Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P00772 (CELA1_PIG)

Protein

Chymotrypsin-like elastase family member 1

Gene

CELA1

Organism
Sus scrofa (Pig)
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

Acts upon elastin.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa. EC:3.4.21.36

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei71Charge relay system2 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi85Calcium1
Metal bindingi90Calcium; via carbonyl oxygen1
Metal bindingi95Calcium1
Active sitei119Charge relay system1 Publication1
Active sitei214Charge relay system1 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

  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionHydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.36 6170

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.153

<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_and_taxonomy_section">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:
Chymotrypsin-like elastase family member 1 (EC:3.4.21.36)
Alternative name(s):
Elastase-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:CELA1
Synonyms:ELA1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unplaced

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3517

<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 – 16Add BLAST16
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_000002768117 – 26Activation peptide2 Publications10
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002768227 – 266Chymotrypsin-like elastase family member 1Add BLAST240

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 bondi56 ↔ 72PROSITE-ProRule annotation1 Publication
Disulfide bondi153 ↔ 220
Disulfide bondi184 ↔ 200
Disulfide bondi210 ↔ 240

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P00772

PRoteomics IDEntifications database

More...PRIDEi		P00772

<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

Pancreas. Basal layers of the epidermis, hair follicle and sebaceous gland epithelia (at protein level).1 Publication

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P00772 SS

<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_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
SERPINA1P010092EBI-986248,EBI-986224From Homo sapiens.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		1148920, 1 interactor

Database of interacting proteins

More...DIPi		DIP-378N

Protein interaction database and analysis system

More...IntActi		P00772, 1 interactor

Molecular INTeraction database

More...MINTi		P00772

STRING: functional protein association networks

More...STRINGi		9823.ENSSSCP00000026330

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P00772

<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

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P00772

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

More...SMRi		P00772

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00772

<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_and_domains_section">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 – 264Peptidase S1PROSITE-ProRule annotationAdd BLAST238

<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 S1 family. Elastase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3627 Eukaryota
COG5640 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00772

KEGG Orthology (KO)

More...KOi		K01326

Identification of Orthologs from Complete Genome Data

More...OMAi		LYGHSTQ

Database of Orthologous Groups

More...OrthoDBi		EOG091G0DF7

TreeFam database of animal gene trees

More...TreeFami		TF330455

Family and domain databases

Conserved Domains Database

More...CDDi		cd00190 Tryp_SPc, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00089 Trypsin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722 CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494 SSF50494, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P00772-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRLLVVASL VLYGHSTQDF PETNARVVGG TEAQRNSWPS QISLQYRSGS 
        60         70         80         90        100
SWAHTCGGTL IRQNWVMTAA HCVDRELTFR VVVGEHNLNQ NDGTEQYVGV 
       110        120        130        140        150
QKIVVHPYWN TDDVAAGYDI ALLRLAQSVT LNSYVQLGVL PRAGTILANN 
       160        170        180        190        200
SPCYITGWGL TRTNGQLAQT LQQAYLPTVD YAICSSSSYW GSTVKNSMVC 
       210        220        230        240        250
AGGDGVRSGC QGDSGGPLHC LVNGQYAVHG VTSFVSRLGC NVTRKPTVFT 
       260 
RVSAYISWIN NVIASN
Length:266
Mass (Da):28,821
Last modified:April 1, 1988 - 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:iBF07D6855BB50FE2
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 conflicti92D → N AA sequence (PubMed:4578945).Curated1
Sequence conflicti126A → G in BAA00118 (PubMed:3648024).Curated1
Sequence conflicti184C → L in BAA00118 (PubMed:3648024).Curated1
Sequence conflicti204D → N AA sequence (PubMed:4578945).Curated1

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
X04036 Transcribed RNA Translation: CAA27670.1
D00160 mRNA Translation: BAA00118.1

Protein sequence database of the Protein Information Resource

More...PIRi		JS0013 ELPG

NCBI Reference Sequences

More...RefSeqi		NP_998988.1, NM_213823.1
XP_005655631.1, XM_005655574.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Ssc.5575
Ssc.89635

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		396766

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ssc:396766

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04036 Transcribed RNA Translation: CAA27670.1
D00160 mRNA Translation: BAA00118.1
PIRiJS0013 ELPG
RefSeqiNP_998988.1, NM_213823.1
XP_005655631.1, XM_005655574.2
UniGeneiSsc.5575
Ssc.89635

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
1B0EX-ray1.80A27-266[»]
1BMAX-ray1.80A27-266[»]
1BTUX-ray1.60A27-266[»]
1C1MX-ray2.20A27-266[»]
1E34X-ray1.80B27-266[»]
1E35X-ray1.90B27-266[»]
1E36X-ray1.70B27-266[»]
1E37X-ray1.75B27-266[»]
1E38X-ray1.70B27-266[»]
1EAIX-ray2.40A/B27-266[»]
1EASX-ray1.80A27-266[»]
1EATX-ray2.00A27-266[»]
1EAUX-ray2.00A27-266[»]
1ELAX-ray2.00A27-266[»]
1ELBX-ray2.10A27-266[»]
1ELCX-ray1.75A27-266[»]
1ELDX-ray2.00E27-266[»]
1ELEX-ray2.00E27-266[»]
1ELFX-ray1.70A27-266[»]
1ELGX-ray1.65A27-266[»]
1ESAX-ray1.65A27-266[»]
1ESBX-ray2.30A27-266[»]
1ESTX-ray2.50A27-266[»]
1FLEX-ray1.90E27-266[»]
1FZZX-ray1.86A27-266[»]
1GVKX-ray0.94B27-266[»]
1GWAX-ray1.85A27-266[»]
1H9LX-ray1.67B27-266[»]
1HAXX-ray1.60B27-266[»]
1HAYX-ray1.70B27-266[»]
1HAZX-ray1.40B27-266[»]
1HB0X-ray2.05B27-266[»]
1HV7X-ray1.70A27-266[»]
1INCX-ray1.94A27-266[»]
1JIMX-ray2.31A27-266[»]
1L0ZX-ray1.50A27-266[»]
1L1GX-ray1.50A27-266[»]
1LKAX-ray1.70A27-266[»]
1LKBX-ray1.70A27-266[»]
1LVYX-ray1.87A27-266[»]
1MCVX-ray1.80A27-266[»]
1MMJX-ray2.20N27-266[»]
1NESX-ray1.65E27-266[»]
1OKXX-ray2.80A/B27-266[»]
1QGFX-ray1.70A27-266[»]
1QIXX-ray1.90B27-266[»]
1QNJX-ray1.10A27-266[»]
1QR3X-ray1.60E27-266[»]
1UO6X-ray1.65A27-266[»]
1UVOX-ray1.85A27-266[»]
1UVPX-ray1.85A27-266[»]
2A7CX-ray1.65A27-266[»]
2A7JX-ray1.65A27-266[»]
2BB4X-ray1.60A27-266[»]
2BD2X-ray1.70A27-266[»]
2BD3X-ray1.60A27-266[»]
2BD4X-ray1.70A27-266[»]
2BD5X-ray1.80A27-266[»]
2BD7X-ray1.60A27-266[»]
2BD8X-ray1.70A27-266[»]
2BD9X-ray1.90A27-266[»]
2BDAX-ray1.80A27-266[»]
2BDBX-ray1.70A27-266[»]
2BDCX-ray1.80A27-266[»]
2BLOX-ray1.33A27-266[»]
2BLQX-ray1.33A27-266[»]
2CV3X-ray1.90A27-266[»]
2D26X-ray3.30C27-266[»]
2DE8X-ray1.50A27-266[»]
2DE9X-ray1.30A27-266[»]
2ESTX-ray2.50E27-266[»]
2FO9X-ray2.00A27-266[»]
2FOAX-ray1.90A27-266[»]
2FOBX-ray1.90A27-266[»]
2FOCX-ray2.00A27-266[»]
2FODX-ray2.00A27-266[»]
2FOEX-ray2.20A27-266[»]
2FOFX-ray2.20A27-266[»]
2FOGX-ray1.90A27-266[»]
2FOHX-ray1.80A27-266[»]
2G4TX-ray2.15A27-266[»]
2G4UX-ray1.84A27-266[»]
2H1UX-ray1.60A27-266[»]
2IOTX-ray1.60A27-266[»]
2OQUX-ray1.80A27-266[»]
2V0BX-ray1.65A27-266[»]
2V35X-ray1.67A27-266[»]
3E3TX-ray1.60A27-266[»]
3ESTX-ray1.65A27-266[»]
3HGNOther1.65A27-266[»]
3HGPX-ray0.94A27-266[»]
3MNBX-ray1.20A27-266[»]
3MNCX-ray1.12A27-266[»]
3MNSX-ray1.50A27-266[»]
3MNXX-ray1.39A27-266[»]
3MO3X-ray1.80A27-266[»]
3MO6X-ray1.66A27-266[»]
3MO9X-ray2.00A27-266[»]
3MOCX-ray1.82A27-266[»]
3MTYX-ray1.10A27-266[»]
3MU0X-ray1.40A27-266[»]
3MU1X-ray1.74A27-266[»]
3MU4X-ray1.10A27-266[»]
3MU5X-ray1.40A27-266[»]
3MU8X-ray1.55A27-266[»]
3ODDX-ray1.10A27-266[»]
3ODFX-ray1.10A27-266[»]
3UOUX-ray2.00A27-266[»]
4ESTX-ray1.78E27-266[»]
4GVUX-ray1.55A27-266[»]
4YM9X-ray1.80A27-266[»]
5AVDX-ray0.86A27-266[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortaliP00772
SMRiP00772
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1148920, 1 interactor
DIPiDIP-378N
IntActiP00772, 1 interactor
MINTiP00772
STRINGi9823.ENSSSCP00000026330

Chemistry databases

BindingDBiP00772
ChEMBLiCHEMBL3517

Protein family/group databases

MEROPSiS01.153

Proteomic databases

PaxDbiP00772
PRIDEiP00772

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396766
KEGGissc:396766

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1990

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
InParanoidiP00772
KOiK01326
OMAiLYGHSTQ
OrthoDBiEOG091G0DF7
TreeFamiTF330455

Enzyme and pathway databases

BRENDAi3.4.21.36 6170

Miscellaneous databases

EvolutionaryTraceiP00772

Protein Ontology

More...PROi		PR:P00772

Gene expression databases

GenevisibleiP00772 SS

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiCELA1_PIG
<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: P00772
Secondary accession number(s): Q29625
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: December 5, 2018
This is version 182 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 programChordata 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again