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Entry version 153 (12 Aug 2020)
Sequence version 1 (01 Jan 1990)
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Protein

Interstitial collagenase

Gene

MMP1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue. EC:3.4.24.7

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

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

Can be activated without removal of the activation peptide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi91Zinc 2; in inhibited formBy similarity1
Metal bindingi123Calcium 1By similarity1
Metal bindingi157Calcium 2By similarity1
Metal bindingi167Zinc 1By 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 1By similarity1
Metal bindingi189Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi191Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi193Calcium 2By similarity1
Metal bindingi195Zinc 1By similarity1
Metal bindingi197Calcium 3By similarity1
Metal bindingi198Calcium 1By similarity1
Metal bindingi200Calcium 3By similarity1
Metal bindingi217Zinc 2; catalyticBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei218PROSITE-ProRule annotation1
Metal bindingi221Zinc 2; catalyticBy similarity1
Metal bindingi227Zinc 2; catalyticBy similarity1
Metal bindingi284Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi328Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi377Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi426Calcium 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

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

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M10.001

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Interstitial collagenase (EC:3.4.24.7)
Alternative name(s):
Matrix metalloproteinase-1
Short name:
MMP-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MMP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOryctolagus cuniculus (Rabbit)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

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

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Add BLAST18
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002871019 – 98Activation peptideAdd BLAST80
<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_000002871199 – 468Interstitial collagenaseAdd BLAST370

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei273PhosphothreonineBy similarity1
<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 bondi277 ↔ 465By similarity
Modified residuei359Phosphotyrosine; by PKDCCBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Tyrosine phosphorylated in platelets by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P13943

<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
ENSOCUG00000017958, Expressed in zone of skin and 6 other tissues

<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

STRING: functional protein association networks

More...
STRINGi
9986.ENSOCUP00000015428

<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
P13943

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>Repeati274 – 323Hemopexin 1Add BLAST50
Repeati324 – 370Hemopexin 2Add BLAST47
Repeati373 – 421Hemopexin 3Add BLAST49
Repeati422 – 465Hemopexin 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>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 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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154907

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_015489_6_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P13943

KEGG Orthology (KO)

More...
KOi
K01388

Identification of Orthologs from Complete Genome Data

More...
OMAi
DFPGIGH

Database of Orthologous Groups

More...
OrthoDBi
1075463at2759

Family and domain databases

Conserved Domains Database

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

Gene3D Structural and Functional Annotation of Protein Families

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

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001191, Peptidase_M10A_matrix, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00138, MATRIXIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00546, CYSTEINE_SWITCH, 1 hit
PS00024, HEMOPEXIN, 1 hit
PS51642, HEMOPEXIN_2, 4 hits
PS00142, ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

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

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

P13943-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPGLPLLLLL LWGVGSHGFP AASETQEQDV EMVQKYLENY YNLKDDWRKI
60 70 80 90 100
PKQRGNGLAV EKLKQMQEFF GLKVTGKPDA ETLKMMKQPR CGVPDVAQFV
110 120 130 140 150
LTPGNPRWEQ THLTYRIENY TPDLSRADVD NAIEKAFQLW SNVTPLTFTK
160 170 180 190 200
VSKGQADIMI SFVRGDHRDN SPFDGPEGQL AHAFQPGLGI GGDVHFDEDD
210 220 230 240 250
RWTKDFRNYN LYRVAAHELG HSLGLSHSTD IGALMYPNYM FSGDVQLAQD
260 270 280 290 300
DIDGIQAIYG PSQNPSQPVG PQTPKVCDSK LTFDAITTIR GEIMFFKDRF
310 320 330 340 350
YMRANPYYSE VELNFISVFW PHLPNGLQAA YEVAHRDEIL FFKGNKYWTV
360 370 380 390 400
QGQNELPGYP KDIHSSFGFP RSVNHIDAAV SEEDTGKTYF FVANKYWRYD
410 420 430 440 450
EYKRSMDAGY PKMIEYDFPG IGNKVDAVFK KDGFFYFFHG TRQYKFDPKT
460
KRILTLQKAN SWFNCRKN
Length:468
Mass (Da):53,740
Last modified:January 1, 1990 - 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:iDA90538919952B8C
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
A0A5F9CRQ6A0A5F9CRQ6_RABIT
Interstitial collagenase
MMP1
475Annotation score:

Annotation score:2 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>

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
M17823 M19240 mRNA Translation: AAB88016.1
M25663 mRNA Translation: AAA31203.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A27500, KCRBI

NCBI Reference Sequences

More...
RefSeqi
NP_001164610.1, NM_001171139.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSOCUT00000017958; ENSOCUP00000015428; ENSOCUG00000017958

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100009110

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100009110

<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
M17823 M19240 mRNA Translation: AAB88016.1
M25663 mRNA Translation: AAA31203.1
PIRiA27500, KCRBI
RefSeqiNP_001164610.1, NM_001171139.2

3D structure databases

SMRiP13943
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015428

Protein family/group databases

MEROPSiM10.001

Proteomic databases

PRIDEiP13943

Genome annotation databases

EnsembliENSOCUT00000017958; ENSOCUP00000015428; ENSOCUG00000017958
GeneIDi100009110
KEGGiocu:100009110

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4312

Phylogenomic databases

eggNOGiKOG1565, Eukaryota
GeneTreeiENSGT00940000154907
HOGENOMiCLU_015489_6_0_1
InParanoidiP13943
KOiK01388
OMAiDFPGIGH
OrthoDBi1075463at2759

Gene expression databases

BgeeiENSOCUG00000017958, Expressed in zone of skin and 6 other tissues

Family and domain databases

CDDicd00094, HX, 1 hit
cd04278, ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR000585, Hemopexin-like_dom
IPR036375, Hemopexin-like_dom_sf
IPR018487, Hemopexin-like_repeat
IPR018486, Hemopexin_CS
IPR033739, M10A_MMP
IPR024079, MetalloPept_cat_dom_sf
IPR001818, Pept_M10_metallopeptidase
IPR021190, Pept_M10A
IPR021158, Pept_M10A_Zn_BS
IPR006026, Peptidase_Metallo
IPR002477, Peptidoglycan-bd-like
IPR036365, PGBD-like_sf
IPR036366, PGBDSf
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 nameiMMP1_RABIT
<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: P13943
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: August 12, 2020
This is version 153 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

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