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P09238

- MMP10_HUMAN

UniProt

P09238 - MMP10_HUMAN

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Protein

Stromelysin-2

Gene

MMP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Zinc; in inhibited formBy similarity
Metal bindingi167 – 1671Zinc 1
Metal bindingi169 – 1691Zinc 1
Metal bindingi182 – 1821Zinc 1
Metal bindingi195 – 1951Zinc 1
Metal bindingi217 – 2171Zinc 2; catalytic
Active sitei218 – 21811 PublicationPROSITE-ProRule annotation
Metal bindingi221 – 2211Zinc 2; catalytic
Metal bindingi227 – 2271Zinc 2; catalytic

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: ProtInc
  3. zinc ion binding Source: ProtInc

GO - Biological processi

  1. collagen catabolic process Source: Reactome
  2. extracellular matrix disassembly Source: Reactome
  3. extracellular matrix organization Source: Reactome
  4. proteolysis Source: ProtInc
  5. regulation of cell migration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.006.

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
Transin-2
Gene namesi
Name:MMP10
Synonyms:STMY2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7156. MMP10.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: ProtInc
  3. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717CuratedAdd
BLAST
Propeptidei18 – 9881Activation peptidePRO_0000028764Add
BLAST
Chaini99 – 476378Stromelysin-2PRO_0000028765Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP09238.
PRIDEiP09238.

PTM databases

PhosphoSiteiP09238.

Expressioni

Gene expression databases

BgeeiP09238.
CleanExiHS_MMP10.
ExpressionAtlasiP09238. baseline and differential.
GenevestigatoriP09238.

Organism-specific databases

HPAiCAB002159.

Interactioni

Protein-protein interaction databases

BioGridi110462. 2 interactions.
STRINGi9606.ENSP00000279441.

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1177Combined sources
Helixi126 – 14116Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1637Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi175 – 1839Combined sources
Beta strandi186 – 1883Combined sources
Turni189 – 1924Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi202 – 2109Combined sources
Helixi211 – 22313Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi237 – 2393Combined sources
Helixi242 – 2476Combined sources
Helixi252 – 26211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3AX-ray2.10A/B/C99-263[»]
3V96X-ray1.90B99-263[»]
4ILWX-ray2.10D/F99-263[»]
ProteinModelPortaliP09238.
SMRiP09238. Positions 33-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09238.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 968Cysteine 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

eggNOGiNOG270148.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP09238.
KOiK01396.
OMAiMEQGFPR.
OrthoDBiEOG7XPZ57.
PhylomeDBiP09238.
TreeFamiTF315428.

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.

P09238-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMHLAFLVLL CLPVCSAYPL SGAAKEEDSN KDLAQQYLEK YYNLEKDVKQ
60 70 80 90 100
FRRKDSNLIV KKIQGMQKFL GLEVTGKLDT DTLEVMRKPR CGVPDVGHFS
110 120 130 140 150
SFPGMPKWRK THLTYRIVNY TPDLPRDAVD SAIEKALKVW EEVTPLTFSR
160 170 180 190 200
LYEGEADIMI SFAVKEHGDF YSFDGPGHSL AHAYPPGPGL YGDIHFDDDE
210 220 230 240 250
KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN SFTELAQFRL
260 270 280 290 300
SQDDVNGIQS LYGPPPASTE EPLVPTKSVP SGSEMPAKCD PALSFDAIST
310 320 330 340 350
LRGEYLFFKD RYFWRRSHWN PEPEFHLISA FWPSLPSYLD AAYEVNSRDT
360 370 380 390 400
VFIFKGNEFW AIRGNEVQAG YPRGIHTLGF PPTIRKIDAA VSDKEKKKTY
410 420 430 440 450
FFAADKYWRF DENSQSMEQG FPRLIADDFP GVEPKVDAVL QAFGFFYFFS
460 470
GSSQFEFDPN ARMVTHILKS NSWLHC
Length:476
Mass (Da):54,151
Last modified:July 1, 1989 - v1
Checksum:i516DCDDFEF92A0D6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41L → V.1 Publication
Corresponds to variant rs17435959 [ dbSNP | Ensembl ].
VAR_020949
Natural varianti53 – 531R → K.2 Publications
Corresponds to variant rs486055 [ dbSNP | Ensembl ].
VAR_020950
Natural varianti65 – 651G → R.1 Publication
Corresponds to variant rs17293607 [ dbSNP | Ensembl ].
VAR_020951
Natural varianti142 – 1421E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036139
Natural varianti226 – 2261F → L.1 Publication
Corresponds to variant rs17860971 [ dbSNP | Ensembl ].
VAR_020952
Natural varianti282 – 2821G → E.1 Publication
Corresponds to variant rs17860973 [ dbSNP | Ensembl ].
VAR_020953
Natural varianti440 – 4401L → F.1 Publication
Corresponds to variant rs17860996 [ dbSNP | Ensembl ].
VAR_020954
Natural varianti475 – 4751H → L.1 Publication
Corresponds to variant rs17861009 [ dbSNP | Ensembl ].
VAR_020955

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8321.1.
PIRiA28816. KCHUS2.
RefSeqiNP_002416.1. NM_002425.2.
UniGeneiHs.2258.

Genome annotation databases

EnsembliENST00000279441; ENSP00000279441; ENSG00000166670.
GeneIDi4319.
KEGGihsa:4319.
UCSCiuc001phg.2. human.

Polymorphism databases

DMDMi116869.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS8321.1.
PIRi A28816. KCHUS2.
RefSeqi NP_002416.1. NM_002425.2.
UniGenei Hs.2258.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q3A X-ray 2.10 A/B/C 99-263 [» ]
3V96 X-ray 1.90 B 99-263 [» ]
4ILW X-ray 2.10 D/F 99-263 [» ]
ProteinModelPortali P09238.
SMRi P09238. Positions 33-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110462. 2 interactions.
STRINGi 9606.ENSP00000279441.

Chemistry

BindingDBi P09238.
ChEMBLi CHEMBL4270.
DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.006.

PTM databases

PhosphoSitei P09238.

Polymorphism databases

DMDMi 116869.

Proteomic databases

PaxDbi P09238.
PRIDEi P09238.

Protocols and materials databases

DNASUi 4319.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000279441 ; ENSP00000279441 ; ENSG00000166670 .
GeneIDi 4319.
KEGGi hsa:4319.
UCSCi uc001phg.2. human.

Organism-specific databases

CTDi 4319.
GeneCardsi GC11M102641.
HGNCi HGNC:7156. MMP10.
HPAi CAB002159.
MIMi 185260. gene.
neXtProti NX_P09238.
PharmGKBi PA30868.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270148.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P09238.
KOi K01396.
OMAi MEQGFPR.
OrthoDBi EOG7XPZ57.
PhylomeDBi P09238.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Miscellaneous databases

EvolutionaryTracei P09238.
GeneWikii MMP10.
GenomeRNAii 4319.
NextBioi 16993.
PROi P09238.
SOURCEi Search...

Gene expression databases

Bgeei P09238.
CleanExi HS_MMP10.
ExpressionAtlasi P09238. baseline and differential.
Genevestigatori P09238.

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

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-142.

Entry informationi

Entry nameiMMP10_HUMAN
AccessioniPrimary (citable) accession number: P09238
Secondary accession number(s): B2R9X9, Q53HH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 160 of the entry and version 1 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, 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

External Data

Dasty 3