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    CPA2 carboxypeptidase A2 [ Homo sapiens (human) ]

    Gene ID: 1358, updated on 28-Oct-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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    See CPA2 in Genome Data Viewer
    Location:
    7q32.2
    Exon count:
    11
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 7 NC_000007.14 (130266863..130289798)
    RS_2024_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_000007.14Genomic 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 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. Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2. Reverter D, et al. FEBS Lett, 1997 Dec 22. PMID 9450539
    2. NMR solution structure of the activation domain of human procarboxypeptidase A2. Jiménez MA, et al. Protein Sci, 2003 Feb. PMID 12538893, Free PMC Article
    3. 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
    4. The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. García-Sáez I, et al. EMBO J, 1997 Dec 1. PMID 9384570, Free PMC Article
    5. 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

    See all (26) 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_2024_08

    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

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