Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P39900 (MMP12_HUMAN)

Entry version 201 (11 Dec 2019)
Sequence version 1 (01 Feb 1995)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Macrophage metalloelastase

Gene

MMP12

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

May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.

<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

  • Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin. EC:3.4.24.65

<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 formBy similarity1
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
<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
Metal bindingi228Zinc 2; catalytic1
Metal bindingi289Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi333Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi381Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi430Calcium 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
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

Protein family/group databases

MEROPS protease database

More...MEROPSi		M10.009

<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:
Macrophage metalloelastase (EC:3.4.24.65)
Short name:
MME
Alternative name(s):
Macrophage elastase
Short name:
ME
Short name:
hME
Matrix metalloproteinase-12
Short name:
MMP-12
<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:MMP12
Synonyms:HME
<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

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000262406.2

Human Gene Nomenclature Database

More...HGNCi		HGNC:7158 MMP12

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601046 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P39900

<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

Organism-specific databases

DisGeNET

More...DisGeNETi		4321

Open Targets

More...OpenTargetsi		ENSG00000262406

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30870

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P39900 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4393

Drug and drug target database

More...DrugBanki		DB07026 (1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDE
DB07921 2-[(4-fluorophenyl)sulfonylamino]-N-oxo-ethanamide
DB04405 2-[2-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)Ethyl]-4-(4'-Ethoxy-1,1'-Biphenyl-4-Yl)-4-Oxobutanoic Acid
DB00551 Acetohydroxamic acid
DB05387 AE-941
DB03880 Batimastat
DB02118 CP-271485
DB00786 Marimastat
DB07446 N-(biphenyl-4-ylsulfonyl)-D-leucine
DB07683 N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine
DB08599 N-[(4-methoxyphenyl)sulfonyl]-D-alanine
DB07556 N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID
DB07922 N-oxo-2-(phenylsulfonylamino)ethanamide
DB07920 N-oxo-2-[(4-phenylphenyl)sulfonylamino]ethanamide
DB03367 PF-00356231

DrugCentral

More...DrugCentrali		P39900

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1636

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MMP12

Domain mapping of disease mutations (DMDM)

More...DMDMi		729179

<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 – 16CuratedAdd BLAST16
<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_000002877617 – 105Activation peptideBy similarityAdd BLAST89
<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_0000028777106 – 470Macrophage metalloelastaseAdd BLAST365

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>Glycosylationi20N-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 bondi282 ↔ 470By similarity
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P39900

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P39900

PeptideAtlas

More...PeptideAtlasi		P39900

PRoteomics IDEntifications database

More...PRIDEi		P39900

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55327

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P39900

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P39900

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

More...PhosphoSitePlusi		P39900

<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

Found in alveolar macrophages but not in peripheral blood monocytes.

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

By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000262406 Expressed in 92 organ(s), highest expression level in amniotic fluid

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P39900 HS

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110464, 1 interactor

Protein interaction database and analysis system

More...IntActi		P39900, 2 interactors

Molecular INTeraction database

More...MINTi		P39900

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000458585

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P39900

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P39900 protein

<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

1470
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		P39900

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P39900

<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>Repeati279 – 328Hemopexin 1Add BLAST50
Repeati329 – 375Hemopexin 2Add BLAST47
Repeati377 – 425Hemopexin 3Add BLAST49
Repeati426 – 470Hemopexin 4Add BLAST45

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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162085

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000217927

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P39900

KEGG Orthology (KO)

More...KOi		K01413

Identification of Orthologs from Complete Genome Data

More...OMAi		YYFFQGS

Database of Orthologous Groups

More...OrthoDBi		1075463at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P39900

Family and domain databases

Conserved Domains Database

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

Database of protein disorder

More...DisProti		DP00571

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
IPR028718 MMP12
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:SF32 PTHR10201:SF32, 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>Sequencei

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

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

P39900-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV 
        60         70         80         90        100
TKMKYSGNLM KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF 
       110        120        130        140        150
REMPGGPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS 
       160        170        180        190        200
KINTGMADIL VVFARGAHGD FHAFDGKGGI LAHAFGPGSG IGGDAHFDED 
       210        220        230        240        250
EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL 
       260        270        280        290        300
SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF 
       310        320        330        340        350
FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD 
       360        370        380        390        400
KYWLISNLRP EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY 
       410        420        430        440        450
WRYDERRQMM DPGYPKLITK NFQGIGPKID AVFYSKNKYY YFFQGSNQFE 
       460        470
YDFLLQRITK TLKSNSWFGC
Length:470
Mass (Da):54,002
Last modified:February 1, 1995 - 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:i8C745EEA8C0EA216
GO

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_021343357N → S2 PublicationsCorresponds to variant dbSNP:rs652438Ensembl.1
Natural variantiVAR_021344469G → R1 PublicationCorresponds to variant dbSNP:rs28381701Ensembl.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
L23808 mRNA Translation: AAA58658.1 Sequence problems.
AY856072 Genomic DNA Translation: AAW29944.1
AK313959 mRNA Translation: BAG36675.1
CH471065 Genomic DNA Translation: EAW67033.1
BC112301 mRNA Translation: AAI12302.1
BC143773 mRNA Translation: AAI43774.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS73375.1

Protein sequence database of the Protein Information Resource

More...PIRi		A49499

NCBI Reference Sequences

More...RefSeqi		NP_002417.2, NM_002426.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000571244; ENSP00000458585; ENSG00000262406

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4321

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4321

UCSC genome browser

More...UCSCi		uc031yde.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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23808 mRNA Translation: AAA58658.1 Sequence problems.
AY856072 Genomic DNA Translation: AAW29944.1
AK313959 mRNA Translation: BAG36675.1
CH471065 Genomic DNA Translation: EAW67033.1
BC112301 mRNA Translation: AAI12302.1
BC143773 mRNA Translation: AAI43774.1
CCDSiCCDS73375.1
PIRiA49499
RefSeqiNP_002417.2, NM_002426.5

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
1JIZX-ray2.60A/B100-264[»]
1JK3X-ray1.09A106-263[»]
1OS2X-ray2.15A/B/C/D/E/F106-268[»]
1OS9X-ray1.85A/B/C/D/E/F106-268[»]
1RMZX-ray1.34A106-263[»]
1ROSX-ray2.00A/B106-268[»]
1UTTX-ray2.20A106-264[»]
1UTZX-ray2.50A/B106-264[»]
1Y93X-ray1.03A106-263[»]
1YCMNMR-A106-263[»]
1Z3JNMR-A106-263[»]
2HU6X-ray1.32A106-263[»]
2JXYNMR-A278-470[»]
2K2GNMR-A100-263[»]
2K9CNMR-A112-263[»]
2KRJNMR-A112-263[»]
2MLRNMR-A100-263[»]
2MLSNMR-A100-263[»]
2N8RNMR-A100-263[»]
2OXUX-ray1.24A106-263[»]
2OXWX-ray1.15A106-263[»]
2OXZX-ray1.90A106-263[»]
2POJNMR-A100-263[»]
2W0DX-ray2.00A/B/C/D106-263[»]
2WO8X-ray2.00A/B/C/D106-268[»]
2WO9X-ray1.70A/B/C/D106-268[»]
2WOAX-ray2.30A/B/C/D106-268[»]
2Z2DNMR-A100-263[»]
3BA0X-ray3.00A106-470[»]
3EHXX-ray1.90A106-263[»]
3EHYX-ray1.90A106-263[»]
3F15X-ray1.70A106-263[»]
3F16X-ray1.16A106-263[»]
3F17X-ray1.10A106-263[»]
3F18X-ray1.13A106-263[»]
3F19X-ray1.13A106-263[»]
3F1AX-ray1.25A106-263[»]
3LIKX-ray1.80A106-263[»]
3LILX-ray1.80A106-263[»]
3LIRX-ray1.90A106-263[»]
3LJGX-ray1.31A106-263[»]
3LK8X-ray1.80A106-263[»]
3LKAX-ray1.80A106-263[»]
3N2UX-ray1.81A106-263[»]
3N2VX-ray1.55A106-263[»]
3NX7X-ray1.80A106-263[»]
3RTSX-ray1.81A106-263[»]
3RTTX-ray1.82A106-263[»]
3TS4X-ray1.59A106-263[»]
3TSKX-ray2.00A106-263[»]
3UVCX-ray1.30A/B106-263[»]
4EFSX-ray1.63A106-263[»]
4GQLX-ray1.15A106-263[»]
4GR0X-ray1.50A106-263[»]
4GR3X-ray1.49A106-263[»]
4GR8X-ray1.30A111-262[»]
4GUYX-ray2.00A106-263[»]
4H30X-ray1.43A/B106-263[»]
4H49X-ray2.16A/B/C/D106-263[»]
4H76X-ray1.50A106-263[»]
4H84X-ray1.59A/B106-263[»]
4I03X-ray1.70A106-263[»]
4IJOX-ray1.90A106-263[»]
5CXAX-ray1.30A106-263[»]
5CZMX-ray1.30A106-263[»]
5D2BX-ray1.20A106-263[»]
5D3CX-ray1.31A106-263[»]
5I0LX-ray2.45A/B106-263[»]
5I2ZX-ray2.30A/B/C/D106-263[»]
5I3MX-ray2.17A/B/C/D106-263[»]
5I43X-ray1.95A/B/C/D106-263[»]
5I4OX-ray2.05A/B/C/D106-263[»]
5L79X-ray2.07A106-263[»]
5L7FX-ray1.80A/B106-263[»]
5LABX-ray1.34A106-263[»]
5N5JX-ray1.80A106-263[»]
5N5KX-ray1.80A108-263[»]
6EKNX-ray1.20A106-263[»]
6ELAX-ray1.49A/B/C/D106-263[»]
6ENMX-ray1.59A/B106-263[»]
6EOXX-ray1.30A106-263[»]
SMRiP39900
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi110464, 1 interactor
IntActiP39900, 2 interactors
MINTiP39900
STRINGi9606.ENSP00000458585

Chemistry databases

BindingDBiP39900
ChEMBLiCHEMBL4393
DrugBankiDB07026 (1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDE
DB07921 2-[(4-fluorophenyl)sulfonylamino]-N-oxo-ethanamide
DB04405 2-[2-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)Ethyl]-4-(4'-Ethoxy-1,1'-Biphenyl-4-Yl)-4-Oxobutanoic Acid
DB00551 Acetohydroxamic acid
DB05387 AE-941
DB03880 Batimastat
DB02118 CP-271485
DB00786 Marimastat
DB07446 N-(biphenyl-4-ylsulfonyl)-D-leucine
DB07683 N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine
DB08599 N-[(4-methoxyphenyl)sulfonyl]-D-alanine
DB07556 N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE
DB08271 N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID
DB07922 N-oxo-2-(phenylsulfonylamino)ethanamide
DB07920 N-oxo-2-[(4-phenylphenyl)sulfonylamino]ethanamide
DB03367 PF-00356231
DrugCentraliP39900
GuidetoPHARMACOLOGYi1636

Protein family/group databases

MEROPSiM10.009

PTM databases

iPTMnetiP39900
PhosphoSitePlusiP39900

Polymorphism and mutation databases

BioMutaiMMP12
DMDMi729179

Proteomic databases

jPOSTiP39900
MassIVEiP39900
PeptideAtlasiP39900
PRIDEiP39900
ProteomicsDBi55327
TopDownProteomicsiP39900

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		4321

Genome annotation databases

EnsembliENST00000571244; ENSP00000458585; ENSG00000262406
GeneIDi4321
KEGGihsa:4321
UCSCiuc031yde.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4321
DisGeNETi4321
EuPathDBiHostDB:ENSG00000262406.2

GeneCards: human genes, protein and diseases

More...GeneCardsi		MMP12
HGNCiHGNC:7158 MMP12
MIMi601046 gene
neXtProtiNX_P39900
OpenTargetsiENSG00000262406
PharmGKBiPA30870

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

GeneTreeiENSGT00940000162085
HOGENOMiHOG000217927
InParanoidiP39900
KOiK01413
OMAiYYFFQGS
OrthoDBi1075463at2759
PhylomeDBiP39900

Enzyme and pathway databases

ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix

Miscellaneous databases

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

More...ChiTaRSi		MMP12 human
EvolutionaryTraceiP39900

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Matrix_metallopeptidase_12

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

More...GenomeRNAii		4321
PharosiP39900 Tchem

Protein Ontology

More...PROi		PR:P39900
RNActiP39900 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000262406 Expressed in 92 organ(s), highest expression level in amniotic fluid
GenevisibleiP39900 HS

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
DisProtiDP00571
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
IPR028718 MMP12
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
PANTHERiPTHR10201:SF32 PTHR10201:SF32, 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 nameiMMP12_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: P39900
Secondary accession number(s): B2R9X8, B7ZLF6, Q2M1L9
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 11, 2019
This is version 201 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
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, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again