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UniProtKB - P42210 (ASPR_HORVU)

Entry version 132 (07 Apr 2021)
Sequence version 1 (01 Nov 1995)
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Protein

Phytepsin

Gene
N/A
Organism
Hordeum vulgare (Barley)
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

Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.By similarity

<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

  • Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds. EC:3.4.23.40

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 sitei1021
Active sitei2891

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPS protease database

More...MEROPSi		A01.020

<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:
Phytepsin (EC:3.4.23.40)
Alternative name(s):
Aspartic proteinase
Cleaved into the following 4 chains:
Phytepsin 32 kDa subunit
Phytepsin 29 kDa subunit
Phytepsin 16 kDa subunit
Phytepsin 11 kDa subunit
<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>OrganismiHordeum vulgare (Barley)
<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 identifieri4513 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › Liliopsida › Poales › Poaceae › BOP clade › Pooideae › Triticodae › Triticeae › Hordeinae › Hordeum

<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

Vacuole

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 27Sequence analysisAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002590328 – 66Activation peptideAdd BLAST39
<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_000002590467 – 377Phytepsin 32 kDa subunitAdd BLAST311
ChainiPRO_000002590567 – ?Phytepsin 29 kDa subunit
ChainiPRO_0000025906378 – 508Phytepsin 16 kDa subunitAdd BLAST131
ChainiPRO_0000025907422 – 508Phytepsin 11 kDa subunitAdd BLAST87

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 bondi115 ↔ 121Combined sources1 Publication
Disulfide bondi280 ↔ 284Combined sources1 Publication
Disulfide bondi319 ↔ 413Combined sources1 Publication
Disulfide bondi344 ↔ 385Combined sources1 Publication
Disulfide bondi350 ↔ 382Combined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi399N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi427 ↔ 464Combined sources1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei377 – 378Cleavage2
Sitei421 – 422Cleavage2

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P42210

<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

Embryo and leaf.

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P42210, baseline and differential

<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

Heterodimer of two subunits (29 kDa and 11 kDa) processed from the precursor molecule. A large enzyme (32 kDa and 16 kDa) is an intermediate precursor form.

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

1508
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		P42210

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P42210

<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>Domaini84 – 505Peptidase A1PROSITE-ProRule annotationAdd BLAST422
Domaini314 – 419Saposin B-typePROSITE-ProRule annotationAdd BLAST106

<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

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...CDDi		cd06098, phytepsin, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.70.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001461, Aspartic_peptidase_A1
IPR001969, Aspartic_peptidase_AS
IPR033121, PEPTIDASE_A1
IPR021109, Peptidase_aspartic_dom_sf
IPR033869, Phytepsin
IPR007856, SapB_1
IPR008138, SapB_2
IPR011001, Saposin-like
IPR008139, SaposinB_dom

The PANTHER Classification System

More...PANTHERi		PTHR47966, PTHR47966, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00026, Asp, 1 hit
PF05184, SapB_1, 1 hit
PF03489, SapB_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00792, PEPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00741, SapB, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47862, SSF47862, 1 hit
SSF50630, SSF50630, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00141, ASP_PROTEASE, 2 hits
PS51767, PEPTIDASE_A1, 1 hit
PS50015, SAP_B, 2 hits

<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.

P42210-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGTRGLALAL LAAVLLLQTV LPAASEAEGL VRIALKKRPI DRNSRVATGL 
        60         70         80         90        100
SGGEEQPLLS GANPLRSEEE GDIVALKNYM NAQYFGEIGV GTPPQKFTVI 
       110        120        130        140        150
FDTGSSNLWV PSAKCYFSIA CYLHSRYKAG ASSTYKKNGK PAAIQYGTGS 
       160        170        180        190        200
IAGYFSEDSV TVGDLVVKDQ EFIEATKEPG ITFLVAKFDG ILGLGFKEIS 
       210        220        230        240        250
VGKAVPVWYK MIEQGLVSDP VFSFWLNRHV DEGEGGEIIF GGMDPKHYVG 
       260        270        280        290        300
EHTYVPVTQK GYWQFDMGDV LVGGKSTGFC AGGCAAIADS GTSLLAGPTA 
       310        320        330        340        350
IITEINEKIG AAGVVSQECK TIVSQYGQQI LDLLLAETQP KKICSQVGLC 
       360        370        380        390        400
TFDGTRGVSA GIRSVVDDEP VKSNGLRADP MCSACEMAVV WMQNQLAQNK 
       410        420        430        440        450
TQDLILDYVN QLCNRLPSPM GESAVDCGSL GSMPDIEFTI GGKKFALKPE 
       460        470        480        490        500
EYILKVGEGA AAQCISGFTA MDIPPPRGPL WILGDVFMGP YHTVFDYGKL 

RIGFAKAA
Length:508
Mass (Da):54,226
Last modified:November 1, 1995 - 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:i87F2C9F93369B962
GO

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
X56136 mRNA Translation: CAA39602.1

Protein sequence database of the Protein Information Resource

More...PIRi		S19697

Genome annotation databases

Ensembl plant genome annotation project

More...EnsemblPlantsi		HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1

Gramene; a comparative resource for plants

More...Gramenei		HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:CAA39602

<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
X56136 mRNA Translation: CAA39602.1
PIRiS19697

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
1QDMX-ray2.30A/B/C31-508[»]
SMRiP42210
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiA01.020

Proteomic databases

PRIDEiP42210

Genome annotation databases

EnsemblPlantsiHORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1
GrameneiHORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1
KEGGiag:CAA39602

Miscellaneous databases

EvolutionaryTraceiP42210

Gene expression databases

ExpressionAtlasiP42210, baseline and differential

Family and domain databases

CDDicd06098, phytepsin, 1 hit
Gene3Di2.40.70.10, 1 hit
InterProiView protein in InterPro
IPR001461, Aspartic_peptidase_A1
IPR001969, Aspartic_peptidase_AS
IPR033121, PEPTIDASE_A1
IPR021109, Peptidase_aspartic_dom_sf
IPR033869, Phytepsin
IPR007856, SapB_1
IPR008138, SapB_2
IPR011001, Saposin-like
IPR008139, SaposinB_dom
PANTHERiPTHR47966, PTHR47966, 1 hit
PfamiView protein in Pfam
PF00026, Asp, 1 hit
PF05184, SapB_1, 1 hit
PF03489, SapB_2, 1 hit
PRINTSiPR00792, PEPSIN
SMARTiView protein in SMART
SM00741, SapB, 1 hit
SUPFAMiSSF47862, SSF47862, 1 hit
SSF50630, SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS00141, ASP_PROTEASE, 2 hits
PS51767, PEPTIDASE_A1, 1 hit
PS50015, SAP_B, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiASPR_HORVU
<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: P42210
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 7, 2021
This is version 132 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. Peptidase families
    Classification of peptidase 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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