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UniProtKB - P08254 (MMP3_HUMAN)

Entry version 213 (03 Jul 2019)
Sequence version 2 (01 Feb 1991)
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Protein

Stromelysin-1

Gene

MMP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Preferential cleavage where P1', P2' and P3' are hydrophobic residues. EC:3.4.24.17

<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 bindingi92Zinc 2; in inhibited form1
Metal bindingi124Calcium 11
Metal bindingi158Calcium 21
Metal bindingi168Zinc 11
Metal bindingi170Zinc 11
Metal bindingi175Calcium 31
Metal bindingi176Calcium 3; via carbonyl oxygen1
Metal bindingi178Calcium 3; via carbonyl oxygen1
Metal bindingi180Calcium 3; via carbonyl oxygen1
Metal bindingi183Zinc 11
Metal bindingi190Calcium 2; via carbonyl oxygen1
Metal bindingi192Calcium 2; via carbonyl oxygen1
Metal bindingi194Calcium 21
Metal bindingi196Zinc 11
Metal bindingi198Calcium 31
Metal bindingi199Calcium 11
Metal bindingi201Calcium 11
Metal bindingi201Calcium 31
Metal bindingi218Zinc 2; catalytic1 Publication1
<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 sitei2191
Metal bindingi222Zinc 2; catalytic1 Publication1
Metal bindingi228Zinc 2; catalytic1 Publication1
Metal bindingi297Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi389Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi438Calcium 4; 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

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-2179392 EGFR Transactivation by Gastrin
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-9009391 Non-genomic estrogen signaling

SIGNOR Signaling Network Open Resource

More...SIGNORi		P08254

Protein family/group databases

MEROPS protease database

More...MEROPSi		M10.005

<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:
Stromelysin-1 (EC:3.4.24.17)
Short name:
SL-1
Alternative name(s):
Matrix metalloproteinase-3
Short name:
MMP-3
Transin-1
<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:MMP3
Synonyms:STMY1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:7173 MMP3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		185250 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P08254

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

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

Coronary heart disease 6 (CHDS6)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions.
Disease descriptionA multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries.
Related information in OMIM

Organism-specific databases

DisGeNET

More...DisGeNETi		4314

MalaCards human disease database

More...MalaCardsi		MMP3
MIMi614466 phenotype

Open Targets

More...OpenTargetsi		ENSG00000149968

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30886

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL283

Drug and drug target database

More...DrugBanki		DB02367 (1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidine
DB04140 1-Benzyl-3-(4-Methoxy-Benzenesulfonyl)-6-Oxo-Hexahydro-Pyrimidine-4-Carboxylic Acid Hydroxyamide
DB03033 1-Methyloxy-4-Sulfone-Benzene
DB08643 2-(2-{2-[(BIPHENYL-4-YLMETHYL)-AMINO]-3-MERCAPTO-PENTANOYLAMINO}-ACETYLAMINO)-3-METHYL-BUTYRIC ACID METHYL ESTER
DB02449 3-(1h-Indol-3-Yl)-2-[4-(4-Phenyl-Piperidin-1-Yl)-Benzenesulfonylamino]-Propionic Acid
DB08030 3-[(4'-cyanobiphenyl-4-yl)oxy]-N-hydroxypropanamide
DB01996 3-Methylpyridine
DB07986 [4-(4-PHENYL-PIPERIDIN-1-YL)-BENZENESULFONYLAMINO]-ACETIC ACID
DB02090 A Disubstituted Succinyl Caprolactam Hydroxymate Mmp3inhibitor
DB02697 Hydroxyaminovaline
DB00786 Marimastat
DB08507 N-[[2-METHYL-4-HYDROXYCARBAMOYL]BUT-4-YL-N]-BENZYL-P-[PHENYL]-P-[METHYL]PHOSPHINAMID
DB04232 N-Hydroxy-1-(4-Methoxyphenyl)Sulfonyl-4-Benzyloxycarbonyl-Piperazine-2-Carboxamide
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID
DB08029 N~2~-(biphenyl-4-ylsulfonyl)-N-hydroxy-N~2~-(2-hydroxyethyl)glycinamide

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1630

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MMP3

Domain mapping of disease mutations (DMDM)

More...DMDMi		116857

<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 – 171 PublicationAdd BLAST17
<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_000002872818 – 99Activation peptideAdd BLAST82
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000028729100 – 477Stromelysin-1Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi290 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P08254

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08254

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

More...PaxDbi		P08254

PeptideAtlas

More...PeptideAtlasi		P08254

PRoteomics IDEntifications database

More...PRIDEi		P08254

ProteomicsDB human proteome resource

More...ProteomicsDBi		52102

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08254

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

More...PhosphoSitePlusi		P08254

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P08254

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000149968 Expressed in 112 organ(s), highest expression level in layer of synovial tissue

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P08254 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P08254 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA007875

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2P502223EBI-6957351,EBI-748397

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110458, 16 interactors

Protein interaction database and analysis system

More...IntActi		P08254, 1 interactor

Molecular INTeraction database

More...MINTi		P08254

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000299855

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P08254

<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

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P08254

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08254

<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>Repeati287 – 336Hemopexin 1Add BLAST50
Repeati337 – 383Hemopexin 2Add BLAST47
Repeati385 – 433Hemopexin 3Add BLAST49
Repeati434 – 477Hemopexin 4Add BLAST44

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>Motifi90 – 97Cysteine 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 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.

<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
ENOG410XQ5D LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159759

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000217927

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08254

KEGG Orthology (KO)

More...KOi		K01394

Identification of Orthologs from Complete Genome Data

More...OMAi		PGFPRQI

Database of Orthologous Groups

More...OrthoDBi		217780at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08254

TreeFam database of animal gene trees

More...TreeFami		TF315428

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
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

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: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P08254-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ 
        60         70         80         90        100
FVRRKDSGPV VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF 
       110        120        130        140        150
RTFPGIPKWR KTHLTYRIVN YTPDLPKDAV DSAVEKALKV WEEVTPLTFS 
       160        170        180        190        200
RLYEGEADIM ISFAVREHGD FYPFDGPGNV LAHAYAPGPG INGDAHFDDD 
       210        220        230        240        250
EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY HSLTDLTRFR 
       260        270        280        290        300
LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS 
       310        320        330        340        350
TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD 
       360        370        380        390        400
LVFIFKGNQF WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT 
       410        420        430        440        450
YFFVEDKYWR FDEKRNSMEP GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF 
       460        470 
TGSSQLEFDP NAKKVTHTLK SNSWLNC
Length:477
Mass (Da):53,977
Last modified:February 1, 1991 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i96194833B907668D
GO

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

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PKX2E9PKX2_HUMAN
Stromelysin-1
MMP3
42Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C139H7C139_HUMAN
Stromelysin-1
MMP3
99Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti420P → L (PubMed:3477804).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01309045K → E3 PublicationsCorresponds to variant dbSNP:rs679620EnsemblClinVar.1

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
X05232 mRNA Translation: CAA28859.1
J03209 mRNA Translation: AAA36321.1
U78045 Genomic DNA Translation: AAB36942.1
AK223283 mRNA Translation: BAD97003.1
AK223291 mRNA Translation: BAD97011.1
AK313310 mRNA Translation: BAG36115.1
AF405705 Genomic DNA Translation: AAK95247.1
CH471065 Genomic DNA Translation: EAW67032.1
BC069676 mRNA Translation: AAH69676.1
BC069716 mRNA Translation: AAH69716.1
BC074815 mRNA Translation: AAH74815.1
BC074869 mRNA Translation: AAH74869.1
BC105954 mRNA Translation: AAI05955.1
BC107490 mRNA Translation: AAI07491.1
BC107491 mRNA Translation: AAI07492.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS8323.1

Protein sequence database of the Protein Information Resource

More...PIRi		A28156 KCHUS1

NCBI Reference Sequences

More...RefSeqi		NP_002413.1, NM_002422.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000299855; ENSP00000299855; ENSG00000149968

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4314

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4314

UCSC genome browser

More...UCSCi		uc001phj.2 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05232 mRNA Translation: CAA28859.1
J03209 mRNA Translation: AAA36321.1
U78045 Genomic DNA Translation: AAB36942.1
AK223283 mRNA Translation: BAD97003.1
AK223291 mRNA Translation: BAD97011.1
AK313310 mRNA Translation: BAG36115.1
AF405705 Genomic DNA Translation: AAK95247.1
CH471065 Genomic DNA Translation: EAW67032.1
BC069676 mRNA Translation: AAH69676.1
BC069716 mRNA Translation: AAH69716.1
BC074815 mRNA Translation: AAH74815.1
BC074869 mRNA Translation: AAH74869.1
BC105954 mRNA Translation: AAI05955.1
BC107490 mRNA Translation: AAI07491.1
BC107491 mRNA Translation: AAI07492.1
CCDSiCCDS8323.1
PIRiA28156 KCHUS1
RefSeqiNP_002413.1, NM_002422.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B3DX-ray2.30A/B100-272[»]
1B8YX-ray2.00A100-266[»]
1BIWX-ray2.50A/B100-272[»]
1BM6NMR-A100-272[»]
1BQOX-ray2.30A/B100-272[»]
1C3IX-ray1.83A/B100-272[»]
1C8TX-ray2.60A/B103-268[»]
1CAQX-ray1.80A100-267[»]
1CIZX-ray1.64A100-267[»]
1CQRX-ray2.00A/B100-272[»]
1D5JX-ray2.60A/B100-272[»]
1D7XX-ray2.00A/B100-272[»]
1D8FX-ray2.40A/B100-272[»]
1D8MX-ray2.44A/B100-272[»]
1G05X-ray2.45A/B100-272[»]
1G49X-ray1.90A/B100-272[»]
1G4KX-ray2.00A/B/C100-267[»]
1HFSX-ray1.70A105-264[»]
1HY7X-ray1.50A/B100-272[»]
1M1Wmodel-A100-268[»]
1OO9NMR-A100-267[»]
1QIAX-ray2.00A/B/C/D106-267[»]
1QICX-ray2.00A/B/C/D106-266[»]
1SLMX-ray1.90A18-272[»]
1SLNX-ray2.27A100-272[»]
1UEAX-ray2.80A/C100-272[»]
1UMSNMR-A100-273[»]
1UMTNMR-A100-273[»]
1USNX-ray1.80A100-264[»]
2D1OX-ray2.02A/B100-270[»]
2JNPNMR-A105-265[»]
2JT5NMR-A105-265[»]
2JT6NMR-A105-265[»]
2SRTNMR-A100-272[»]
2USNX-ray2.20A100-264[»]
3OHLX-ray2.36A100-266[»]
3OHOX-ray2.50A100-268[»]
3USNNMR-A100-267[»]
4DPEX-ray1.96A/B100-272[»]
4G9LX-ray1.88A/B100-272[»]
4JA1X-ray1.96A/B100-272[»]
6MAVX-ray2.37A100-267[»]
6N9DX-ray2.67A100-264[»]
SMRiP08254
ModBaseiSearch...

Protein-protein interaction databases

BioGridi110458, 16 interactors
IntActiP08254, 1 interactor
MINTiP08254
STRINGi9606.ENSP00000299855

Chemistry databases

BindingDBiP08254
ChEMBLiCHEMBL283
DrugBankiDB02367 (1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidine
DB04140 1-Benzyl-3-(4-Methoxy-Benzenesulfonyl)-6-Oxo-Hexahydro-Pyrimidine-4-Carboxylic Acid Hydroxyamide
DB03033 1-Methyloxy-4-Sulfone-Benzene
DB08643 2-(2-{2-[(BIPHENYL-4-YLMETHYL)-AMINO]-3-MERCAPTO-PENTANOYLAMINO}-ACETYLAMINO)-3-METHYL-BUTYRIC ACID METHYL ESTER
DB02449 3-(1h-Indol-3-Yl)-2-[4-(4-Phenyl-Piperidin-1-Yl)-Benzenesulfonylamino]-Propionic Acid
DB08030 3-[(4'-cyanobiphenyl-4-yl)oxy]-N-hydroxypropanamide
DB01996 3-Methylpyridine
DB07986 [4-(4-PHENYL-PIPERIDIN-1-YL)-BENZENESULFONYLAMINO]-ACETIC ACID
DB02090 A Disubstituted Succinyl Caprolactam Hydroxymate Mmp3inhibitor
DB02697 Hydroxyaminovaline
DB00786 Marimastat
DB08507 N-[[2-METHYL-4-HYDROXYCARBAMOYL]BUT-4-YL-N]-BENZYL-P-[PHENYL]-P-[METHYL]PHOSPHINAMID
DB04232 N-Hydroxy-1-(4-Methoxyphenyl)Sulfonyl-4-Benzyloxycarbonyl-Piperazine-2-Carboxamide
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID
DB08029 N~2~-(biphenyl-4-ylsulfonyl)-N-hydroxy-N~2~-(2-hydroxyethyl)glycinamide
GuidetoPHARMACOLOGYi1630

Protein family/group databases

MEROPSiM10.005

PTM databases

iPTMnetiP08254
PhosphoSitePlusiP08254

Polymorphism and mutation databases

BioMutaiMMP3
DMDMi116857

Proteomic databases

EPDiP08254
jPOSTiP08254
PaxDbiP08254
PeptideAtlasiP08254
PRIDEiP08254
ProteomicsDBi52102

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		4314
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299855; ENSP00000299855; ENSG00000149968
GeneIDi4314
KEGGihsa:4314
UCSCiuc001phj.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4314
DisGeNETi4314

GeneCards: human genes, protein and diseases

More...GeneCardsi		MMP3
HGNCiHGNC:7173 MMP3
HPAiHPA007875
MalaCardsiMMP3
MIMi185250 gene
614466 phenotype
neXtProtiNX_P08254
OpenTargetsiENSG00000149968
PharmGKBiPA30886

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000159759
HOGENOMiHOG000217927
InParanoidiP08254
KOiK01394
OMAiPGFPRQI
OrthoDBi217780at2759
PhylomeDBiP08254
TreeFamiTF315428

Enzyme and pathway databases

ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-2179392 EGFR Transactivation by Gastrin
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-9009391 Non-genomic estrogen signaling
SIGNORiP08254

Miscellaneous databases

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

More...ChiTaRSi		MMP3 human
EvolutionaryTraceiP08254

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MMP3

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

More...GenomeRNAii		4314
PMAP-CutDBiP08254

Protein Ontology

More...PROi		PR:P08254

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000149968 Expressed in 112 organ(s), highest expression level in layer of synovial tissue
ExpressionAtlasiP08254 baseline and differential
GenevisibleiP08254 HS

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
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
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 nameiMMP3_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08254
Secondary accession number(s): B2R8B8, Q3B7S0, Q6GRF8
<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: August 1, 1988
Last sequence update: February 1, 1991
Last modified: July 3, 2019
This is version 213 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  7. Peptidase families
    Classification of peptidase families and list of entries
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