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UniProtKB - O18927 (MMP13_HORSE)

Entry version 130 (12 Aug 2020)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
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Protein

Collagenase 3

Gene

MMP13

Organism
Equus caballus (Horse)
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 transcript 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

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity).By similarity

<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:

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 bindingi97Zinc 2; in inhibited formBy similarity1
Metal bindingi129Calcium 1By similarity1
Metal bindingi163Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi173Zinc 1; via tele nitrogenBy similarity1
Metal bindingi175Zinc 1By similarity1
Metal bindingi180Calcium 3By similarity1
Metal bindingi181Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi183Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi185Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi188Zinc 1; via tele nitrogenBy similarity1
Metal bindingi195Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi197Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi199Calcium 2By similarity1
Metal bindingi201Zinc 1; via pros nitrogenBy similarity1
Metal bindingi203Calcium 3By similarity1
Metal bindingi204Calcium 1By similarity1
Metal bindingi206Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi206Calcium 3By similarity1
Metal bindingi223Zinc 2; via tele nitrogen; catalyticBy similarity1
<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 sitei224PROSITE-ProRule annotation1
Metal bindingi227Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi233Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi241Zinc 2; via carbonyl oxygen; catalyticBy similarity1
Metal bindingi292Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi294Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi336Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi338Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi384Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi386Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi433Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi435Calcium 5; via carbonyl oxygenBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.24.B4, 2120

Protein family/group databases

MEROPS protease database

More...MEROPSi		M10.013

<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 3 (EC:3.4.24.-)
Alternative name(s):
Matrix metalloproteinase-13
Short name:
MMP-13
<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:MMP13
<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>OrganismiEquus caballus (Horse)
<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 identifieri9796 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002281 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

<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 – 19Sequence analysisAdd BLAST19
<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_000002878620 – 104Activation peptideSequence analysisAdd BLAST85
<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_0000028787105 – 472Collagenase 3Add BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi118N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi159N-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 bondi285 ↔ 472By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei367Phosphotyrosine; by PKDCCBy similarity1

<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

The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity).By similarity
N-glycosylated.By similarity
Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

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

More...PaxDbi		O18927

<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

Seems to be specific to breast carcinomas.

<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

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

More...SMRi		O18927

Database of comparative protein structure models

More...ModBasei		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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati282 – 331Hemopexin 1Add BLAST50
Repeati332 – 378Hemopexin 2Add BLAST47
Repeati380 – 428Hemopexin 3Add BLAST49
Repeati429 – 472Hemopexin 4Add BLAST44

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>Regioni177 – 247Interaction with TIMP2By similarityAdd BLAST71
Regioni269 – 472Interaction with collagenBy similarityAdd BLAST204

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>Motifi95 – 102Cysteine switchBy similarity8

<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 C-terminal region binds to collagen.By similarity
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity).By similarity

<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 M10A family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O18927

KEGG Orthology (KO)

More...KOi		K07994

Database of Orthologous Groups

More...OrthoDBi		1075463at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd00094, HX, 1 hit
cd04278, ZnMc_MMP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028711, Collagenase_3
IPR000585, Hemopexin-like_dom
IPR036375, Hemopexin-like_dom_sf
IPR018487, Hemopexin-like_repeat
IPR018486, Hemopexin_CS
IPR033739, M10A_MMP
IPR024079, MetalloPept_cat_dom_sf
IPR001818, Pept_M10_metallopeptidase
IPR021190, Pept_M10A
IPR021158, Pept_M10A_Zn_BS
IPR006026, Peptidase_Metallo
IPR002477, Peptidoglycan-bd-like
IPR036365, PGBD-like_sf
IPR036366, PGBDSf

The PANTHER Classification System

More...PANTHERi		PTHR10201:SF165, PTHR10201:SF165, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00045, Hemopexin, 4 hits
PF00413, Peptidase_M10, 1 hit
PF01471, PG_binding_1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001191, Peptidase_M10A_matrix, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00138, MATRIXIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00120, HX, 4 hits
SM00235, ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47090, SSF47090, 1 hit
SSF50923, SSF50923, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00546, CYSTEINE_SWITCH, 1 hit
PS00024, HEMOPEXIN, 1 hit
PS51642, HEMOPEXIN_2, 4 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%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.

O18927-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHPGVLAAFL FLSWTRCWSL PVPNDDDDDD DMSEEDFQLA ERYLKSYYYP 
        60         70         80         90        100
LNPAGILKKT AANSVVDRLR EMQSFFGLEV TGKLDDNTLD IMKKPRCGVP 
       110        120        130        140        150
DVGEYNVFPR TLKWPKMNLT YRIVNYTPDL THSEVEKAFK KAFKVWSDVT 
       160        170        180        190        200
PLNFTRLYNG TADIMISFGT KEHGDFYPFD GPSGLLAHAF PPGPNYGGDA 
       210        220        230        240        250
HFDDDETWTS SSKGYNLFLV AAHEFGHSLG LDHSKDPGAL MFPIYTYTGK 
       260        270        280        290        300
SHFVLPDDDV QGIQYLYGPG DEDPNPKHPK TPDKCDPSLS LDAITSLRGE 
       310        320        330        340        350
TMVFKDRFFW RLHPQLVDAE LFLTKSFWPE LPNRIDAAYE HPSKDLIFIF 
       360        370        380        390        400
RGRKFWALNG YDILEGYPQK ISELGFPKDV KKISAAVHFE DTGKTLFFSG 
       410        420        430        440        450
NQVWRYDDTN RMMDKDYPRL IEEDFPGIGD KVDAVYEKNG YIYFFNGPIQ 
       460        470 
FEYSIWSNRI VRVMPTNSLL WC
Length:472
Mass (Da):54,226
Last modified:January 1, 1998 - 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:i92B2697583F016D1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF034087 mRNA Translation: AAB86893.1

NCBI Reference Sequences

More...RefSeqi		NP_001075273.1, NM_001081804.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		100009711

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecb:100009711

<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
AF034087 mRNA Translation: AAB86893.1
RefSeqiNP_001075273.1, NM_001081804.1

3D structure databases

SMRiO18927
ModBaseiSearch...

Protein family/group databases

MEROPSiM10.013

Proteomic databases

PaxDbiO18927

Genome annotation databases

GeneIDi100009711
KEGGiecb:100009711

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4322

Phylogenomic databases

InParanoidiO18927
KOiK07994
OrthoDBi1075463at2759

Enzyme and pathway databases

BRENDAi3.4.24.B4, 2120

Family and domain databases

CDDicd00094, HX, 1 hit
cd04278, ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR028711, Collagenase_3
IPR000585, Hemopexin-like_dom
IPR036375, Hemopexin-like_dom_sf
IPR018487, Hemopexin-like_repeat
IPR018486, Hemopexin_CS
IPR033739, M10A_MMP
IPR024079, MetalloPept_cat_dom_sf
IPR001818, Pept_M10_metallopeptidase
IPR021190, Pept_M10A
IPR021158, Pept_M10A_Zn_BS
IPR006026, Peptidase_Metallo
IPR002477, Peptidoglycan-bd-like
IPR036365, PGBD-like_sf
IPR036366, PGBDSf
PANTHERiPTHR10201:SF165, PTHR10201:SF165, 1 hit
PfamiView protein in Pfam
PF00045, Hemopexin, 4 hits
PF00413, Peptidase_M10, 1 hit
PF01471, PG_binding_1, 1 hit
PIRSFiPIRSF001191, Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138, MATRIXIN
SMARTiView protein in SMART
SM00120, HX, 4 hits
SM00235, ZnMc, 1 hit
SUPFAMiSSF47090, SSF47090, 1 hit
SSF50923, SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546, CYSTEINE_SWITCH, 1 hit
PS00024, HEMOPEXIN, 1 hit
PS51642, HEMOPEXIN_2, 4 hits
PS00142, ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMMP13_HORSE
<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: O18927
<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: December 15, 1998
Last sequence update: January 1, 1998
Last modified: August 12, 2020
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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