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Protein

Matrix metalloproteinase-21

Gene

Mmp21

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin (By similarity).By similarity

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Zinc; in inhibited formBy similarity
Metal bindingi282 – 2821Zinc; catalyticPROSITE-ProRule annotation
Active sitei283 – 2831PROSITE-ProRule annotation
Metal bindingi286 – 2861Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi292 – 2921Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. metallopeptidase activity Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. hematopoietic progenitor cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.026.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-21 (EC:3.4.24.-)
Short name:
MMP-21
Gene namesi
Name:Mmp21
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2664387. Mmp21.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular matrix Source: InterPro
  2. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 568544Matrix metalloproteinase-21PRO_0000028841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi328 ↔ 559By similarity
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ8K3F2.

PTM databases

PhosphoSiteiQ8K3F2.

Expressioni

Gene expression databases

CleanExiMM_MMP21.
ExpressionAtlasiQ8K3F2. baseline.
GenevestigatoriQ8K3F2.

Structurei

3D structure databases

ProteinModelPortaliQ8K3F2.
SMRiQ8K3F2. Positions 68-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati329 – 38860Hemopexin 1Add
BLAST
Repeati390 – 44657Hemopexin 2Add
BLAST
Repeati447 – 49549Hemopexin 3Add
BLAST
Repeati502 – 55857Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 1178Cysteine switchBy similarity

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.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG115777.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000113608.
HOVERGENiHBG052483.
InParanoidiQ8K3F2.
KOiK08000.
OMAiLYENRNN.
OrthoDBiEOG7X9G6K.
PhylomeDBiQ8K3F2.
TreeFamiTF315428.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K3F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAASVLRLT LPLCWLVAPQ PTQPERLFHS RDRSDLEPSP LSQAKPIADL
60 70 80 90 100
HDAQSFLLKY GWSEIPSPKE SAGVPVGFTL AQAVRRFQKA NRLPASGELD
110 120 130 140 150
SPTLAAMNKP RCGVPDTRLP PRAALPTPPA LLTSLGLRPR ARQKRFLQML
160 170 180 190 200
FPKPDGQQED ASDTGASRAF SKKTLTWRLV GDAYSSQLSG DEQRYIFRLA
210 220 230 240 250
FRMWSEVTPL DFREDRTAPG TMVDIKLGFG RGRHLGCPRV FDGSGQEFAH
260 270 280 290 300
AWRLGEIHFD DDEHFTPLSS DTGISLLKVA VHEIGHVLGL PHTYRVGSIM
310 320 330 340 350
QPNYIPQEPA FELDWADRKA IQRLYGSCKG SFDTVFDWIR KERNQYGEVR
360 370 380 390 400
VRFNTYFFRN SWYWLYENRN NRTRYGDPLQ ILTGWRGIPT QSIDAYVHVW
410 420 430 440 450
SWGKDERYFF KGSQYWRYDS ENDQAHTEDE QGRSYPKLIS EGFPGIPSPL
460 470 480 490 500
DTAFYDRRQQ LIYFFKESLV FAFDVNRNQV LNSYPKKMSQ VFPAIMPQNH
510 520 530 540 550
PFRNLDSAYY SYAHNSIFFF KGNSYWKVVS DKDKQQNTRL PLNGLFPKKP
560
VSEKWFDVCD VHTSTLNM
Length:568
Mass (Da):65,454
Last modified:September 30, 2002 - v1
Checksum:iEDDBDDD9B6E00546
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY124569 mRNA. Translation: AAM94032.1.
AF507967 mRNA. Translation: AAN09805.1.
CCDSiCCDS21933.1.
RefSeqiNP_694423.1. NM_152944.1.
UniGeneiMm.222952.

Genome annotation databases

EnsembliENSMUST00000033278; ENSMUSP00000033278; ENSMUSG00000030981.
GeneIDi214766.
KEGGimmu:214766.
UCSCiuc009kdd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY124569 mRNA. Translation: AAM94032.1.
AF507967 mRNA. Translation: AAN09805.1.
CCDSiCCDS21933.1.
RefSeqiNP_694423.1. NM_152944.1.
UniGeneiMm.222952.

3D structure databases

ProteinModelPortaliQ8K3F2.
SMRiQ8K3F2. Positions 68-527.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.026.

PTM databases

PhosphoSiteiQ8K3F2.

Proteomic databases

PRIDEiQ8K3F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033278; ENSMUSP00000033278; ENSMUSG00000030981.
GeneIDi214766.
KEGGimmu:214766.
UCSCiuc009kdd.1. mouse.

Organism-specific databases

CTDi118856.
MGIiMGI:2664387. Mmp21.

Phylogenomic databases

eggNOGiNOG115777.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000113608.
HOVERGENiHBG052483.
InParanoidiQ8K3F2.
KOiK08000.
OMAiLYENRNN.
OrthoDBiEOG7X9G6K.
PhylomeDBiQ8K3F2.
TreeFamiTF315428.

Miscellaneous databases

NextBioi374464.
PROiQ8K3F2.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MMP21.
ExpressionAtlasiQ8K3F2. baseline.
GenevestigatoriQ8K3F2.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein."
    Marchenko G.N., Marchenko N.D., Strongin A.Y.
    Biochem. J. 372:503-515(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. "Mouse MMP-21, a novel matrix metalloproteinase."
    Lopez-Otin C., Pendas A.M., Llano E.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: A/J.

Entry informationi

Entry nameiMMP21_MOUSE
AccessioniPrimary (citable) accession number: Q8K3F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 18, 2004
Last sequence update: September 30, 2002
Last modified: January 6, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.