Skip Header

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

Atrial natriuretic peptide-converting enzyme

Gene

CORIN

Organism
Homo sapiens (Human)
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

Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide.
Isoform 2: has weaker endopeptidase activity compared to isoform 1.

Miscellaneous

Initially named CORIN due to its abundant expression in the heart.1 Publication

<p>This subsection of the ‘Function’ 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

Inhibited in a dose-dependent manner by non-specific trypsin-like serine protease inhibitors including benzamidine.

<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

  1. KM=1.28 mM for pyroGlu-Phe-Lys-pNA.HCl1 Publication
  2. KM=3.52 mM for pyroGlu-Pro-Arg-pNA.HCl1 Publication
  3. KM=2.95 mM for H-D-Pro-Phe-Arg-pNA.2HCl1 Publication
  4. KM=1.92 mM for Bz-Ile-Glu-(gamma-OR)-Gly-Arg-pNA.HCl1 Publication
  5. KM=16 mM for pyroGlu-Gly-Arg-pNA.HCl1 Publication

    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 sitei843Charge relay systemBy similarity1
    Active sitei892Charge relay systemBy similarity1
    Active sitei985Charge relay system1

    <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

    • serine-type endopeptidase 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 functionHydrolase, Protease, Serine protease

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5578768 Physiological factors

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    S01.019

    <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
    <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:CORIN
    Synonyms:CRN, TMPRSS10
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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
    • UP000005640 <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: Chromosome 4

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000145244.11

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:19012 CORIN

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    605236 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9Y5Q5

    <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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 45CytoplasmicSequence analysisAdd BLAST45
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei46 – 66Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini67 – 1042ExtracellularSequence analysisAdd BLAST976

    Keywords - Cellular componenti

    Cell membrane, Membrane, 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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Pre-eclampsia/eclampsia 5 (PEE5)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA hypertensive disorder of pregnancy characterized by new hypertension (blood pressure 140/90 or greater) presenting after 20 weeks' gestation with clinically relevant proteinuria. It impacts 2 individuals, the mother and her child, both of whom can be severely affected. Preeclampsia is one of the causes of maternal mortality and morbidity worldwide.
    See also OMIM:614595
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_067795317K → E in PEE5. 1 PublicationCorresponds to variant dbSNP:rs387906894EnsemblClinVar.1
    Natural variantiVAR_067797472S → G in PEE5. 1 PublicationCorresponds to variant dbSNP:rs387906895EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi26D → A: Impairs cell membrane targeting; when associated with A-30. 1 Publication1
    Mutagenesisi30M → A: Impairs cell membrane targeting; when associated with A-26. 1 Publication1
    Mutagenesisi134R → A: Does not affect autocatalytic cleavage. 1 Publication1
    Mutagenesisi164R → A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment. 1 Publication1
    Mutagenesisi180R → A: Does not affect autocatalytic cleavage. 1 Publication1
    Mutagenesisi213R → A: Does not affect autocatalytic cleavage. 1 Publication1
    Mutagenesisi239R → A: Does not affect autocatalytic cleavage. 1 Publication1
    Mutagenesisi244R → A: Does not affect autocatalytic cleavage. 1 Publication1
    Mutagenesisi427R → A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment. 1 Publication1
    Mutagenesisi801R → A: Loss of activity towards NPPA. 2 Publications1
    Mutagenesisi985S → A: Loss of activity towards NPPA. 3 Publications1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    10699

    MalaCards human disease database

    More...
    MalaCardsi
    CORIN
    MIMi614595 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000145244

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    275555 Preeclampsia

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA134972424

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CORIN

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    317373348

    <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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000417986? – 801Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragmentCurated
    ChainiPRO_00000886731 – 1042Atrial natriuretic peptide-converting enzymeAdd BLAST1042
    ChainiPRO_00003917651 – 801Atrial natriuretic peptide-converting enzyme, N-terminal propeptideCuratedAdd BLAST801
    ChainiPRO_0000417984165 – 801Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragmentCuratedAdd BLAST637
    ChainiPRO_0000417985428 – 801Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragmentCuratedAdd BLAST374
    ChainiPRO_0000391766802 – 1042Atrial natriuretic peptide-converting enzyme, activated protease fragmentCuratedAdd BLAST241

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi80N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi135N-linked (GlcNAc...) asparagineSequence analysis1
    <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 bondi139 ↔ 199By similarity
    Glycosylationi141N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi147 ↔ 192By similarity
    Disulfide bondi183 ↔ 223By similarity
    Disulfide bondi212 ↔ 256By similarity
    Disulfide bondi216 ↔ 240By similarity
    Glycosylationi231N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi245N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi251N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi269 ↔ 282By similarity
    Disulfide bondi277 ↔ 295By similarity
    Disulfide bondi289 ↔ 304By similarity
    Glycosylationi305N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi306 ↔ 318By similarity
    Disulfide bondi313 ↔ 331By similarity
    Glycosylationi320N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi325 ↔ 340By similarity
    Disulfide bondi342 ↔ 355By similarity
    Disulfide bondi350 ↔ 368By similarity
    Disulfide bondi362 ↔ 377By similarity
    Glycosylationi376N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi379 ↔ 392By similarity
    Disulfide bondi387 ↔ 405By similarity
    Disulfide bondi399 ↔ 414By similarity
    Glycosylationi413N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi446N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi451N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi455 ↔ 518By similarity
    Disulfide bondi463 ↔ 511By similarity
    Glycosylationi469N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi502 ↔ 540By similarity
    Disulfide bondi529 ↔ 570By similarity
    Disulfide bondi533 ↔ 557By similarity
    Glycosylationi567N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi580 ↔ 592By similarity
    Disulfide bondi587 ↔ 605By similarity
    Disulfide bondi599 ↔ 614By similarity
    Disulfide bondi616 ↔ 630By similarity
    Disulfide bondi624 ↔ 643By similarity
    Disulfide bondi637 ↔ 652By similarity
    Glycosylationi651N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi655 ↔ 667By similarity
    Disulfide bondi662 ↔ 680By similarity
    Disulfide bondi674 ↔ 689By similarity
    Glycosylationi697N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi761N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi790 ↔ 912Interchain (between N-terminal propeptide and activated protease fragment chains)1 Publication
    Disulfide bondi828 ↔ 844By similarity
    Disulfide bondi926 ↔ 991By similarity
    Disulfide bondi955 ↔ 970By similarity
    Disulfide bondi981 ↔ 1010By similarity
    Glycosylationi1022N-linked (GlcNAc...) asparagineSequence analysis1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    N-glycosylated; required for processing and activation.2 Publications
    Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Different soluble forms are produced by cleavage and autocatalytic cleavage: Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10, while 160 kDa and 100 kDa soluble fragments are produced by autocatalytic cleavage. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1.
    A disulfide bond links the activated corin protease fragment and the N-terminal propeptide. The disulfide bond also links the activated corin protease fragment with soluble fragments (100 kDa, 160 kDa and 180 kDa fragments).

    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>Sitei164 – 165Cleavage; by autolysis2
    Sitei427 – 428Cleavage; by autolysis2
    Sitei801 – 802CleavageCurated2

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9Y5Q5

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

    More...
    PaxDbi
    Q9Y5Q5

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9Y5Q5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9Y5Q5

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    86472
    86473 [Q9Y5Q5-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9Y5Q5

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q9Y5Q5

    <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 heart. Expressed in heart myocytes. Also expressed in pregnant uterus. Detected in blood, in plasma as well as in serum (at protein level).3 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000145244 Expressed in 118 organ(s), highest expression level in heart

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_CORIN

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9Y5Q5 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9Y5Q5 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA070941

    <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

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    Q9Y5Q5, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000273857

    <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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9Y5Q5

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

    More...
    SMRi
    Q9Y5Q5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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_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>Domaini134 – 259FZ 1PROSITE-ProRule annotationAdd BLAST126
    Domaini268 – 304LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST37
    Domaini305 – 340LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST36
    Domaini341 – 377LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST37
    Domaini378 – 415LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST38
    Domaini450 – 573FZ 2PROSITE-ProRule annotationAdd BLAST124
    Domaini579 – 614LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST36
    Domaini615 – 653LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST39
    Domaini654 – 689LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST36
    Domaini690 – 801SRCRAdd BLAST112
    Domaini802 – 1035Peptidase S1PROSITE-ProRule annotationAdd BLAST234

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi26 – 29DDNN motif4

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The DDNN motif is required for targeting to the cell membrane and enzyme activation.1 Publication

    <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.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3577 Eukaryota
    KOG3627 Eukaryota
    COG5640 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157103

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000060148

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG051079

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9Y5Q5

    KEGG Orthology (KO)

    More...
    KOi
    K09614

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HECVSRD

    Database of Orthologous Groups

    More...
    OrthoDBi
    1314811at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9Y5Q5

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF351678

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00112 LDLa, 7 hits
    cd00190 Tryp_SPc, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.2000.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017052 Corin
    IPR020067 Frizzled_dom
    IPR036790 Frizzled_dom_sf
    IPR036055 LDL_receptor-like_sf
    IPR023415 LDLR_class-A_CS
    IPR002172 LDrepeatLR_classA_rpt
    IPR009003 Peptidase_S1_PA
    IPR017448 SRCR-like_dom
    IPR036772 SRCR-like_dom_sf
    IPR001254 Trypsin_dom
    IPR033116 TRYPSIN_SER

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01392 Fz, 2 hits
    PF00057 Ldl_recept_a, 6 hits
    PF15494 SRCR_2, 1 hit
    PF00089 Trypsin, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF036376 Corin, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00261 LDLRECEPTOR

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00063 FRI, 2 hits
    SM00192 LDLa, 7 hits
    SM00202 SR, 1 hit
    SM00020 Tryp_SPc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50494 SSF50494, 1 hit
    SSF56487 SSF56487, 1 hit
    SSF57424 SSF57424, 7 hits
    SSF63501 SSF63501, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50038 FZ, 2 hits
    PS01209 LDLRA_1, 6 hits
    PS50068 LDLRA_2, 7 hits
    PS00420 SRCR_1, 1 hit
    PS50240 TRYPSIN_DOM, 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>Sequences (2+)i

    <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.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q9Y5Q5-1) [UniParc]FASTAAdd to basket
    Also known as: E1, hE1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MKQSPALAPE ERCRRAGSPK PVLRADDNNM GNGCSQKLAT ANLLRFLLLV
    60 70 80 90 100
    LIPCICALVL LLVILLSYVG TLQKVYFKSN GSEPLVTDGE IQGSDVILTN
    110 120 130 140 150
    TIYNQSTVVS TAHPDQHVPA WTTDASLPGD QSHRNTSACM NITHSQCQML
    160 170 180 190 200
    PYHATLTPLL SVVRNMEMEK FLKFFTYLHR LSCYQHIMLF GCTLAFPECI
    210 220 230 240 250
    IDGDDSHGLL PCRSFCEAAK EGCESVLGMV NYSWPDFLRC SQFRNQTESS
    260 270 280 290 300
    NVSRICFSPQ QENGKQLLCG RGENFLCASG ICIPGKLQCN GYNDCDDWSD
    310 320 330 340 350
    EAHCNCSENL FHCHTGKCLN YSLVCDGYDD CGDLSDEQNC DCNPTTEHRC
    360 370 380 390 400
    GDGRCIAMEW VCDGDHDCVD KSDEVNCSCH SQGLVECRNG QCIPSTFQCD
    410 420 430 440 450
    GDEDCKDGSD EENCSVIQTS CQEGDQRCLY NPCLDSCGGS SLCDPNNSLN
    460 470 480 490 500
    NCSQCEPITL ELCMNLPYNS TSYPNYFGHR TQKEASISWE SSLFPALVQT
    510 520 530 540 550
    NCYKYLMFFS CTILVPKCDV NTGEHIPPCR ALCEHSKERC ESVLGIVGLQ
    560 570 580 590 600
    WPEDTDCSQF PEENSDNQTC LMPDEYVEEC SPSHFKCRSG QCVLASRRCD
    610 620 630 640 650
    GQADCDDDSD EENCGCKERD LWECPSNKQC LKHTVICDGF PDCPDYMDEK
    660 670 680 690 700
    NCSFCQDDEL ECANHACVSR DLWCDGEADC SDSSDEWDCV TLSINVNSSS
    710 720 730 740 750
    FLMVHRAATE HHVCADGWQE ILSQLACKQM GLGEPSVTKL IQEQEKEPRW
    760 770 780 790 800
    LTLHSNWESL NGTTLHELLV NGQSCESRSK ISLLCTKQDC GRRPAARMNK
    810 820 830 840 850
    RILGGRTSRP GRWPWQCSLQ SEPSGHICGC VLIAKKWVLT VAHCFEGREN
    860 870 880 890 900
    AAVWKVVLGI NNLDHPSVFM QTRFVKTIIL HPRYSRAVVD YDISIVELSE
    910 920 930 940 950
    DISETGYVRP VCLPNPEQWL EPDTYCYITG WGHMGNKMPF KLQEGEVRII
    960 970 980 990 1000
    SLEHCQSYFD MKTITTRMIC AGYESGTVDS CMGDSGGPLV CEKPGGRWTL
    1010 1020 1030 1040
    FGLTSWGSVC FSKVLGPGVY SNVSYFVEWI KRQIYIQTFL LN
    Length:1,042
    Mass (Da):116,486
    Last modified:January 11, 2011 - v2
    <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:iA3F1CB8EBB676F78
    GO
    Isoform 2 (identifier: Q9Y5Q5-2) [UniParc]FASTAAdd to basket
    Also known as: E1a, hE1a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: Missing.

    Show »
    Length:1,013
    Mass (Da):113,297
    Checksum:iF4084E8B3AFFFDB8
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A087X1D5A0A087X1D5_HUMAN
    Atrial natriuretic peptide-converti...
    CORIN
    938Annotation score:

    Annotation score:2 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>
    J3KR88J3KR88_HUMAN
    Atrial natriuretic peptide-converti...
    CORIN
    975Annotation score:

    Annotation score:2 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>
    J3KR90J3KR90_HUMAN
    Atrial natriuretic peptide-converti...
    CORIN
    1,005Annotation score:

    Annotation score:2 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>
    E7EQE7E7EQE7_HUMAN
    Atrial natriuretic peptide-converti...
    CORIN
    903Annotation score:

    Annotation score:2 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>
    J3KR83J3KR83_HUMAN
    Atrial natriuretic peptide-converti...
    CORIN
    734Annotation score:

    Annotation score:1 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 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 conflicti854W → R in AAF21966 (PubMed:11082206).Curated1
    Sequence conflicti876K → R in AAF21966 (PubMed:11082206).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03800013C → Y2 PublicationsCorresponds to variant dbSNP:rs2289433Ensembl.1
    Natural variantiVAR_067795317K → E in PEE5. 1 PublicationCorresponds to variant dbSNP:rs387906894EnsemblClinVar.1
    Natural variantiVAR_067796444D → G. Corresponds to variant dbSNP:rs13105608Ensembl.1
    Natural variantiVAR_067797472S → G in PEE5. 1 PublicationCorresponds to variant dbSNP:rs387906895EnsemblClinVar.1
    Natural variantiVAR_038001525H → R3 PublicationsCorresponds to variant dbSNP:rs11934749Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0439521 – 29Missing in isoform 2. CuratedAdd BLAST29

    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
    AF133845 mRNA Translation: AAD31850.1
    AC092597 Genomic DNA No translation available.
    AC104646 Genomic DNA Translation: AAY40991.1
    AC107068 Genomic DNA Translation: AAY40917.1
    EU326305 Genomic DNA Translation: ACA05911.1
    BC110451 mRNA Translation: AAI10452.1
    AF113248 mRNA Translation: AAF21966.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS3477.1 [Q9Y5Q5-1]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001265514.1, NM_001278585.1
    NP_006578.2, NM_006587.3 [Q9Y5Q5-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.518618
    Hs.604887

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000273857; ENSP00000273857; ENSG00000145244 [Q9Y5Q5-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    10699

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:10699

    UCSC genome browser

    More...
    UCSCi
    uc003gxm.5 human [Q9Y5Q5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <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
    AF133845 mRNA Translation: AAD31850.1
    AC092597 Genomic DNA No translation available.
    AC104646 Genomic DNA Translation: AAY40991.1
    AC107068 Genomic DNA Translation: AAY40917.1
    EU326305 Genomic DNA Translation: ACA05911.1
    BC110451 mRNA Translation: AAI10452.1
    AF113248 mRNA Translation: AAF21966.1
    CCDSiCCDS3477.1 [Q9Y5Q5-1]
    RefSeqiNP_001265514.1, NM_001278585.1
    NP_006578.2, NM_006587.3 [Q9Y5Q5-1]
    UniGeneiHs.518618
    Hs.604887

    3D structure databases

    ProteinModelPortaliQ9Y5Q5
    SMRiQ9Y5Q5
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9Y5Q5, 4 interactors
    STRINGi9606.ENSP00000273857

    Protein family/group databases

    MEROPSiS01.019

    PTM databases

    iPTMnetiQ9Y5Q5
    PhosphoSitePlusiQ9Y5Q5

    Polymorphism and mutation databases

    BioMutaiCORIN
    DMDMi317373348

    Proteomic databases

    jPOSTiQ9Y5Q5
    PaxDbiQ9Y5Q5
    PeptideAtlasiQ9Y5Q5
    PRIDEiQ9Y5Q5
    ProteomicsDBi86472
    86473 [Q9Y5Q5-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000273857; ENSP00000273857; ENSG00000145244 [Q9Y5Q5-1]
    GeneIDi10699
    KEGGihsa:10699
    UCSCiuc003gxm.5 human [Q9Y5Q5-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    10699
    DisGeNETi10699
    EuPathDBiHostDB:ENSG00000145244.11

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CORIN

    H-Invitational Database, human transcriptome db

    More...
    H-InvDBi
    HIX0024555
    HGNCiHGNC:19012 CORIN
    HPAiHPA070941
    MalaCardsiCORIN
    MIMi605236 gene
    614595 phenotype
    neXtProtiNX_Q9Y5Q5
    OpenTargetsiENSG00000145244
    Orphaneti275555 Preeclampsia
    PharmGKBiPA134972424

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG3577 Eukaryota
    KOG3627 Eukaryota
    COG5640 LUCA
    GeneTreeiENSGT00940000157103
    HOGENOMiHOG000060148
    HOVERGENiHBG051079
    InParanoidiQ9Y5Q5
    KOiK09614
    OMAiHECVSRD
    OrthoDBi1314811at2759
    PhylomeDBiQ9Y5Q5
    TreeFamiTF351678

    Enzyme and pathway databases

    ReactomeiR-HSA-5578768 Physiological factors

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    CORIN human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    CORIN

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    10699

    Protein Ontology

    More...
    PROi
    PR:Q9Y5Q5

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000145244 Expressed in 118 organ(s), highest expression level in heart
    CleanExiHS_CORIN
    ExpressionAtlasiQ9Y5Q5 baseline and differential
    GenevisibleiQ9Y5Q5 HS

    Family and domain databases

    CDDicd00112 LDLa, 7 hits
    cd00190 Tryp_SPc, 1 hit
    Gene3Di1.10.2000.10, 2 hits
    InterProiView protein in InterPro
    IPR017052 Corin
    IPR020067 Frizzled_dom
    IPR036790 Frizzled_dom_sf
    IPR036055 LDL_receptor-like_sf
    IPR023415 LDLR_class-A_CS
    IPR002172 LDrepeatLR_classA_rpt
    IPR009003 Peptidase_S1_PA
    IPR017448 SRCR-like_dom
    IPR036772 SRCR-like_dom_sf
    IPR001254 Trypsin_dom
    IPR033116 TRYPSIN_SER
    PfamiView protein in Pfam
    PF01392 Fz, 2 hits
    PF00057 Ldl_recept_a, 6 hits
    PF15494 SRCR_2, 1 hit
    PF00089 Trypsin, 1 hit
    PIRSFiPIRSF036376 Corin, 1 hit
    PRINTSiPR00261 LDLRECEPTOR
    SMARTiView protein in SMART
    SM00063 FRI, 2 hits
    SM00192 LDLa, 7 hits
    SM00202 SR, 1 hit
    SM00020 Tryp_SPc, 1 hit
    SUPFAMiSSF50494 SSF50494, 1 hit
    SSF56487 SSF56487, 1 hit
    SSF57424 SSF57424, 7 hits
    SSF63501 SSF63501, 2 hits
    PROSITEiView protein in PROSITE
    PS50038 FZ, 2 hits
    PS01209 LDLRA_1, 6 hits
    PS50068 LDLRA_2, 7 hits
    PS00420 SRCR_1, 1 hit
    PS50240 TRYPSIN_DOM, 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 nameiCORIN_HUMAN
    <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: Q9Y5Q5
    Secondary accession number(s): B0ZBE3
    , Q2TBD2, Q4W5E5, Q4W5G6, Q9UHY2
    <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: April 27, 2001
    Last sequence update: January 11, 2011
    Last modified: January 16, 2019
    This is version 175 of the entry and version 2 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
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    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