CPA2 carboxypeptidase A2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: CPA2provided by HGNC
Official Full Name: carboxypeptidase A2provided by HGNC
Primary source: HGNC:HGNC:2297
See related: Ensembl:ENSG00000158516 MIM:600688; AllianceGenome:HGNC:2297
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Summary: Three different forms of human pancreatic procarboxypeptidase A have been isolated. The encoded protein represents the A2 form, which is a monomeric protein with different biochemical properties from the A1 and A3 forms. The A2 form of pancreatic procarboxypeptidase acts on aromatic C-terminal residues and is a secreted protein. [provided by RefSeq, Dec 2008]
Expression: Restricted expression toward pancreas (RPKM 5496.0) See more
Orthologs: all
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Genomic context

Location:: 7q32.2

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2025_08	current	GRCh38.p14 (GCF_000001405.40)	7	NC_000007.14 (130266863..130289798)
RS_2025_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	7	NC_060931.1 (131580250..131603180)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	7	NC_000007.13 (129906703..129929638)

Chromosome 7 - NC_000007.14 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Tissue-specific circular RNA induction during human fetal development
Description: 35 human fetal samples from 6 tissues (3 - 7 replicates per tissue) collected between 10 and 20 weeks gestational time were sequenced using Illumina TruSeq Stranded Total RNA
BioProject: PRJNA270632
Publication: PMID 26076956
Analysis date: Mon Apr 2 22:54:59 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.
Title: Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.
This study showed that CPA2 and CPB1 variants are not associated with chronic pancreatitis.
Title: Variants in pancreatic carboxypeptidase genes CPA2 and CPB1 are not associated with chronic pancreatitis.
CPMG RD data analysis thus allowed a detailed structural characterization of the ADA2h denatured state under folding conditions not previously achieved for this protein.
Title: Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy.
Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.
Title: Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.
Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
we have used one of the best-characterized models for folding and misfolding, the activation domain of procarboxypeptidase A2. The wild type (WT) and three mutants affecting the kinetics of aggregation have been studied by IR from the folded state
Title: Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis.
Observational study of gene-disease association. (HuGE Navigator)
Title: High-density SNP association study and copy number variation analysis of the AUTS1 and AUTS5 loci implicate the IMMP2L-DOCK4 gene region in autism susceptibility.
changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily
Title: Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily.
The high-resolution crystal structure and solution NMR structure of AYEdesign show that the experimentally determined backbone and side-chains conformations are effectively superimposable with the computational model at atomic resolution.
Title: High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design.
NMR structure of the activation domain
Title: NMR solution structure of the activation domain of human procarboxypeptidase A2.

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Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

STS-U19977 (e-PCR)
- UniSTS:74898

D7S2544 (e-PCR), detects polymorphism
- UniSTS:76463

D7S2544 (e-PCR), detects polymorphism
- UniSTS:66514

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables carboxypeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables metallocarboxypeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metallocarboxypeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables metallocarboxypeptidase activity	IEA Inferred from Electronic Annotation more info
enables metallocarboxypeptidase activity	TAS Traceable Author Statement more info	PubMed
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in protein catabolic process in the vacuole	TAS Traceable Author Statement more info	PubMed
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in extracellular region	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular region	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in extracellular region	ISS Inferred from Sequence or Structural Similarity more info
located_in vacuole	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: carboxypeptidase A2

Names: carboxypeptidase A2 (pancreatic)

NP_001860.2

EC 3.4.17.15

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001869.3 → NP_001860.2 carboxypeptidase A2 precursor

See identical proteins and their annotated locations for NP_001860.2

Status: REVIEWED

Source sequence(s)

BC007009, BX106544, CD613167

Consensus CDS

CCDS5817.2

UniProtKB/Swiss-Prot

A4D1M4, C9JIK1, P48052, Q53XS1, Q96A12, Q96QN3, Q9UCF1

UniProtKB/TrEMBL

A0A0S2Z3K5

Related

ENSP00000222481.4, ENST00000222481.9

Conserved Domains (2) summary

cd03870
Location:118 → 417

M14_CPA; Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup

pfam02244
Location:29 → 101

Propep_M14; Carboxypeptidase activation peptide