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Protein

Matrix metalloproteinase-2

Gene

Mmp2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Has metalloproteinase activity (PubMed:11967260). Required for larval tissue histolysis during metamorphosis and is involved in pupal head eversion and fusion of the wing imaginal tissue (PubMed:12530966). Required for growth of the dorsal air sac primordium and development of the dorsal air sacs (PubMed:19751719). Promotes embryonic motor axon fasciculation (PubMed:18045838). Cleaves and activates frac to promote motor axon bundling during outgrowth (PubMed:21471368). Promotes the reshaping of adult sensory neuron dendrites from a radial to lattice-like shape which occurs after eclosion by degrading the basement membrane on which the dendrites grow (PubMed:20412776). Involved in inhibition of follicle stem cell proliferation by cleaving Dlp, inhibiting its interaction with wg and preventing Dlp-mediated spreading of wg to follicle stem cells to enhance their proliferation (PubMed:25267296). Plays a role in wound healing (PubMed:22262460). Involved in fat body dissociation which occurs during metamorphosis by degrading basement membrane components, leading to destruction of cell-basement membrane junctions (PubMed:25520167). Required for posterior follicle cell degradation and ovulation (PubMed:25695427).10 Publications

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi257 – 2571Zinc; catalyticPROSITE-ProRule annotation
Active sitei258 – 2581PROSITE-ProRule annotation
Metal bindingi261 – 2611Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi267 – 2671Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • endopeptidase activity Source: FlyBase
  • metalloendopeptidase activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of innate immune response Source: FlyBase
  • adult fat body development Source: FlyBase
  • basement membrane disassembly Source: FlyBase
  • basement membrane organization Source: FlyBase
  • cell-cell junction organization Source: FlyBase
  • fasciculation of motor neuron axon Source: FlyBase
  • imaginal disc eversion Source: FlyBase
  • imaginal disc fusion, thorax closure Source: FlyBase
  • lateral inhibition Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • negative regulation of canonical Wnt signaling pathway Source: FlyBase
  • negative regulation of fibroblast growth factor receptor signaling pathway Source: FlyBase
  • negative regulation of Wnt signaling pathway Source: FlyBase
  • oogenesis Source: FlyBase
  • open tracheal system development Source: FlyBase
  • ovulation Source: FlyBase
  • phototransduction Source: FlyBase
  • protein processing Source: FlyBase
  • tracheal outgrowth, open tracheal system Source: FlyBase
  • tracheal pit formation in open tracheal system Source: FlyBase
  • wound healing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.036.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-21 Publication (EC:3.4.24.-Curated)
Short name:
Dm2-MMP1 Publication
Gene namesi
Name:Mmp2Imported
ORF Names:CG1794Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033438. Mmp2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini? – 738ExtracellularSequence analysis
Transmembranei739 – 75618HelicalSequence analysisAdd
BLAST
Topological domaini757 – 7582CytoplasmicSequence analysis

GO - Cellular componenti

  • dendrite Source: FlyBase
  • external side of plasma membrane Source: FlyBase
  • extracellular matrix Source: InterPro
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Defective larval tissue histolysis and epithelial fusion during metamorphosis (PubMed:12530966). Impaired fasciculation of ISNb nerves (PubMed:18045838).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 758Matrix metalloproteinase-2CuratedPRO_0000434512
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – ?Activation peptideCuratedPRO_0000434511

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi516 ↔ 707Curated

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ8MPP3.
PRIDEiQ5BIL2.

Expressioni

Tissue specificityi

Widely expressed during embryogenesis including in the mesoderm, developing gut, central and peripheral nervous systems and imaginal disks (PubMed:12530966). In the embryonic nervous system, expressed in neurons and glia (PubMed:18045838). In third instar larvae, strongly expressed in the morphogenetic furrow of eye imaginal disks and in the optic lobe region of the brain (PubMed:11967260). Expressed in posterior follicle cells in all mature stage 14 follicles but not in earlier follicles and is also expressed in some anterior follicle cells that help form dorsal eggshell structures (PubMed:25695427).4 Publications

Developmental stagei

Expressed in embryos beginning at 8-12 hours, in first instar larvae, in pupae and in male and female adults with highest expression in early pupae (PubMed:11967260, PubMed:12530966). In epithelial cells, weakly expressed at late pupal stages with significantly elevated expression at the early adult stage of 0-4 hours after eclosion and levels returning to normal by 3 days after eclosion (PubMed:20412776).3 Publications

Gene expression databases

BgeeiQ5BIL2.
ExpressionAtlasiQ8MPP3. differential.
GenevisibleiQ8MPP3. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0087585.

Structurei

3D structure databases

ProteinModelPortaliQ8MPP3.
SMRiQ8MPP3. Positions 78-327, 520-691.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati513 – 56149Hemopexin 1PROSITE-ProRule annotationAdd
BLAST
Repeati565 – 61046Hemopexin 2PROSITE-ProRule annotationAdd
BLAST
Repeati612 – 65948Hemopexin 3PROSITE-ProRule annotationAdd
BLAST
Repeati660 – 70748Hemopexin 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi314 – 32310Thr-richPROSITE-ProRule annotation
Compositional biasi350 – 477128Arg-richPROSITE-ProRule annotationAdd
BLAST
Compositional biasi355 – 469115Glu-richPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00830000128254.
HOGENOMiHOG000244884.
OMAiDDSHGTN.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ8MPP3.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform BImported (identifier: Q8MPP3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFSKYVLATL LALFAQSMCI QELSLPPEGS HSTAATRSKK AKTAISEDIM
60 70 80 90 100
YNYLMQFDYL PKSDLETGAL RTEDQLKEAI RSLQSFGNIT VTGEIDSATA
110 120 130 140 150
RLIQKPRCGV GDRRSADSFS PDNLYHEIGS NVRVRRFALQ GPKWSRTDLT
160 170 180 190 200
WSMVNRSMPD ASKVERMVQT ALDVWANHSK LTFREVYSDQ ADIQILFARR
210 220 230 240 250
AHGDGYKFDG PGQVLAHAFY PGEGRGGDAH FDADETWNFD GESDDSHGTN
260 270 280 290 300
FLNVALHELG HSLGLAHSAI PDAVMFPWYQ NNEVAGNLPD DDRYGIQQLY
310 320 330 340 350
GTKEKTWGPY KPQTTTTTTT TTTMRAMIYR ADKPAYWPWN NPSNNPNNDR
360 370 380 390 400
NRARERQEEE RRRQEKERRR QEEERRHQEE ERRRQVEERQ RQEEERWRQE
410 420 430 440 450
QERQEEENRR RKIEHKSQWE RNPSKERNRP RERQEMERRR QEQERQEQER
460 470 480 490 500
QEQEDRRRER ERDRQLEWER RNRNGAREPV TPTANTTPRP TNKPYPTVHR
510 520 530 540 550
QHHHHNKPRK PKPDSCMTYY DAISIIRGEL FIFRGPYLWR IGTSGLYNGY
560 570 580 590 600
PTEIRRHWSA LPENLTKVDA VYENKQRQIV FFIGREYYVF NSVMLAPGFP
610 620 630 640 650
KPLASLGLPP TLTHIDASFV WGHNNRTYMT SGTLYWRIDD YTGQVELDYP
660 670 680 690 700
RDMSIWSGVG YNIDAAFQYL DGKTYFFKNL GYWEFNDDRM KVAHARAKLS
710 720 730 740 750
ARRWMQCARS ANEVDDEQRW TASLVSEGEE TGRSGSRELR INHFILSILL

LAIANWRS
Length:758
Mass (Da):89,137
Last modified:October 1, 2002 - v1
Checksum:i0F06C262A5F4CB4A
GO
Isoform CImported (identifier: Q8MPP3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.

Note: Gene prediction based on EST data.Curated
Show »
Length:606
Mass (Da):72,128
Checksum:i0541E4F0FE791B88
GO
Isoform DImported (identifier: Q8MPP3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MFSKYVLATL...KWSRTDLTWS → MLSLWPRRQF...SWRLFLCFLR

Note: Gene prediction based on EST data.Curated
Show »
Length:650
Mass (Da):77,261
Checksum:iB6ABCF9DA98746DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431T → N in AAX33360 (Ref. 4) Curated
Sequence conflicti412 – 4121K → E in AAX33360 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 152152Missing in isoform C. VSP_057940Add
BLAST
Alternative sequencei1 – 152152MFSKY…DLTWS → MLSLWPRRQFSAAAVLLHFG CTWSLVLATRLAVISWRLFL CFLR in isoform D. VSP_057941Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ289232 mRNA. Translation: CAC81969.1.
AE013599 Genomic DNA. Translation: AAF58911.6.
AE013599 Genomic DNA. Translation: AAS64885.1.
AE013599 Genomic DNA. Translation: AGB93363.1.
BT021212 mRNA. Translation: AAX33360.1.
BT150239 mRNA. Translation: AGV77141.1.
RefSeqiNP_001260830.1. NM_001273901.1. [Q8MPP3-2]
NP_610511.3. NM_136667.3. [Q8MPP3-3]
NP_995788.1. NM_206066.3. [Q8MPP3-1]
UniGeneiDm.11246.

Genome annotation databases

EnsemblMetazoaiFBtr0088501; FBpp0087585; FBgn0033438. [Q8MPP3-1]
GeneIDi35997.
KEGGidme:Dmel_CG1794.
UCSCiCG1794-RB. d. melanogaster. [Q8MPP3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ289232 mRNA. Translation: CAC81969.1.
AE013599 Genomic DNA. Translation: AAF58911.6.
AE013599 Genomic DNA. Translation: AAS64885.1.
AE013599 Genomic DNA. Translation: AGB93363.1.
BT021212 mRNA. Translation: AAX33360.1.
BT150239 mRNA. Translation: AGV77141.1.
RefSeqiNP_001260830.1. NM_001273901.1. [Q8MPP3-2]
NP_610511.3. NM_136667.3. [Q8MPP3-3]
NP_995788.1. NM_206066.3. [Q8MPP3-1]
UniGeneiDm.11246.

3D structure databases

ProteinModelPortaliQ8MPP3.
SMRiQ8MPP3. Positions 78-327, 520-691.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0087585.

Protein family/group databases

MEROPSiM10.036.

Proteomic databases

PaxDbiQ8MPP3.
PRIDEiQ5BIL2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088501; FBpp0087585; FBgn0033438. [Q8MPP3-1]
GeneIDi35997.
KEGGidme:Dmel_CG1794.
UCSCiCG1794-RB. d. melanogaster. [Q8MPP3-1]

Organism-specific databases

CTDi4313.
FlyBaseiFBgn0033438. Mmp2.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00830000128254.
HOGENOMiHOG000244884.
OMAiDDSHGTN.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ8MPP3.

Miscellaneous databases

ChiTaRSiMmp2. fly.
GenomeRNAii35997.
PROiQ8MPP3.

Gene expression databases

BgeeiQ5BIL2.
ExpressionAtlasiQ8MPP3. differential.
GenevisibleiQ8MPP3. DM.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression."
    Llano E., Adam G., Pendas A.M., Quesada V., Sanchez L.M., Santamaria I., Noselli S., Lopez-Otin C.
    J. Biol. Chem. 277:23321-23329(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  3. Cited for: GENOME REANNOTATION.
    Strain: BerkeleyImported.
  4. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development."
    Page-McCaw A., Serano J., Sante J.M., Rubin G.M.
    Dev. Cell 4:95-106(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  6. "Matrix metalloproteinases promote motor axon fasciculation in the Drosophila embryo."
    Miller C.M., Page-McCaw A., Broihier H.T.
    Development 135:95-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  7. "Regulation of Drosophila matrix metalloprotease Mmp2 is essential for wing imaginal disc:trachea association and air sac tubulogenesis."
    Guha A., Lin L., Kornberg T.B.
    Dev. Biol. 335:317-326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Dendrite reshaping of adult Drosophila sensory neurons requires matrix metalloproteinase-mediated modification of the basement membranes."
    Yasunaga K., Kanamori T., Morikawa R., Suzuki E., Emoto K.
    Dev. Cell 18:621-632(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  9. "Drosophila MMP2 regulates the matrix molecule faulty attraction (Frac) to promote motor axon targeting in Drosophila."
    Miller C.M., Liu N., Page-McCaw A., Broihier H.T.
    J. Neurosci. 31:5335-5347(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A secreted MMP is required for reepithelialization during wound healing."
    Stevens L.J., Page-McCaw A.
    Mol. Biol. Cell 23:1068-1079(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "A matrix metalloproteinase mediates long-distance attenuation of stem cell proliferation."
    Wang X., Page-McCaw A.
    J. Cell Biol. 206:923-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Mmp1 and Mmp2 cooperatively induce Drosophila fat body cell dissociation with distinct roles."
    Jia Q., Liu Y., Liu H., Li S.
    Sci. Rep. 4:7535-7535(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Matrix metalloproteinase 2 is required for ovulation and corpus luteum formation in Drosophila."
    Deady L.D., Shen W., Mosure S.A., Spradling A.C., Sun J.
    PLoS Genet. 11:E1004989-E1004989(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiD2MP_DROME
AccessioniPrimary (citable) accession number: Q8MPP3
Secondary accession number(s): A0A0B4KFG9, A0A0C4DHC9, Q5BIL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.