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Entry version 161 (29 Sep 2021)
Sequence version 1 (01 Nov 1991)
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Protein

Collagenase 3

Gene

Mmp13

Organism
Rattus norvegicus (Rat)
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

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_section">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 bindingi91Zinc 2; in inhibited formBy similarity1
Metal bindingi123Calcium 1By similarity1
Metal bindingi157Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi167Zinc 1; via tele nitrogenBy similarity1
Metal bindingi169Zinc 1By similarity1
Metal bindingi174Calcium 3By similarity1
Metal bindingi175Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi177Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi179Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi182Zinc 1; via tele nitrogenBy similarity1
Metal bindingi189Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi191Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi193Calcium 2By similarity1
Metal bindingi195Zinc 1; via pros nitrogenBy similarity1
Metal bindingi197Calcium 3By similarity1
Metal bindingi198Calcium 1By similarity1
Metal bindingi200Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi200Calcium 3By similarity1
Metal bindingi217Zinc 2; via tele nitrogen; catalyticBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei218PROSITE-ProRule annotation1
Metal bindingi221Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi227Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi235Zinc 2; via carbonyl oxygen; catalyticBy similarity1
Metal bindingi286Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi288Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi330Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi332Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi378Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi380Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi427Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi429Calcium 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

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 processCollagen degradation
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.B4, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1442490, Collagen degradation
R-RNO-1474228, Degradation of the extracellular matrix
R-RNO-1592389, Activation of Matrix Metalloproteinases
R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures

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_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 3 (EC:3.4.24.-)
Alternative name(s):
Matrix metalloproteinase-13
Short name:
MMP-13
UMRCASE
<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:Mmp13
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
620196, Mmp13

<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

Extracellular matrix, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4944

<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 peptidei‹1 – 13Sequence analysisAdd BLAST›13
<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_000002879414 – 98Activation peptideAdd 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_000002879599 – 466Collagenase 3Add BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi112N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi147N-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 bondi279 ↔ 466By 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 residuei361Phosphotyrosine; by PKDCCBy similarity1
Glycosylationi404N-linked (GlcNAc...) asparagineSequence analysis1

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

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
P23097

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P23097, 3 sites

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

More...
PhosphoSitePlusi
P23097

<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

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000011507

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P23097

<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
P23097

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>Repeati276 – 325Hemopexin 1Add BLAST50
Repeati326 – 372Hemopexin 2Add BLAST47
Repeati374 – 422Hemopexin 3Add BLAST49
Repeati423 – 466Hemopexin 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>Regioni171 – 241Interaction with TIMP2By similarityAdd BLAST71
Regioni258 – 279DisorderedSequence analysisAdd BLAST22
Regioni263 – 466Interaction 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>Motifi89 – 96Cysteine 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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1565, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23097

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P23097

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
2.110.10.10, 1 hit
3.40.390.10, 1 hit

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

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_length">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>Sequence (1+)i

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

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P23097-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
ATFFLLSWTH CWSLPLPYGD DDDDDLSEED LEFAEHYLKS YYHPVTLAGI
60 70 80 90 100
LKKSTVTSTV DRLREMQSFF GLDVTGKLDD PTLDIMRKPR CGVPDVGVYN
110 120 130 140 150
VFPRTLKWSQ TNLTYRIVNY TPDISHSEVE KAFRKAFKVW SDVTPLNFTR
160 170 180 190 200
IHDGTADIMI SFGTKEHGDF YPFDGPSGLL AHAFPPGPNL GGDAHFDDDE
210 220 230 240 250
TWTSSSKGYN LFIVAAHELG HSLGLDHSKD PGALMFPIYT YTGKSHFMLP
260 270 280 290 300
DDDVQGIQSL YGPGDEDPNP KHPKTPEKCD PALSLDAITS LRGETMIFKD
310 320 330 340 350
RFFWRLHPQQ VEPELFLTKS FWPELPNHVD AAYEHPSRDL MFIFRGRKFW
360 370 380 390 400
ALNGYDIMEG YPRKISDLGF PKEVKRLSAA VHFEDTGKTL FFSGNHVWSY
410 420 430 440 450
DDANQTMDKD YPRLIEEEFP GIGDKVDAVY EKNGYIYFFN GPIQFEYSIW
460
SNRIVRVMPT NSLLWC
Length:466
Mass (Da):53,375
Last modified:November 1, 1991 - 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:iBF66021BD734813D
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V742G3V742_RAT
Collagenase 3
Mmp13 rCG_31693
472Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

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
M60616 mRNA Translation: AAA72124.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A23685

Genome annotation databases

UCSC genome browser

More...
UCSCi
RGD:620196, rat

<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
M60616 mRNA Translation: AAA72124.1
PIRiA23685

3D structure databases

SMRiP23097
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011507

Chemistry databases

BindingDBiP23097
ChEMBLiCHEMBL4944

Protein family/group databases

MEROPSiM10.013

PTM databases

GlyGeniP23097, 3 sites
PhosphoSitePlusiP23097

Proteomic databases

PaxDbiP23097

Genome annotation databases

UCSCiRGD:620196, rat

Organism-specific databases

RGDi620196, Mmp13

Phylogenomic databases

eggNOGiKOG1565, Eukaryota
InParanoidiP23097
PhylomeDBiP23097

Enzyme and pathway databases

BRENDAi3.4.24.B4, 5301
ReactomeiR-RNO-1442490, Collagen degradation
R-RNO-1474228, Degradation of the extracellular matrix
R-RNO-1592389, Activation of Matrix Metalloproteinases
R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P23097

Family and domain databases

CDDicd00094, HX, 1 hit
cd04278, ZnMc_MMP, 1 hit
Gene3Di2.110.10.10, 1 hit
3.40.390.10, 1 hit
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
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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_RAT
<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: P23097
<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: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 29, 2021
This is version 161 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

Direct protein sequencing, 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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