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P09238 (MMP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromelysin-2

Short name=SL-2
EC=3.4.24.22
Alternative name(s):
Matrix metalloproteinase-10
Short name=MMP-10
Transin-2
Gene names
Name:MMP10
Synonyms:STMY2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Similar to stromelysin 1, but action on collagen types III, IV and V is weak. Ref.8

Cofactor

Binds 2 zinc ions per subunit. Ref.8

Calcium. Ref.8

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

Domain

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 similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Probable
Propeptide18 – 9881Activation peptide
PRO_0000028764
Chain99 – 476378Stromelysin-2
PRO_0000028765

Regions

Repeat286 – 33550Hemopexin 1
Repeat336 – 38247Hemopexin 2
Repeat384 – 43249Hemopexin 3
Repeat433 – 47644Hemopexin 4
Motif89 – 968Cysteine switch By similarity

Sites

Active site2181 Ref.8
Metal binding911Zinc; in inhibited form By similarity
Metal binding1671Zinc 1
Metal binding1691Zinc 1
Metal binding1821Zinc 1
Metal binding1951Zinc 1
Metal binding2171Zinc 2; catalytic
Metal binding2211Zinc 2; catalytic
Metal binding2271Zinc 2; catalytic

Amino acid modifications

Disulfide bond289 ↔ 476 By similarity

Natural variations

Natural variant41L → V. Ref.5
Corresponds to variant rs17435959 [ dbSNP | Ensembl ].
VAR_020949
Natural variant531R → K. Ref.4 Ref.5
Corresponds to variant rs486055 [ dbSNP | Ensembl ].
VAR_020950
Natural variant651G → R. Ref.5
Corresponds to variant rs17293607 [ dbSNP | Ensembl ].
VAR_020951
Natural variant1421E → Q in a breast cancer sample; somatic mutation. Ref.9
VAR_036139
Natural variant2261F → L. Ref.5
Corresponds to variant rs17860971 [ dbSNP | Ensembl ].
VAR_020952
Natural variant2821G → E. Ref.5
Corresponds to variant rs17860973 [ dbSNP | Ensembl ].
VAR_020953
Natural variant4401L → F. Ref.5
Corresponds to variant rs17860996 [ dbSNP | Ensembl ].
VAR_020954
Natural variant4751H → L. Ref.5
Corresponds to variant rs17861009 [ dbSNP | Ensembl ].
VAR_020955

Secondary structure

............................... 476
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09238 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 516DCDDFEF92A0D6

FASTA47654,151
        10         20         30         40         50         60 
MMHLAFLVLL CLPVCSAYPL SGAAKEEDSN KDLAQQYLEK YYNLEKDVKQ FRRKDSNLIV 

        70         80         90        100        110        120 
KKIQGMQKFL GLEVTGKLDT DTLEVMRKPR CGVPDVGHFS SFPGMPKWRK THLTYRIVNY 

       130        140        150        160        170        180 
TPDLPRDAVD SAIEKALKVW EEVTPLTFSR LYEGEADIMI SFAVKEHGDF YSFDGPGHSL 

       190        200        210        220        230        240 
AHAYPPGPGL YGDIHFDDDE KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN 

       250        260        270        280        290        300 
SFTELAQFRL SQDDVNGIQS LYGPPPASTE EPLVPTKSVP SGSEMPAKCD PALSFDAIST 

       310        320        330        340        350        360 
LRGEYLFFKD RYFWRRSHWN PEPEFHLISA FWPSLPSYLD AAYEVNSRDT VFIFKGNEFW 

       370        380        390        400        410        420 
AIRGNEVQAG YPRGIHTLGF PPTIRKIDAA VSDKEKKKTY FFAADKYWRF DENSQSMEQG 

       430        440        450        460        470 
FPRLIADDFP GVEPKVDAVL QAFGFFYFFS GSSQFEFDPN ARMVTHILKS NSWLHC 

« Hide

References

« Hide 'large scale' references
[1]"The collagenase gene family in humans consists of at least four members."
Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J., Breathnach R.
Biochem. J. 253:187-192(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Esophagus.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-53.
Tissue: Coronary artery.
[5]NIEHS SNPs program
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-4; LYS-53; ARG-65; LEU-226; GLU-282; PHE-440 AND LEU-475.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[8]"Crystal structure of the catalytic domain of human matrix metalloproteinase 10."
Bertini I., Calderone V., Fragai M., Luchinat C., Mangani S., Terni B.
J. Mol. Biol. 336:707-716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 99-263, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, CALCIUM-BINDING, ZINC-BINDING SITES.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-142.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07820 mRNA. Translation: CAA30679.1.
BT007442 mRNA. Translation: AAP36110.1.
AK222601 mRNA. Translation: BAD96321.1.
AK313960 mRNA. Translation: BAG36676.1.
AY744675 Genomic DNA. Translation: AAU21039.1.
CH471065 Genomic DNA. Translation: EAW67029.1.
BC002591 mRNA. Translation: AAH02591.1.
PIRKCHUS2. A28816.
RefSeqNP_002416.1. NM_002425.2.
UniGeneHs.2258.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3AX-ray2.10A/B/C99-263[»]
3V96X-ray1.90B99-263[»]
4ILWX-ray2.10D/F99-263[»]
ProteinModelPortalP09238.
SMRP09238. Positions 31-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110462. 1 interaction.
STRING9606.ENSP00000279441.

Chemistry

BindingDBP09238.
ChEMBLCHEMBL4270.

Protein family/group databases

MEROPSM10.006.

PTM databases

PhosphoSiteP09238.

Polymorphism databases

DMDM116869.

Proteomic databases

PaxDbP09238.
PRIDEP09238.

Protocols and materials databases

DNASU4319.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279441; ENSP00000279441; ENSG00000166670.
GeneID4319.
KEGGhsa:4319.
UCSCuc001phg.2. human.

Organism-specific databases

CTD4319.
GeneCardsGC11M102641.
HGNCHGNC:7156. MMP10.
HPACAB002159.
MIM185260. gene.
neXtProtNX_P09238.
PharmGKBPA30868.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270148.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidP09238.
KOK01396.
OMAMEQGFPR.
OrthoDBEOG7XPZ57.
PhylomeDBP09238.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP09238.
BgeeP09238.
CleanExHS_MMP10.
GenevestigatorP09238.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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.
IPR028700. Stromelysin_1/2.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF38. PTHR10201:SF38. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09238.
GeneWikiMMP10.
GenomeRNAi4319.
NextBio16993.
PROP09238.
SOURCESearch...

Entry information

Entry nameMMP10_HUMAN
AccessionPrimary (citable) accession number: P09238
Secondary accession number(s): B2R9X9, Q53HH9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM