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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)DescriptionActionsGraphical viewLength
Metal bindingi92Zinc 2; in inhibited formBy similarity1
Metal bindingi124Calcium 1By similarity1
Metal bindingi158Calcium 2By similarity1
Metal bindingi168Zinc 1By similarity1
Metal bindingi170Zinc 1By similarity1
Metal bindingi175Calcium 3By similarity1
Metal bindingi176Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi180Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi183Zinc 1By similarity1
Metal bindingi190Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi192Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi194Calcium 2By similarity1
Metal bindingi196Zinc 1By similarity1
Metal bindingi198Calcium 3By similarity1
Metal bindingi199Calcium 1By similarity1
Metal bindingi201Calcium 1By similarity1
Metal bindingi201Calcium 3By similarity1
Metal bindingi218Zinc 2; catalyticBy similarity1
Active sitei219PROSITE-ProRule annotation1
Metal bindingi222Zinc 2; catalyticBy similarity1
Metal bindingi228Zinc 2; catalyticBy similarity1
Metal bindingi297Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi389Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi438Calcium 4; via carbonyl oxygenBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002872618 – 99Activation peptideAdd BLAST82
ChainiPRO_0000028727100 – 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

PaxDbiQ28397.
PRIDEiQ28397.

Interactioni

Protein-protein interaction databases

STRINGi9796.ENSECAP00000001652.

Structurei

3D structure databases

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

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.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ28397.
KOiK01394.
OMAiVAVCSAY.

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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti346V → E (PubMed:9442239).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L9Imodel-A100-267[»]
ProteinModelPortaliQ28397.
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

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.
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: November 30, 2016
This is version 133 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.