg or Lys (such as kinins or
CC anaphylatoxins) which are released into the circulation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal basic amino acid, preferentially
CC lysine.; EC=3.4.17.3;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive
CC chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:10878383}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in liver. Also detected in lung,
CC stomach, intestine, spleen and kidney. {ECO:0000269|PubMed:10878383,
CC ECO:0000269|PubMed:11342641}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AB021969; BAB03403.1; -; mRNA.
DR EMBL; AF326477; AAK06821.1; -; mRNA.
DR EMBL; BC014692; AAH14692.1; -; mRNA.
DR CCDS; CCDS29840.1; -.
DR RefSeq; NP_109628.1; NM_030703.2.
DR AlphaFoldDB; Q9JJN5; -.
DR SMR; Q9JJN5; -.
DR BioGRID; 220268; 1.
DR STRING; 10090.ENSMUSP00000026210; -.
DR GlyGen; Q9JJN5; 3 sites.
DR PhosphoSitePlus; Q9JJN5; -.
DR CPTAC; non-CPTAC-3344; -.
DR CPTAC; non-CPTAC-3696; -.
DR MaxQB; Q9JJN5; -.
DR PaxDb; Q9JJN5; -.
DR PeptideAtlas; Q9JJN5; -.
DR PRIDE; Q9JJN5; -.
DR ProteomicsDB; 265683; -.
DR Antibodypedia; 31135; 250 antibodies from 29 providers.
DR DNASU; 93721; -.
DR Ensembl; ENSMUST00000026210; ENSMUSP00000026210; ENSMUSG00000025196.
DR GeneID; 93721; -.
DR KEGG; mmu:93721; -.
DR UCSC; uc008hpa.1; mouse.
DR CTD; 1369; -.
DR MGI; MGI:2135874; Cpn1.
DR VEuPathDB; HostDB:ENSMUSG00000025196; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158235; -.
DR HOGENOM; CLU_006722_1_3_1; -.
DR InParanoid; Q9JJN5; -.
DR OMA; MGDYFRL; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q9JJN5; -.
DR TreeFam; TF315592; -.
DR BRENDA; 3.4.17.3; 3474.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 93721; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9JJN5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9JJN5; protein.
DR Bgee; ENSMUSG00000025196; Expressed in left lobe of liver and 88 other tissues.
DR Genevisible; Q9JJN5; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:MGI.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010815; P:bradykinin catabolic process; ISO:MGI.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR027063; CPN1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF80; PTHR11532:SF80; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..457
FT /note="Carboxypeptidase N catalytic chain"
FT /id="PRO_0000042578"
FT REGION 21..340
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 418..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 400
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 402
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 409
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 42..104
FT /evidence="ECO:0000250"
FT DISULFID 271..311
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT CONFLICT 381
FT /note="L -> LL (in Ref. 3; AAH14692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 51845 MW; E36FEDA7B44FBC8F CRC64;
MPDLPSAFLP LLLLSKFVTP VTFRHHRYDD LVRTLYKVHN QCPDITRLYN IGRSVKGRYL
YVLEFSDYPG IHEPLEPEVK YVGNMHGNEV LGRELLLQLS EFLCEEFRNR NQRILRLIQD
TRIHILPSMN PDGYEVAAAQ GPNMSGYLVG RNNANGVDLN RNFPDLNTYF YYNSKNGGPN
HHLPLPDNWK SQVEPETRAV IQWIRSLNFV LSANMHGGAV VANYPYDKSL EHRFRGPHRT
SNSPTPDDEL FQTLAKVYSY AHGWMHQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
NCFEITLELS CDKFPRQEEL QREWLGNREA LIQFLEQVHQ GIKGMVLDEN SNNLTGAVIS
VTGINHDVTS GEHGDYFRLL LPGTYSVTAK APGYDPKTVT VTVGPAGPTV VDFQLKRSSS
QVYPVQRAPG RGQGGRAKQP RTSRKKDPAT KRHRGPA
