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P09238

- MMP10_HUMAN

UniProt

P09238 - MMP10_HUMAN

Protein

Stromelysin-2

Gene

MMP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    Binds 2 zinc ions per subunit.1 Publication
    Calcium.1 Publication

    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

    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.
    REACT_201925. Degradation of the extracellular matrix.

    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

    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

    ArrayExpressiP09238.
    BgeeiP09238.
    CleanExiHS_MMP10.
    GenevestigatoriP09238.

    Organism-specific databases

    HPAiCAB002159.

    Interactioni

    Protein-protein interaction databases

    BioGridi110462. 1 interaction.
    STRINGi9606.ENSP00000279441.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MMHLAFLVLL CLPVCSAYPL SGAAKEEDSN KDLAQQYLEK YYNLEKDVKQ    50
    FRRKDSNLIV KKIQGMQKFL GLEVTGKLDT DTLEVMRKPR CGVPDVGHFS 100
    SFPGMPKWRK THLTYRIVNY TPDLPRDAVD SAIEKALKVW EEVTPLTFSR 150
    LYEGEADIMI SFAVKEHGDF YSFDGPGHSL AHAYPPGPGL YGDIHFDDDE 200
    KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN SFTELAQFRL 250
    SQDDVNGIQS LYGPPPASTE EPLVPTKSVP SGSEMPAKCD PALSFDAIST 300
    LRGEYLFFKD RYFWRRSHWN PEPEFHLISA FWPSLPSYLD AAYEVNSRDT 350
    VFIFKGNEFW AIRGNEVQAG YPRGIHTLGF PPTIRKIDAA VSDKEKKKTY 400
    FFAADKYWRF DENSQSMEQG FPRLIADDFP GVEPKVDAVL QAFGFFYFFS 450
    GSSQFEFDPN ARMVTHILKS NSWLHC 476
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 1 interaction.
    STRINGi 9606.ENSP00000279441.

    Chemistry

    BindingDBi P09238.
    ChEMBLi CHEMBL4270.

    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.
    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.
    REACT_201925. Degradation of the extracellular matrix.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi P09238.
    Bgeei P09238.
    CleanExi HS_MMP10.
    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

    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: October 1, 2014
    This is version 158 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