Skip Header

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

Stromelysin-1

Gene

MMP3

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
Metal bindingi124 – 1241Calcium 1By similarity
Metal bindingi158 – 1581Calcium 2By similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi170 – 1701Zinc 1By similarity
Metal bindingi175 – 1751Calcium 3By similarity
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi183 – 1831Zinc 1By similarity
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi194 – 1941Calcium 2By similarity
Metal bindingi196 – 1961Zinc 1By similarity
Metal bindingi198 – 1981Calcium 3By similarity
Metal bindingi199 – 1991Calcium 1By similarity
Metal bindingi201 – 2011Calcium 1By similarity
Metal bindingi201 – 2011Calcium 3By similarity
Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
Active sitei219 – 2191PROSITE-ProRule annotation
Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
Metal bindingi228 – 2281Zinc 2; catalyticBy similarity
Metal bindingi297 – 2971Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi389 – 3891Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi438 – 4381Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

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
Gene namesi
Name:MMP3
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 9982Activation peptidePRO_0000028726Add
BLAST
Chaini100 – 477378Stromelysin-1PRO_0000028727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence analysis
Disulfide bondi290 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ28397.
PRIDEiQ28397.

Interactioni

Protein-protein interaction databases

STRINGi9796.ENSECAP00000001652.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9Imodel-A100-267[»]
ProteinModelPortaliQ28397.
SMRiQ28397. Positions 33-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati287 – 33650Hemopexin 1Add
BLAST
Repeati337 – 38347Hemopexin 2Add
BLAST
Repeati385 – 43349Hemopexin 3Add
BLAST
Repeati434 – 47744Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine 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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ28397.
KOiK01394.
OMAiVAVCSAY.

Family and domain databases

CDDicd04278. 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.
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.
PROSITEiPS00024. 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.

Q28397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNLPILLLL CVAACSAYPL DRSARDEDSN MDLLQDYLEK YYDLGKEMRQ
60 70 80 90 100
YVRRKDSGPI VKKIQEMQKF LGLKVTGKLD SDTVEVMHKS RCGVPDVGHF
110 120 130 140 150
TTFPGMPKWS KTHLTYRIVN YTQDLPRDAV DSDVEKALKI WEEVTPLTFS
160 170 180 190 200
RIYEGEADIM ITFAVREHGD FFPFDGPGKV LAHAYPPGPG MNGDAHFDDD
210 220 230 240 250
EHWTKDASGI NFLLVAAHEL GHSLGLYHST NTEALMYPLY NTLKGPARVR
260 270 280 290 300
LSQDDVTGIQ SLYGPPPASP DSPVEPSEPE PPAPGTLAMC DPALSFDAIS
310 320 330 340 350
TLRGEILFFK DRYFWRKTFR TLVPEFHPIS SFWPSLPSGI DAAYEVTSRD
360 370 380 390 400
SVFIFKGNKF WAIRGNEEQA GYPRGIHTLG FPPTVRKIDA AIFDKEKQKT
410 420 430 440 450
YFFVEDKYWR FDEKRQSMEP GYPKQIAEDF PGIDSKLDAA FESFGFFYFF
460 470
SGSSQFEFDP NAKKVTHVLK SNSWFNC
Length:477
Mass (Da):54,190
Last modified:November 1, 1996 - v1
Checksum:i361CE1427E09A272
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461V → E (PubMed:9442239).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62529 mRNA. Translation: AAB05774.1.
RefSeqiNP_001075964.1. NM_001082495.2.
UniGeneiEca.8032.

Genome annotation databases

GeneIDi100034195.
KEGGiecb:100034195.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62529 mRNA. Translation: AAB05774.1.
RefSeqiNP_001075964.1. NM_001082495.2.
UniGeneiEca.8032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9Imodel-A100-267[»]
ProteinModelPortaliQ28397.
SMRiQ28397. Positions 33-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000001652.

Protein family/group databases

MEROPSiM10.005.

Proteomic databases

PaxDbiQ28397.
PRIDEiQ28397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100034195.
KEGGiecb:100034195.

Organism-specific databases

CTDi4314.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ28397.
KOiK01394.
OMAiVAVCSAY.

Family and domain databases

CDDicd04278. 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.
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.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP3_HORSE
AccessioniPrimary (citable) accession number: Q28397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.