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CPA2 carboxypeptidase A2 [ Homo sapiens (human) ]

Gene ID: 1358, updated on 13-Apr-2024

Summary

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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
mouse all
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Genomic context

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Location:
7q32.2
Exon count:
11
Annotation release Status Assembly Chr Location
RS_2023_10 current GRCh38.p14 (GCF_000001405.40) 7 NC_000007.14 (130266863..130289798)
RS_2023_10 current T2T-CHM13v2.0 (GCF_009914755.1) 7 NC_060931.1 (131580250..131603180)
105.20220307 previous assembly GRCh37.p13 (GCF_000001405.25) 7 NC_000007.13 (129906703..129929638)

Chromosome 7 - NC_000007.14Genomic Context describing neighboring genes Neighboring gene transmembrane protein 209 Neighboring gene uncharacterized LOC124901745 Neighboring gene Sharpr-MPRA regulatory region 12451 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr7:129844685-129845484 Neighboring gene serine rich single-pass membrane protein 1 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr7:129912168-129912820 Neighboring gene OCT4-NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr7:129912821-129913472 Neighboring gene Sharpr-MPRA regulatory region 5425 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26652 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr7:129937306-129937806 Neighboring gene carboxypeptidase A4 Neighboring gene uncharacterized LOC105375503 Neighboring gene small nucleolar RNA U13 Neighboring gene small nucleolar RNA U13

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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Related articles in PubMed

  1. Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy. Pustovalova Y, et al. Biochemistry, 2015 Aug 4. PMID 26115097
  2. Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis. Cerdà-Costa N, et al. Biochemistry, 2009 Nov 10. PMID 19817500
  3. High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design. Dantas G, et al. J Mol Biol, 2007 Mar 2. PMID 17196978, Free PMC Article
  4. A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins. Dantas G, et al. J Mol Biol, 2003 Sep 12. PMID 12948494
  5. NMR solution structure of the activation domain of human procarboxypeptidase A2. Jiménez MA, et al. Protein Sci, 2003 Feb. PMID 12538893, Free PMC Article

See all (25) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.
    Title: Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. NMR structure of the activation domain
    Title: NMR solution structure of the activation domain of human procarboxypeptidase A2.
Submit: New GeneRIF Correction

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

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)

See Variation Viewer (GRCh38)

Genotypes

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

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 zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
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
  
Component Evidence Code Pubs
located_in extracellular region IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in extracellular space IBA
Inferred from Biological aspect of Ancestor
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

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)

  1. 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

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000007.14 Reference GRCh38.p14 Primary Assembly

    Range
    130266863..130289798
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060931.1 Alternate T2T-CHM13v2.0

    Range
    131580250..131603180
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P48052.3 GenPept UniProtKB/Swiss-Prot:P48052

Gene LinkOut

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Chemical Information
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