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Entry version 47 (02 Jun 2021)
Sequence version 1 (16 Nov 2011)
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Protein

Acidic endochitinase Pun g 14, amyloplastic

Gene

PSC

Organism
Punica granatum (Pomegranate)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.PROSITE-ProRule annotation1 Publication EC:3.2.1.14

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity is not affected by addition of 10 mM Ca2+ or removal of Ca2+.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat/KM is 0.119 M(-1)s(-1) for native protein, 0.130 M(-1)s(-1) for native protein with 10 mM Ca2+ and 0.116 M(-1)s(-1) for EDTA-treated protein, using 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (4-MU(GlcNAc)3) as substrate at pH 4.5 and 37 degrees Celsius.1 Publication

      pH dependencei

      Optimum pH is between 2.5 and 5.0. Removal of Ca2+ from the protein by EDTA treatment narrows the pH range to 2.5-3.5.1 Publication

      Temperature dependencei

      Optimum temperature is approximately 45 degrees Celsius. Removal of Ca2+ from the protein by EDTA treatment decreases the optimum temperature to 35 degrees Celsius.1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei153Proton donorPROSITE-ProRule annotation1 Publication1

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      • calcium ion binding Source: UniProtKB
      • chitinase activity Source: UniProtKB

      GO - Biological processi

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionGlycosidase, Hydrolase
      Biological processCarbohydrate metabolism, Chitin degradation, Polysaccharide degradation
      LigandCalcium, Metal-binding

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
      Recommended name:
      Acidic endochitinase Pun g 14, amyloplasticCurated (EC:3.2.1.14PROSITE-ProRule annotation1 PublicationImported)
      Alternative name(s):
      Chitinase III3 Publications
      Pomegranate seed chitinase1 Publication
      Allergen: Pun g 141 Publication
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:PSC1 PublicationImported
      ORF Names:CDL15_Pgr011527Imported
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPunica granatum (Pomegranate)Imported
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri22663 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMyrtalesLythraceaePunica
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000197138 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

      <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

      Keywords - Cellular componenti

      Amyloplast, Plastid

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section is used for proteins that cause an allergic reaction in mammals. We usually specify in which species the protein is allergenic.<p><a href='/help/allergenic_properties' target='_top'>More...</a></p>Allergenic propertiesi

      Causes an allergic reaction in human. Binds to IgE in 19% of 357 patients allergic to pomegranate.1 Publication

      Keywords - Diseasei

      Allergen

      Protein family/group databases

      Allergome; a platform for allergen knowledge

      More...
      Allergomei
      11786, Pun g 14
      12339, Pun g 14.0101

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 26Amyloplast2 PublicationsAdd BLAST26
      <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_501120658127 – 299Acidic endochitinase Pun g 14, amyloplastic2 PublicationsAdd BLAST273

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi46 ↔ 93Combined sources1 Publication
      Disulfide bondi76 ↔ 83Combined sources1 Publication
      Disulfide bondi185 ↔ 216Combined sources1 Publication

      Keywords - PTMi

      Disulfide bond

      <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

      <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

      Highly expressed in seeds and to a lesser extent in the skin of the pomegranate fruit (at protein level). Not expressed in leaves or flesh of the fruit (at protein level).1 Publication

      <p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

      Expressed at all stages of seed germination. Expression decreases markedly from day 1 to day 15 after imbibition.1 Publication

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Monomer.

      1 Publication

      <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

      Secondary structure

      1299
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...
      SMRi
      G1UH28

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      Protein Data Bank in Europe - Knowledge Base

      More...
      PDBe-KBi
      Search...

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 299GH18PROSITE-ProRule annotationAdd BLAST273

      <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Keywords - Domaini

      Transit peptide

      Family and domain databases

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR001223, Glyco_hydro18_cat
      IPR001579, Glyco_hydro_18_chit_AS
      IPR017853, Glycoside_hydrolase_SF

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF00704, Glyco_hydro_18, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF51445, SSF51445, 1 hit

      PROSITE; a protein domain and family database

      More...
      PROSITEi
      View protein in PROSITE
      PS01095, GH18_1, 1 hit
      PS51910, GH18_2, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

      G1UH28-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MAKTLPFSRA LLLSLSILLV ARAISAGDIA IYWGQNGGEG TLASTCDTGR
      60 70 80 90 100
      YAYVIVSFVT TFGNFRAPVV NLAGHCDPAA GTCTGLSDEI RSCQGKDIKV
      110 120 130 140 150
      LMSIGGGAGD YSLVSEADAD NFADYLWNNF LGGQSSSRPL GDAVLDGIDF
      160 170 180 190 200
      DIELGTTTFY DTLARALSSR STQAAKVYLT AAPQCPHPDS HLDAALNTGL
      210 220 230 240 250
      FDNVWIQFYN NPLAQCQYSS GNTNDILSSW NTWTSSTTAG KIFLGLPAAP
      260 270 280 290
      EAAGSGYIPP DVLTGQILPQ IKTSAKYGGV MLYSKFYDTT YSTTIKDQV
      Length:299
      Mass (Da):31,747
      Last modified:November 16, 2011 - v1
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD5D28157AA92D0B1
      GO

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti90I → L AA sequence (PubMed:21790816).Curated1
      Sequence conflicti295I → L AA sequence (PubMed:21790816).Curated1

      <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

      Molecular mass is 29008.70 Da. Determined by MALDI. The measured mass is that of EDTA-treated protein to remove Ca2+.1 Publication
      Molecular mass is 29389.80 Da. Determined by MALDI. The measured mass is that of protein without EDTA-treatment to retain Ca2+.1 Publication
      Molecular mass is 29001.76 Da. Determined by MALDI. The measured mass is that of protein with three disulfide bridges.1 Publication

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      AB605773 mRNA Translation: BAK68869.1
      MTKT01005817 Genomic DNA Translation: OWM64072.1

      <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AB605773 mRNA Translation: BAK68869.1
      MTKT01005817 Genomic DNA Translation: OWM64072.1

      3D structure databases

      Select the link destinations:

      Protein Data Bank Europe

      More...
      PDBei

      Protein Data Bank RCSB

      More...
      RCSB PDBi

      Protein Data Bank Japan

      More...
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      4TOQX-ray1.60A/B/C/D27-299[»]
      SMRiG1UH28
      ModBaseiSearch...
      PDBe-KBiSearch...

      Protein family/group databases

      Allergomei11786, Pun g 14
      12339, Pun g 14.0101

      Family and domain databases

      InterProiView protein in InterPro
      IPR001223, Glyco_hydro18_cat
      IPR001579, Glyco_hydro_18_chit_AS
      IPR017853, Glycoside_hydrolase_SF
      PfamiView protein in Pfam
      PF00704, Glyco_hydro_18, 1 hit
      SUPFAMiSSF51445, SSF51445, 1 hit
      PROSITEiView protein in PROSITE
      PS01095, GH18_1, 1 hit
      PS51910, GH18_2, 1 hit

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCHIT_PUNGR
      <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: G1UH28
      <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 8, 2019
      Last sequence update: November 16, 2011
      Last modified: June 2, 2021
      This is version 47 of the entry and version 1 of the sequence. See complete history.
      <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programPlant Protein Annotation Program

      <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      3D-structure, Direct protein sequencing

      Documents

      1. Glycosyl hydrolases
        Classification of glycosyl hydrolase families and list of entries
      2. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      3. SIMILARITY comments
        Index of protein domains and families
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