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Entry version 119 (05 Dec 2018)
Sequence version 1 (01 Nov 1996)
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Protein

Collagenase ColH

Gene

colH

Organism
Hathewaya histolytica (Clostridium histolyticum)
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

Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (PubMed:3002446). The full-length protein has collagenase activity, while both the 116 kDa and 98 kDa forms act on gelatin (PubMed:7961400). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain is also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). Digestion of collagen requires Ca2+ and is inhibited by EDTA (PubMed:9452493). The activator domain (residues 119-388) and catalytic subdomain (330-601) open and close around substrate allowing digestion when the protein is closed (PubMed:23703618).9 Publications

Miscellaneous

Clostridial collagenases enable the bacteria to infiltrate and colonize host tissue, and contribute to gas gangrene (myonecrosis) pathogenesis.Curated

<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

<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

Protein has several cofactor binding sites:

<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 by EDTA (PubMed:9452493). Inhibited by 1-10-phenanthroline (PubMed:18937627). Inhibited by broad-spectrum zinc metalloprotease inhibitor batimastat (PubMed:28820255). N-aryl mercaptoacetamide-based inhibitors have been isolated that act on clostridial collagenases with submicromolar affinity while having negligibile activity on human collagenases (PubMed:28820255).3 Publications

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

kcat is 0.11 per second on Pz peptide with whole enzyme (PubMed:10217773). kcat is 15.9 per second on FALGPA with a catalytic fragment (residues 41-717) (PubMed:18937627).2 Publications
  1. KM=0.88 mM for Pz peptide (4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg)1 Publication
  2. KM=0.269 mM for furylacryloyl-Leu-Gly-Pro-Ala (FALGPA) with a catalytic fragment (residues 41-717)1 Publication
  3. KM=62 µM for (7-Methoxycoumarin-4-yl)acetyl-Ala-Gly-Pro-Pro-Gly-Pro-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Gly-Arg-NH2 with peptidase fragment (residues 331-721)1 Publication
  1. Vmax=12.1 µmol/min/mg enzyme on FALGPA with a catalytic fragment (residues 41-717)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi421Zinc; catalyticCombined sources1 Publication1
Metal bindingi430Calcium 1Combined sources2 Publications1
Metal bindingi455Zinc; catalytic; via tele nitrogenPROSITE-ProRule annotationCombined sources1 Publication2 Publications1
<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 sitei456PROSITE-ProRule annotation1 Publication1
Metal bindingi459Zinc; catalytic; via tele nitrogenPROSITE-ProRule annotationCombined sources1 Publication2 Publications1
Metal bindingi463Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi467Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi469Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi487Zinc; catalyticCombined sources1 Publication2 Publications1
Metal bindingi725Calcium 2Combined sources1 Publication1
Metal bindingi726Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi753Calcium 2Combined sources1 Publication1
Metal bindingi755Calcium 2Combined sources1 Publication1
Metal bindingi794Calcium 2Combined sources1 Publication1
Metal bindingi814Calcium 3Combined sources1 Publication1
Metal bindingi815Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi842Calcium 3Combined sources1 Publication1
Metal bindingi844Calcium 3Combined sources1 Publication1
Metal bindingi884Calcium 3Combined sources1 Publication1
Metal bindingi908Calcium 4Combined sources1 Publication1
Metal bindingi910Calcium 4Combined sources1 Publication1
Metal bindingi910Calcium 5Combined sources1 Publication1
Metal bindingi912Calcium 5Combined sources1 Publication1
Metal bindingi913Calcium 5Combined sources1 Publication1
Metal bindingi931Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi937Calcium 4Combined sources1 Publication1
Metal bindingi937Calcium 5Combined sources1 Publication1
Metal bindingi938Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi939Calcium 4Combined sources1 Publication1
Metal bindingi939Calcium 5Combined sources1 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei977Collagen-binding1 PublicationBy similarity1

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

  • calcium ion binding Source: UniProtKB
  • collagen binding Source: UniProtKB
  • endopeptidase activity Source: UniProtKB
  • metalloendopeptidase activity Source: UniProtKB
  • tripeptidase activity Source: UniProtKB
  • zinc ion binding 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, Metalloprotease, Protease
Biological processVirulence
LigandCalcium, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M09.003

<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:
Collagenase ColH1 Publication (EC:3.4.24.31 Publication)
Alternative name(s):
Class II collagenase2 Publications
Gelatinase ColH1 Publication
Microbial collagenase
<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:colH1 Publication
<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>OrganismiHathewaya histolytica (Clostridium histolyticum)
<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 identifieri1498 [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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeHathewaya

<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

GO - Cellular componenti

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Widely used for tissue dissociation due to its potent activity on connective tissue.Curated
A mix of ColG and ColH is used for isolation of pancreatic islet cells for subsequent transplantation.2 Publications
A mix of ColG and ColH has been used to allow release of retained placenta in cows and mares, and its use in humans has been proposed.1 Publication
Has been used to anchor otherwise diffusible proteins to the host extracellular matrix. Fusions between the collagen-binding domain (S2B plus S3) and rat epidermal growth factor or human basic fibroblast growth factor (bFGF) were injected subcutaneously into adult male BALB/c-nu mice. The fusion proteins remained at the sites of injection for up to 10 days, and bFGF strongly stimulated fibroblast growth (PubMed:9618531).1 Publication
N-aryl mercaptoacetamide-based inhibitors with submicromolar affinity for clostridial collagenases but negligibile activity on human collagenases have been discovered that may lead to promising anti-infective drugs against Clostridia (PubMed:28820255).1 Publication

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

SANTYL Ointment (Smith and Nephew, Inc.) is indicated for debriding chronic dermal ulcers and severely burned areas. It is unclear which of the collagenases from this bacteria is in the ointment.1 Publication
Xiaflex (Endo Pharmaceuticals, Inc.) is a mix of H.histolytica collagenases (ColG and ColH) used to treat both Dupuytren disease and Peyronie disease. Dupuytren disease is a progressive genetic disorder of pathologic collagen production and deposition under the skin of the hand that causes the fingers to be drawn into the palm, leading to flexion contractures of the joints, which can severely limit hand function. Injections of collagenase may reduce these joint contractures (PubMed:19726771, PubMed:10913202). Peyronie disease (PD) is characterized by a disorganized, excessive deposition of collagen that forms a plaque within the penis. The plaque restricts lengthening on the affected side during erection, which can lead to penile curvature deformity, discomfort and erectile dysfunction, and can eventually lead to psychosocial effects such as depression and relationship difficulties. Studies have shown the clinical efficacy of collagenase injection for reducing penile curvature deformity and PD symptom bother (PubMed:8417217, PubMed:25711400).4 Publications

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>Mutagenesisi426G → V: Loss of activity, in a catalytic fragment (residues 41-717) using FALGPA as substrate. 1 Publication1
Mutagenesisi455H → A: No collagen degradation, about 50% zinc content. 1 Publication1
Mutagenesisi455H → F: No collagen degradation, about 10% zinc content. 1 Publication1
Mutagenesisi456E → D or Q: No collagen degradation, wild-type zinc content. 1 Publication1
Mutagenesisi456E → D: Does not degrade collagen, still binds collagen. 1 Publication1
Mutagenesisi459H → R: No collagen degradation, about 20% zinc content. 1 Publication1
Mutagenesisi479N → A: Wild-type collagen degradation and zinc content. 1 Publication1
Mutagenesisi486E → A or Q: About 15% collagen degradation, wild-type zinc content. KM for PZ peptide is wild-type, kcat decreases 4-fold for Ala-486. 1 Publication1
Mutagenesisi486E → D: About 50% collagen degradation, wild-type zinc content. 1 Publication1
Mutagenesisi487E → A, D or Q: Less than 5% collagen degradation, 20-42% zinc content. KM for PZ peptide is 75%, kcat decreases 20-fold for Gln-487. 1 Publication1
Mutagenesisi487E → H: Slight decrease in inhibition of collagenase activity by an N-aryl mercaptoacetamide-based inhibitor. 1 Publication1
Mutagenesisi491E → A, D or Q: 5 to 12% collagen degradation, 70% to wild-type zinc content. KM for PZ peptide is nearly wild-type, kcat decreases 15-fold for Ala-491. 1 Publication1

<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 – 30Sequence analysisAdd BLAST30
<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_000044354731 – 401 Publication10
<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_501084360541 – 1021Collagenase ColHAdd BLAST981

<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

Upon purification gives rise to 98 kDa, 105 kDa and 116 kDa (full-length) proteins, all of which have the same N-terminus (PubMed:7961400, PubMed:9922257).2 Publications

Keywords - PTMi

Zymogen

<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

11021
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JQWX-ray2.00A/B/C902-1021[»]
3JQXX-ray2.20A/B/C902-1021[»]
4AR1X-ray2.01A331-721[»]
4ARFX-ray1.77A331-721[»]
4JGUX-ray1.42A/B806-900[»]
4U6TX-ray1.76A/B/C/D725-810[»]
4U7KX-ray1.91A/B/C/D/E/F/G/H724-810[»]
5O7EX-ray1.87A331-721[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q46085

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

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SMRi
Q46085

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q46085

<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>Domaini727 – 808PKD 1PROSITE-ProRule annotationAdd BLAST82
Domaini816 – 905PKD 2PROSITE-ProRule annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni41 – 717S1 metalloprotease domain2 PublicationsAdd BLAST677
Regioni41 – 320Activator domain1 PublicationAdd BLAST280
Regioni330 – 601Catalytic subdomain1 PublicationAdd BLAST272
Regioni609 – 721Helper subdomain1 PublicationAdd BLAST113
Regioni718 – 810S2a domain2 PublicationsAdd BLAST93
Regioni811 – 904S2b domain2 PublicationsAdd BLAST94
Regioni905 – 1021S3 collagen-binding domain2 PublicationsAdd BLAST117
Regioni1002 – 1004Collagen-binding1 PublicationBy similarity3

<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 mature protein has 4 domains; a metalloprotease domain (S1, approximately residues 41-717), S2a (718-810, equivalent to PKD 1), S2b (811-904, equivalent to PKD 2) and a collagen-binding domain (S3, 905-1021) (PubMed:9922257, PubMed:9452493). The protein has an elongated shape, which lengthens further in calcium-chelated conditions; calcium-chelation also increases its susceptibility to exogenous proteases (PubMed:23561530). The S1 domain has the collagen hydrolytic activity (PubMed:9452493, PubMed:18937627). The metalloprotease S1 domain is composed of 3 subdomains which together resemble a saddle; an activator domain (residues 41-320), the catalytic peptidase subdomain (330-601) and a helper subdomain (609-721) (PubMed:23703618). Unlike the S2 domain in ColG, upon binding to Ca2+ the midsections of S2a and S2b remain rigid; Ca2+ binding confers thermostability (PubMed:25760606). Ca2+-binding also alters the orientation of the N-terminal linker of S2b so it lies along the long axis of the domain (PubMed:25760606). S3 has collagen-binding activity (PubMed:9452493). The structure of S3 becomes more thermostable when it is bound to Ca2+ (PubMed:23144249). Isolated CBD S3 binds unidirectionally to the C-terminus of the collagen triple helix via a surface cleft (PubMed:23144249).3 Publications6 Publications

<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 M9B family. Collagenase subfamily.2 Publications

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013783 Ig-like_fold
IPR013661 Peptidase_M9_N_dom
IPR002169 Peptidase_M9A/M9B
IPR022409 PKD/Chitinase_dom
IPR000601 PKD_dom
IPR035986 PKD_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01752 Peptidase_M9, 1 hit
PF08453 Peptidase_M9_N, 1 hit
PF00801 PKD, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00931 MICOLLPTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00089 PKD, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49299 SSF49299, 2 hits
SSF49899 SSF49899, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50093 PKD, 2 hits
PS00142 ZINC_PROTEASE, 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.

Q46085-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRKCLSKRL MLAITMATIF TVNSTLPIYA AVDKNNATAA VQNESKRYTV
60 70 80 90 100
SYLKTLNYYD LVDLLVKTEI ENLPDLFQYS SDAKEFYGNK TRMSFIMDEI
110 120 130 140 150
GRRAPQYTEI DHKGIPTLVE VVRAGFYLGF HNKELNEINK RSFKERVIPS
160 170 180 190 200
ILAIQKNPNF KLGTEVQDKI VSATGLLAGN ETAPPEVVNN FTPILQDCIK
210 220 230 240 250
NIDRYALDDL KSKALFNVLA APTYDITEYL RATKEKPENT PWYGKIDGFI
260 270 280 290 300
NELKKLALYG KINDNNSWII DNGIYHIAPL GKLHSNNKIG IETLTEVMKV
310 320 330 340 350
YPYLSMQHLQ SADQIKRHYD SKDAEGNKIP LDKFKKEGKE KYCPKTYTFD
360 370 380 390 400
DGKVIIKAGA RVEEEKVKRL YWASKEVNSQ FFRVYGIDKP LEEGNPDDIL
410 420 430 440 450
TMVIYNSPEE YKLNSVLYGY DTNNGGMYIE PEGTFFTYER EAQESTYTLE
460 470 480 490 500
ELFRHEYTHY LQGRYAVPGQ WGRTKLYDND RLTWYEEGGA ELFAGSTRTS
510 520 530 540 550
GILPRKSIVS NIHNTTRNNR YKLSDTVHSK YGASFEFYNY ACMFMDYMYN
560 570 580 590 600
KDMGILNKLN DLAKNNDVDG YDNYIRDLSS NYALNDKYQD HMQERIDNYE
610 620 630 640 650
NLTVPFVADD YLVRHAYKNP NEIYSEISEV AKLKDAKSEV KKSQYFSTFT
660 670 680 690 700
LRGSYTGGAS KGKLEDQKAM NKFIDDSLKK LDTYSWSGYK TLTAYFTNYK
710 720 730 740 750
VDSSNRVTYD VVFHGYLPNE GDSKNSLPYG KINGTYKGTE KEKIKFSSEG
760 770 780 790 800
SFDPDGKIVS YEWDFGDGNK SNEENPEHSY DKVGTYTVKL KVTDDKGESS
810 820 830 840 850
VSTTTAEIKD LSENKLPVIY MHVPKSGALN QKVVFYGKGT YDPDGSIAGY
860 870 880 890 900
QWDFGDGSDF SSEQNPSHVY TKKGEYTVTL RVMDSSGQMS EKTMKIKITD
910 920 930 940 950
PVYPIGTEKE PNNSKETASG PIVPGIPVSG TIENTSDQDY FYFDVITPGE
960 970 980 990 1000
VKIDINKLGY GGATWVVYDE NNNAVSYATD DGQNLSGKFK ADKPGRYYIH
1010 1020
LYMFNGSYMP YRINIEGSVG R
Length:1,021
Mass (Da):116,377
Last modified:November 1, 1996 - 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:i826F45EFD96F917C
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB014075 Genomic DNA Translation: BAA34542.1
D29981 Genomic DNA Translation: BAA06251.1

Protein sequence database of the Protein Information Resource

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PIRi
I40805

<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
AB014075 Genomic DNA Translation: BAA34542.1
D29981 Genomic DNA Translation: BAA06251.1
PIRiI40805

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JQWX-ray2.00A/B/C902-1021[»]
3JQXX-ray2.20A/B/C902-1021[»]
4AR1X-ray2.01A331-721[»]
4ARFX-ray1.77A331-721[»]
4JGUX-ray1.42A/B806-900[»]
4U6TX-ray1.76A/B/C/D725-810[»]
4U7KX-ray1.91A/B/C/D/E/F/G/H724-810[»]
5O7EX-ray1.87A331-721[»]
ProteinModelPortaliQ46085
SMRiQ46085
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM09.003

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ46085

Family and domain databases

Gene3Di2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013783 Ig-like_fold
IPR013661 Peptidase_M9_N_dom
IPR002169 Peptidase_M9A/M9B
IPR022409 PKD/Chitinase_dom
IPR000601 PKD_dom
IPR035986 PKD_dom_sf
PfamiView protein in Pfam
PF01752 Peptidase_M9, 1 hit
PF08453 Peptidase_M9_N, 1 hit
PF00801 PKD, 2 hits
PRINTSiPR00931 MICOLLPTASE
SMARTiView protein in SMART
SM00089 PKD, 2 hits
SUPFAMiSSF49299 SSF49299, 2 hits
SSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS50093 PKD, 2 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiCOLH_HATHI
<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: Q46085
<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: March 28, 2018
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 119 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 programProkaryotic 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, Pharmaceutical

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
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