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P07152

- MMP10_RAT

UniProt

P07152 - MMP10_RAT

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Protein
Stromelysin-2
Gene
Mmp10
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.

Catalytic activityi

Similar to stromelysin 1, but action on collagen types III, IV and V is weak.

Cofactori

Binds 2 zinc ions per subunit By similarity.
Calcium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc; in inhibited form By similarity
Metal bindingi168 – 1681Zinc 1 By similarity
Metal bindingi170 – 1701Zinc 1 By similarity
Metal bindingi183 – 1831Zinc 1 By similarity
Metal bindingi196 – 1961Zinc 1 By similarity
Metal bindingi218 – 2181Zinc 2; catalytic By similarity
Active sitei219 – 2191 By similarity
Metal bindingi222 – 2221Zinc 2; catalytic By similarity
Metal bindingi228 – 2281Zinc 2; catalytic By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-2 (EC:3.4.24.22)
Short name:
SL-2
Alternative name(s):
Matrix metalloproteinase-10
Short name:
MMP-10
Transformation-associated protein 34A
Transin-2
Gene namesi
Name:Mmp10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620192. Mmp10.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Inferred
Add
BLAST
Propeptidei18 – 9982Activation peptide By similarity
PRO_0000028768Add
BLAST
Chaini100 – 476377Stromelysin-2
PRO_0000028769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi289 ↔ 476 By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP07152.
PRIDEiP07152.

Expressioni

Gene expression databases

GenevestigatoriP07152.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013118.

Structurei

3D structure databases

ProteinModelPortaliP07152.
SMRiP07152. Positions 33-267.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati286 – 33550Hemopexin 1
Add
BLAST
Repeati336 – 38247Hemopexin 2
Add
BLAST
Repeati384 – 43249Hemopexin 3
Add
BLAST
Repeati433 – 47644Hemopexin 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switch By 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.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG270148.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP07152.
KOiK01396.
PhylomeDBiP07152.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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.
[Graphical view]
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.

P07152-1 [UniParc]FASTAAdd to Basket

« Hide

MEPLAILVLL CFPICSAYPL HGAVRQDHST MDLAQQYLEK YYNFRKNEKQ    50
FFKRKDSSPV VKKIEEMQKF LGLEMTGKLD SNTVEMMHKP RCGVPDVGGF 100
STFPGSPKWR KNHISYRIVN YTLDLPRESV DSAIERALKV WEEVTPLTFS 150
RISEGEADIM ISFAVGEHGD FYPFDGVGQS LAHAYPPGPG FYGDAHFDDD 200
EKWSLGPSGT NLFLVAAHEL GHSLGLFHSN NKESLMYPVY RFSTSQANIR 250
LSQDDIEGIQ SLYGARPSSD ATVVPVPSVS PKPETPVKCD PALSFDAVTM 300
LRGEFLFFKD RHFWRRTQWN PEPEFHLISA FWPSLPSGLD AAYEANNKDR 350
VLIFKGSQFW AVRGNEVQAG YPKRIHTLGF PPTVKKIDAA VFEKEKKKTY 400
FFVGDKYWRF DETRQLMDKG FPRLITDDFP GIEPQVDAVL HAFGFFYFFC 450
GSSQFEFDPN ARTVTHTLKS NSWLLC 476
Length:476
Mass (Da):54,222
Last modified:April 1, 1988 - v1
Checksum:iB556B6FB1D8BA7EE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05083 mRNA. Translation: CAA28739.1.
M65253 mRNA. Translation: AAA42202.1.
PIRiB26403. KCRTS2.
RefSeqiNP_598198.1. NM_133514.1.
UniGeneiRn.9946.

Genome annotation databases

GeneIDi117061.
KEGGirno:117061.
UCSCiRGD:620192. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05083 mRNA. Translation: CAA28739.1 .
M65253 mRNA. Translation: AAA42202.1 .
PIRi B26403. KCRTS2.
RefSeqi NP_598198.1. NM_133514.1.
UniGenei Rn.9946.

3D structure databases

ProteinModelPortali P07152.
SMRi P07152. Positions 33-267.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000013118.

Protein family/group databases

MEROPSi M10.011.

Proteomic databases

PaxDbi P07152.
PRIDEi P07152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 117061.
KEGGi rno:117061.
UCSCi RGD:620192. rat.

Organism-specific databases

CTDi 4319.
RGDi 620192. Mmp10.

Phylogenomic databases

eggNOGi NOG270148.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P07152.
KOi K01396.
PhylomeDBi P07152.

Miscellaneous databases

NextBioi 619922.

Gene expression databases

Genevestigatori P07152.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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.
[Graphical view ]
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene."
    Breathnach R., Matrisian L.M., Gesnel M.-C., Staub A., Leroy P.
    Nucleic Acids Res. 15:1139-1151(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and characterization of v-mos-activated transformation-associated proteins."
    Chan J.C., Scanlon M., Zhang H.Z., Jia L.B., Yu D., Hung M.C., French M., Eastman E.M.
    J. Biol. Chem. 267:1099-1103(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMMP10_RAT
AccessioniPrimary (citable) accession number: P07152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 129 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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