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Entry version 103 (07 Apr 2021)
Sequence version 1 (01 Nov 1999)
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Protein

Collagenase ColG

Gene

colG

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). Active on soluble type I collagen, insoluble collagen, azocoll, soluble PZ-peptide (all collagenase substrates) and gelatin (PubMed:9922257). The full-length protein has collagenase activity, while the in vivo derived C-terminally truncated shorter versions only act on gelatin (PubMed:9922257). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain are also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). The activator domain (residues 119-388) and catalytic subdomain (389-670) open and close around substrate using a Gly-rich hinge (387-397), allowing digestion when the protein is closed (PubMed:21947205, PubMed:23703618). Binding of collagen requires Ca2+ and is inhibited by EGTA; the collagen-binding domain (CBD, S3a plus S3b) specifically recognizes the triple-helical conformation made by 3 collagen protein chains in the triple-helical region (PubMed:11121400). Isolated CBD (S3a plus S3b) binds collagen fibrils and sheets of many tissues (PubMed:11913772).11 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%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Inhibited by 1-10-phenanthroline (PubMed:18937627). Inhibited by peptidomimetic isoamyl-phosphonyl-Gly-Pro-Ala, which binds to Zn2+ (PubMed:21947205). 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/sec, using a catalytic fragment (119-790) on an artificial substrate.1 Publication
  1. KM=0.840 mM for furylacryloyl-Leu-Gly-Pro-Ala (FALGPA)1 Publication
  1. Vmax=0.0852 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi498Calcium 11 PublicationBy similarity1
Metal bindingi523Zinc; catalytic; via tele nitrogenPROSITE-ProRule annotationCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei524PROSITE-ProRule annotation1 Publication1
Metal bindingi527Zinc; catalytic; via tele nitrogenPROSITE-ProRule annotationCombined sources2 Publications1
Metal bindingi531Calcium 1; via carbonyl oxygen1 PublicationBy similarity1
Metal bindingi535Calcium 1; via carbonyl oxygen1 PublicationBy similarity1
Metal bindingi537Calcium 1; via carbonyl oxygen1 PublicationBy similarity1
Metal bindingi555Zinc; catalyticCombined sources2 Publications1
Metal bindingi795Calcium 2Combined sources1 Publication1
Metal bindingi796Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi823Calcium 2Combined sources1 Publication1
Metal bindingi825Calcium 2Combined sources1 Publication1
Metal bindingi864Calcium 2Combined sources1 Publication1
Metal bindingi890Calcium 3Combined sources1
Metal bindingi892Calcium 3Combined sources1
Metal bindingi892Calcium 4Combined sources1
Metal bindingi894Calcium 4Combined sources1
Metal bindingi913Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi918Calcium 3Combined sources1
Metal bindingi918Calcium 4Combined sources1
Metal bindingi920Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi921Calcium 3Combined sources1
Metal bindingi921Calcium 4Combined sources1
<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>Sitei1006C-terminus of form C1b1 Publication1
Metal bindingi1009Calcium 5Combined sources2 Publications1
Metal bindingi1011Calcium 5Combined sources2 Publications1
Metal bindingi1011Calcium 6Combined sources2 Publications1
Metal bindingi1013Calcium 6Combined sources2 Publications1
Metal bindingi1014Calcium 6Combined sources2 Publications1
Sitei1018C-terminus of form C1c1 Publication1
Metal bindingi1032Calcium 5; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi1037Calcium 5Combined sources2 Publications1
Metal bindingi1037Calcium 6Combined sources2 Publications1
Metal bindingi1039Calcium 6; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi1040Calcium 5Combined sources2 Publications1
Metal bindingi1040Calcium 6Combined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei1067Collagen-binding2 Publications1
Binding sitei1080Collagen-binding2 Publications1

<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

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.3, 1481

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M09.002

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagenase ColG1 Publication (EC:3.4.24.31 Publication)
Alternative name(s):
Class I collagenase2 Publications
Gelatinase ColG1 Publication
Microbial collagenase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:colG1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHathewaya histolytica (Clostridium histolyticum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1498 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic 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

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 their 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
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 reduce these joint contractures (PubMed:10913202, PubMed:19726771). 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 psychosocial symptoms (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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi389 – 397Missing : Degrades soluble FALGPA peptide (furylacryloyl-Leu-Gly-Pro-Ala) but only 40% active on type I collagen. 1 Publication9
Mutagenesisi524E → D: Retains 4% digestion of collagen, still bind collagen. 1 Publication1
Mutagenesisi1039R → A: S3b fragment has 2.3-fold increased affinity for collagen. 1 Publication1
Mutagenesisi1062F → A: S3b fragment has 2.4-fold increased affinity for collagen. 1 Publication1
Mutagenesisi1067T → A: S3b fragment has 10-fold decreased affinity for collagen. 1 Publication1
Mutagenesisi1080Y → A: S3b fragment has 12-fold decreased affinity for collagen. 1 Publication1
Mutagenesisi1088V → A: S3b fragment has 2.2-fold increased affinity for collagen. 1 Publication1
Mutagenesisi1102L → A: S3b fragment has 5-fold decreased affinity for collagen. 1 Publication1
Mutagenesisi1104Y → A or S: S3b fragment has no collagen binding. 1 Publication1
Mutagenesisi1104Y → F: S3b fragment has 12-fold decreased affinity for collagen. 1 Publication1
Mutagenesisi1106Y → A: S3b fragment has 40-fold decreased affinity for collagen. 1 Publication1

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
5989, Clo hi Collagenase

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2268009

<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 – 45Sequence analysisAdd BLAST45
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044354546 – 1101 PublicationAdd BLAST65
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000443546111 – 1118Collagenase ColGAdd BLAST1008

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 67 kDa, 78 kDa, 82 kDa and 116 kDa (full-length) proteins all of which have the same N-terminus; only the longest form digests insoluble collagen (PubMed:9922257). At least 2 in vivo isolated forms (C1b and C1c) are missing the second collagen-binding domain, ending on Lys-1006 and Lys-1018 respectively (PubMed:22099748).2 Publications

Keywords - PTMi

Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9X721

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

RNA levels are high in late logarithmic phase.1 Publication

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

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q9X721

<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

11118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

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SASBDBi
Q9X721

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

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SMRi
Q9X721

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9X721

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini797 – 885PKDPROSITE-ProRule annotationAdd BLAST89

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>Regioni111 – 786S1 metalloprotease domain, degrades both FALGPA (furylacryloyl-Leu-Gly-Pro-Ala) and type I collagen2 Publications1 PublicationAdd BLAST676
Regioni119 – 388Activator domain required for full activity on collagen1 Publication1 PublicationAdd BLAST270
Regioni389 – 670Catalytic subdomain1 PublicationAdd BLAST282
Regioni396 – 1118Degrades soluble FALGPA peptide (furylacryloyl-Leu-Gly-Pro-Ala) but not type I collagen1 PublicationAdd BLAST723
Regioni679 – 790Helper subdomain1 PublicationAdd BLAST112
Regioni787 – 882S2 domain2 PublicationsAdd BLAST96
Regioni886 – 1003S3a collagen-binding domain2 PublicationsAdd BLAST118
Regioni1008 – 1118S3b collagen-binding domain2 Publications1 PublicationAdd BLAST111
Regioni1102 – 1106Collagen-binding2 Publications5

<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 111-786), S2 (877-882, equivalent to PKD), and 2 collagen-binding domains (CBD) S3a (997-1003) and S3b (1008-1118) (PubMed:9922257, PubMed:11121400). The S1 domain has collagen hydrolytic activity (PubMed:11121400, PubMed:18937627). The metalloprotease S1 domain is composed of 3 subdomains which together resemble a saddle; an activator domain (residues 119-388), the catalytic peptidase subdomain (398-670) and a helper subdomain (679-790) joined by a Gly-rich hinge (387-397) (PubMed:21947205, PubMed:23703618). The S2 domain (799-880, PKD) is flexible within a larger structure (S1 plus S2, residues 119-880) (PubMed:21947205, PubMed:21871007). Binding to Ca2+ renders the midsection of S2 more flexible; Ca2+ binding confers thermostability (PubMed:25760606). S3a and S3b each have collagen-binding activity; collagen is bound more efficiently when both S3a and S3b are present (PubMed:11121400). CBD S3a plus S3b binds to many types of collagen in vitro and in vivo (PubMed:11913772). The structure of CBD S3b becomes more compact and thermostable when it is bound to Ca2+ and its N-terminal linker (approximately residues 1008-1020) changes from an extended alpha-helix to a beta-sheet anchored to the rest of the CBD (PubMed:12682007, PubMed:23144249). S3b may act as a Ca2+-activated molecular switch to trigger domain reorientation (PubMed:12682007). Isolated CBD S3b binds unidirectionally to the C-terminus of the collagen triple helix via a surface cleft (PubMed:19208618, PubMed:23144249). The S3b domain binds preferentially to undertwisted segions of collagen (PubMed:22898990).4 Publications10 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, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR041379, ColG_subdomain
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
PF18496, ColG_sub, 1 hit
PF01752, Peptidase_M9, 1 hit
PF08453, Peptidase_M9_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00931, MICOLLPTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00089, PKD, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49299, SSF49299, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50093, PKD, 1 hit
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

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

Q9X721-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKNILKILM DSYSKESKIQ TVRRVTSVSL LAVYLTMNTS SLVLAKPIEN
60 70 80 90 100
TNDTSIKNVE KLRNAPNEEN SKKVEDSKND KVEHVKNIEE AKVEQVAPEV
110 120 130 140 150
KSKSTLRSAS IANTNSEKYD FEYLNGLSYT ELTNLIKNIK WNQINGLFNY
160 170 180 190 200
STGSQKFFGD KNRVQAIINA LQESGRTYTA NDMKGIETFT EVLRAGFYLG
210 220 230 240 250
YYNDGLSYLN DRNFQDKCIP AMIAIQKNPN FKLGTAVQDE VITSLGKLIG
260 270 280 290 300
NASANAEVVN NCVPVLKQFR ENLNQYAPDY VKGTAVNELI KGIEFDFSGA
310 320 330 340 350
AYEKDVKTMP WYGKIDPFIN ELKALGLYGN ITSATEWASD VGIYYLSKFG
360 370 380 390 400
LYSTNRNDIV QSLEKAVDMY KYGKIAFVAM ERITWDYDGI GSNGKKVDHD
410 420 430 440 450
KFLDDAEKHY LPKTYTFDNG TFIIRAGDKV SEEKIKRLYW ASREVKSQFH
460 470 480 490 500
RVVGNDKALE VGNADDVLTM KIFNSPEEYK FNTNINGVST DNGGLYIEPR
510 520 530 540 550
GTFYTYERTP QQSIFSLEEL FRHEYTHYLQ ARYLVDGLWG QGPFYEKNRL
560 570 580 590 600
TWFDEGTAEF FAGSTRTSGV LPRKSILGYL AKDKVDHRYS LKKTLNSGYD
610 620 630 640 650
DSDWMFYNYG FAVAHYLYEK DMPTFIKMNK AILNTDVKSY DEIIKKLSDD
660 670 680 690 700
ANKNTEYQNH IQELADKYQG AGIPLVSDDY LKDHGYKKAS EVYSEISKAA
710 720 730 740 750
SLTNTSVTAE KSQYFNTFTL RGTYTGETSK GEFKDWDEMS KKLDGTLESL
760 770 780 790 800
AKNSWSGYKT LTAYFTNYRV TSDNKVQYDV VFHGVLTDNA DISNNKAPIA
810 820 830 840 850
KVTGPSTGAV GRNIEFSGKD SKDEDGKIVS YDWDFGDGAT SRGKNSVHAY
860 870 880 890 900
KKAGTYNVTL KVTDDKGATA TESFTIEIKN EDTTTPITKE MEPNDDIKEA
910 920 930 940 950
NGPIVEGVTV KGDLNGSDDA DTFYFDVKED GDVTIELPYS GSSNFTWLVY
960 970 980 990 1000
KEGDDQNHIA SGIDKNNSKV GTFKSTKGRH YVFIYKHDSA SNISYSLNIK
1010 1020 1030 1040 1050
GLGNEKLKEK ENNDSSDKAT VIPNFNTTMQ GSLLGDDSRD YYSFEVKEEG
1060 1070 1080 1090 1100
EVNIELDKKD EFGVTWTLHP ESNINDRITY GQVDGNKVSN KVKLRPGKYY
1110
LLVYKYSGSG NYELRVNK
Length:1,118
Mass (Da):126,242
Last modified:November 1, 1999 - 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:i770CF3F60E4D4FD4
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 conflicti606F → V in BAA86030 (Ref. 2) Curated1
Sequence conflicti656 – 659EYQN → DYQT in BAA86030 (Ref. 2) Curated4
Sequence conflicti836 – 837GD → VY in BAA86030 (Ref. 2) Curated2

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
D87215 Genomic DNA Translation: BAA77453.1
AB026889 Genomic DNA Translation: BAA86030.1

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">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
D87215 Genomic DNA Translation: BAA77453.1
AB026889 Genomic DNA Translation: BAA86030.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
1NQDX-ray1.65A/B1003-1118[»]
1NQJX-ray1.00A/B1003-1118[»]
2O8OX-ray1.35A/B1003-1118[»]
2Y3UX-ray2.55A119-880[»]
2Y50X-ray2.80A119-880[»]
2Y6IX-ray3.25A119-880[»]
2Y72X-ray1.18A/B799-880[»]
4AQOX-ray0.99A792-880[»]
4AREX-ray2.19A119-789[»]
4HPKX-ray1.35A1006-1118[»]
B1003-1118[»]
4JRWX-ray1.60A/B797-881[»]
4TN9X-ray1.40A/B797-881[»]
5IKUX-ray1.90A883-1118[»]
SASBDBiQ9X721
SMRiQ9X721
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

BindingDBiQ9X721
ChEMBLiCHEMBL2268009

Protein family/group databases

Allergomei5989, Clo hi Collagenase
MEROPSiM09.002

Proteomic databases

PRIDEiQ9X721

Enzyme and pathway databases

BRENDAi3.4.24.3, 1481

Miscellaneous databases

EvolutionaryTraceiQ9X721

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR041379, ColG_subdomain
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
PF18496, ColG_sub, 1 hit
PF01752, Peptidase_M9, 1 hit
PF08453, Peptidase_M9_N, 1 hit
PRINTSiPR00931, MICOLLPTASE
SMARTiView protein in SMART
SM00089, PKD, 1 hit
SUPFAMiSSF49299, SSF49299, 1 hit
PROSITEiView protein in PROSITE
PS50093, PKD, 1 hit
PS00142, ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCOLG_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: Q9X721
Secondary accession number(s): Q9S0X0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2018
Last sequence update: November 1, 1999
Last modified: April 7, 2021
This is version 103 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. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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