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Protein

Stromelysin-1

Gene

MMP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca2+ ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • endopeptidase activity Source: ParkinsonsUK-UCL
  • metalloendopeptidase activity Source: ProtInc
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to nitric oxide Source: ParkinsonsUK-UCL
  • collagen catabolic process Source: Reactome
  • extracellular matrix disassembly Source: Reactome
  • negative regulation of hydrogen peroxide metabolic process Source: ParkinsonsUK-UCL
  • positive regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
  • positive regulation of protein oligomerization Source: ParkinsonsUK-UCL
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS07652-MONOMER.
ZFISH:HS10866-MONOMER.
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.
SIGNORiP08254.

Protein family/group databases

MEROPSiM10.005.

Names & Taxonomyi

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
Gene namesi
Name:MMP3
Synonyms:STMY1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7173. MMP3.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

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.
See also OMIM:614466

Organism-specific databases

DisGeNETi4314.
MalaCardsiMMP3.
MIMi614466. phenotype.
OpenTargetsiENSG00000149968.
PharmGKBiPA30886.

Chemistry databases

ChEMBLiCHEMBL283.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1630.

Polymorphism and mutation databases

BioMutaiMMP3.
DMDMi116857.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
PropeptideiPRO_000002872818 – 99Activation peptideAdd BLAST82
ChainiPRO_0000028729100 – 477Stromelysin-1Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi290 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP08254.
PaxDbiP08254.
PeptideAtlasiP08254.
PRIDEiP08254.

PTM databases

iPTMnetiP08254.
PhosphoSitePlusiP08254.

Miscellaneous databases

PMAP-CutDBP08254.

Expressioni

Gene expression databases

BgeeiENSG00000149968.
CleanExiHS_MMP3.
ExpressionAtlasiP08254. baseline and differential.
GenevisibleiP08254. HS.

Organism-specific databases

HPAiHPA007875.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2A4D1273EBI-6957351,EBI-10172134

Protein-protein interaction databases

BioGridi110458. 14 interactors.
IntActiP08254. 1 interactor.
MINTiMINT-269333.
STRINGi9606.ENSP00000299855.

Chemistry databases

BindingDBiP08254.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 41Combined sources8
Helixi58 – 70Combined sources13
Helixi81 – 86Combined sources6
Beta strandi96 – 98Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi110 – 118Combined sources9
Beta strandi123 – 125Combined sources3
Helixi127 – 142Combined sources16
Beta strandi144 – 146Combined sources3
Beta strandi148 – 151Combined sources4
Beta strandi153 – 155Combined sources3
Beta strandi158 – 164Combined sources7
Beta strandi169 – 171Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi182 – 184Combined sources3
Beta strandi187 – 189Combined sources3
Turni190 – 193Combined sources4
Beta strandi195 – 198Combined sources4
Beta strandi199 – 201Combined sources3
Beta strandi203 – 211Combined sources9
Helixi212 – 223Combined sources12
Beta strandi232 – 234Combined sources3
Beta strandi237 – 239Combined sources3
Helixi240 – 243Combined sources4
Helixi246 – 248Combined sources3
Helixi253 – 263Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP08254.
SMRiP08254.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08254.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati287 – 336Hemopexin 1Add BLAST50
Repeati337 – 383Hemopexin 2Add BLAST47
Repeati385 – 433Hemopexin 3Add BLAST49
Repeati434 – 477Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi90 – 97Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP08254.
KOiK01394.
OMAiVAVCSAY.
OrthoDBiEOG091G03DP.
PhylomeDBiP08254.
TreeFamiTF315428.

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.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1.
[Graphical view]
PANTHERiPTHR10201:SF164. PTHR10201:SF164. 1 hit.
PfamiPF00045. Hemopexin. 4 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.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. 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.

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
Checksum:i96194833B907668D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti420P → L (PubMed:3477804).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01309045K → E.3 PublicationsCorresponds to variant rs679620dbSNPEnsembl.1

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.
UniGeneiHs.375129.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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.
UniGeneiHs.375129.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP08254.
SMRiP08254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110458. 14 interactors.
IntActiP08254. 1 interactor.
MINTiMINT-269333.
STRINGi9606.ENSP00000299855.

Chemistry databases

BindingDBiP08254.
ChEMBLiCHEMBL283.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1630.

Protein family/group databases

MEROPSiM10.005.

PTM databases

iPTMnetiP08254.
PhosphoSitePlusiP08254.

Polymorphism and mutation databases

BioMutaiMMP3.
DMDMi116857.

Proteomic databases

EPDiP08254.
PaxDbiP08254.
PeptideAtlasiP08254.
PRIDEiP08254.

Protocols and materials databases

DNASUi4314.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4314.
DisGeNETi4314.
GeneCardsiMMP3.
HGNCiHGNC:7173. MMP3.
HPAiHPA007875.
MalaCardsiMMP3.
MIMi185250. gene.
614466. phenotype.
neXtProtiNX_P08254.
OpenTargetsiENSG00000149968.
PharmGKBiPA30886.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP08254.
KOiK01394.
OMAiVAVCSAY.
OrthoDBiEOG091G03DP.
PhylomeDBiP08254.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciZFISH:HS07652-MONOMER.
ZFISH:HS10866-MONOMER.
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.
SIGNORiP08254.

Miscellaneous databases

ChiTaRSiMMP3. human.
EvolutionaryTraceiP08254.
GeneWikiiMMP3.
GenomeRNAii4314.
PMAP-CutDBP08254.
PROiP08254.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149968.
CleanExiHS_MMP3.
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.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1.
[Graphical view]
PANTHERiPTHR10201:SF164. PTHR10201:SF164. 1 hit.
PfamiPF00045. Hemopexin. 4 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.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP3_HUMAN
AccessioniPrimary (citable) accession number: P08254
Secondary accession number(s): B2R8B8, Q3B7S0, Q6GRF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 189 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

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 one 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.