CPN1

Protein identityUniProt · HPA

UniProt accession

P15169

Gene

CPN1

Ensembl

ENSG00000120054

Chromosome

10

Canonical length

458 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Predicted secreted proteins

Secretome location

Secreted to blood

OverviewNCBI Gene

Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

458 residues, UniProt reviewed canonical sequence.

>P15169|CPN1
     1  MSDLLSVFLH LLLLFKLVAP VTFRHHRYDD LVRTLYKVQN ECPGITRVYS IGRSVEGRHL
    61  YVLEFSDHPG IHEPLEPEVK YVGNMHGNEA LGRELMLQLS EFLCEEFRNR NQRIVQLIQD
   121  TRIHILPSMN PDGYEVAAAQ GPNKPGYLVG RNNANGVDLN RNFPDLNTYI YYNEKYGGPN
   181  HHLPLPDNWK SQVEPETRAV IRWMHSFNFV LSANLHGGAV VANYPYDKSF EHRVRGVRRT
   241  ASTPTPDDKL FQKLAKVYSY AHGWMFQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
   301  NCFEITLELS CDKFPPEEEL QREWLGNREA LIQFLEQVHQ GIKGMVLDEN YNNLANAVIS
   361  VSGINHDVTS GDHGDYFRLL LPGIYTVSAT APGYDPETVT VTVGPAEPTL VNFHLKRSIP
   421  QVSPVRRAPS RRHGVRAKVQ PQARKKEMEM RQLQRGPA

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against CPN1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.27

Highest tissue expression

73 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about CPN1.

Disease | AllUniProt

Conditions CPN1 is implicated in, by any mechanism.

• Carboxypeptidase N deficiency (CPND) MIM:212070

Disease | GeneticClinVar

2 pathogenic / likely-pathogenic of 67 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Anaphylotoxin inactivator deficiency

Disease | ImmuneIEDB

Conditions an epitope on CPN1 was assayed in.

• melanoma T cell
• hepatitis B T cell

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.06

gnomAD pLI

0

gnomAD missense Z

0.34

DepMap mean gene effect

0

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• bradykinin catabolic process
• peptide metabolic process
• protein catabolic process
• protein processing
• response to glucocorticoid

Molecular functions

• metallocarboxypeptidase activity
• zinc ion binding

Cellular components

• extracellular region
• extracellular space

Protein domainsUniProt · Pfam · InterPro

• Peptidase M14, carboxypeptidase A
• Carboxypeptidase-like, regulatory domain superfamily
• Peptidase M14 domain-containing protein
• Zinc carboxypeptidases, zinc-binding region 1
• Zinc carboxypeptidases, zinc-binding region 2
• Zinc carboxypeptidase
• Carboxypeptidase regulatory-like domain
• Carboxypeptidase N, N-terminal domain

KeywordsUniProt

• Carboxypeptidase
• Disulfide bond
• Glycoprotein
• Hydrolase
• Metal-binding
• Metalloprotease
• Protease
• Secreted
• Signal
• Zinc