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Protein

Metalloendoproteinase 1-MMP

Gene

1MMP

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (PubMed:10574937). Can cleave myelin basic protein as well as fluorigenic peptide substrates, McaPLANvaDpaAR-NH2 and McaPChaGNvaHADpa-NH2 4-fold more efficiently than McaPLGLDpaAR-NH2 (QF24) (PubMed:10574937). Active on myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH2 (QF24) and beta-casein (PubMed:24156403).1 Publication2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Inhibited by human TIMP-1 and TIMP-2 and by the peptide hydroxamate inhibitor (BB-94) (PubMed:10574937). Repressed by acetohydroxamic acid (AHA) (PubMed:24156403).2 Publications

pH dependencei

Optimum pH is 7-8.1 Publication

Temperature dependencei

Optimum temperature is 45-55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Zinc 2; in inhibited formBy similarity
Metal bindingi211 – 2111Calcium 2By similarity
Metal bindingi221 – 2211Zinc 1By similarity
Metal bindingi223 – 2231Zinc 1By similarity
Metal bindingi228 – 2281Calcium 1By similarity
Metal bindingi229 – 2291Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi236 – 2361Zinc 1By similarity
Metal bindingi243 – 2431Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi246 – 2461Zinc 1By similarity
Metal bindingi248 – 2481Calcium 1By similarity
Metal bindingi251 – 2511Calcium 1By similarity
Metal bindingi275 – 2751Zinc 2; catalyticPROSITE-ProRule annotationBy similarity
Active sitei276 – 2761PROSITE-ProRule annotation
Metal bindingi279 – 2791Zinc 2; catalyticPROSITE-ProRule annotationBy similarity
Metal bindingi285 – 2851Zinc 2; catalyticPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • metalloendopeptidase activity Source: UniProtKB
  • zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G16640-MONOMER.
ReactomeiR-ATH-1592389. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiM10.A04.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloendoproteinase 1-MMP1 Publication (EC:3.4.24.-Curated)
Short name:
At1-MMP1 Publication
Gene namesi
Name:1MMP1 Publication
Ordered Locus Names:At4g16640Imported
ORF Names:dl4345cImported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G16640.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: TAIR
  • extracellular matrix Source: InterPro
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 149121Activation peptideBy similarityPRO_0000433519Add
BLAST
Chaini150 – 339190Metalloendoproteinase 1-MMPSequence analysisPRO_0000433520Add
BLAST
Propeptidei340 – 36425Removed in mature formSequence analysisPRO_0000433521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi338 – 3381N-linked (GlcNAc...)PROSITE-ProRule annotation
Lipidationi339 – 3391GPI-anchor amidated glycine1 Publication

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

Proteomic databases

PaxDbiO23507.
PRIDEiO23507.

Expressioni

Tissue specificityi

Mostly expressed in flowers, roots and stems, and, to a lower extent, in leaves.1 Publication

Gene expression databases

GenevisibleiO23507. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G16640.1.

Structurei

3D structure databases

ProteinModelPortaliO23507.
SMRiO23507. Positions 96-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi128 – 1358Cysteine 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.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000239471.
InParanoidiO23507.
OMAiFEREESR.
PhylomeDBiO23507.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O23507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRNLIYRRN RALCFVLILF CFPYRFGARN TPEAEQSTAK ATQIIHVSNS
60 70 80 90 100
TWHDFSRLVD VQIGSHVSGV SELKRYLHRF GYVNDGSEIF SDVFDGPLES
110 120 130 140 150
AISLYQENLG LPITGRLDTS TVTLMSLPRC GVSDTHMTIN NDFLHTTAHY
160 170 180 190 200
TYFNGKPKWN RDTLTYAISK THKLDYLTSE DVKTVFRRAF SQWSSVIPVS
210 220 230 240 250
FEEVDDFTTA DLKIGFYAGD HGDGLPFDGV LGTLAHAFAP ENGRLHLDAA
260 270 280 290 300
ETWIVDDDLK GSSEVAVDLE SVATHEIGHL LGLGHSSQES AVMYPSLRPR
310 320 330 340 350
TKKVDLTVDD VAGVLKLYGP NPKLRLDSLT QSEDSIKNGT VSHRFLSGNF
360
IGYVLLVVGL ILFL
Length:364
Mass (Da):40,528
Last modified:January 1, 1998 - v1
Checksum:i844C5D612EAED662
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301N → I in AAO42162 (PubMed:14593172).Curated
Sequence conflicti84 – 841N → K in AAM62476 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97341 Genomic DNA. Translation: CAB10439.1.
AL161544 Genomic DNA. Translation: CAB78706.1.
CP002687 Genomic DNA. Translation: AEE83779.1.
BT004141 mRNA. Translation: AAO42162.1.
AY085244 mRNA. Translation: AAM62476.1.
PIRiE71433.
RefSeqiNP_193397.1. NM_117765.3.
UniGeneiAt.33062.

Genome annotation databases

EnsemblPlantsiAT4G16640.1; AT4G16640.1; AT4G16640.
GeneIDi827365.
GrameneiAT4G16640.1; AT4G16640.1; AT4G16640.
KEGGiath:AT4G16640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97341 Genomic DNA. Translation: CAB10439.1.
AL161544 Genomic DNA. Translation: CAB78706.1.
CP002687 Genomic DNA. Translation: AEE83779.1.
BT004141 mRNA. Translation: AAO42162.1.
AY085244 mRNA. Translation: AAM62476.1.
PIRiE71433.
RefSeqiNP_193397.1. NM_117765.3.
UniGeneiAt.33062.

3D structure databases

ProteinModelPortaliO23507.
SMRiO23507. Positions 96-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G16640.1.

Protein family/group databases

MEROPSiM10.A04.

Proteomic databases

PaxDbiO23507.
PRIDEiO23507.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G16640.1; AT4G16640.1; AT4G16640.
GeneIDi827365.
GrameneiAT4G16640.1; AT4G16640.1; AT4G16640.
KEGGiath:AT4G16640.

Organism-specific databases

TAIRiAT4G16640.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000239471.
InParanoidiO23507.
OMAiFEREESR.
PhylomeDBiO23507.

Enzyme and pathway databases

BioCyciARA:AT4G16640-MONOMER.
ReactomeiR-ATH-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

PROiO23507.

Gene expression databases

GenevisibleiO23507. AT.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Matrix metalloproteinase homologues from Arabidopsis thaliana. Expression and activity."
    Maidment J.M., Moore D., Murphy G.P., Murphy G., Clark I.M.
    J. Biol. Chem. 274:34706-34710(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
  7. "Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis."
    Borner G.H.H., Lilley K.S., Stevens T.J., Dupree P.
    Plant Physiol. 132:568-577(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS] AT GLY-339.
    Strain: cv. Columbia.
    Tissue: Callus.
  8. "Family-wide characterization of matrix metalloproteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity."
    Marino G., Huesgen P.F., Eckhard U., Overall C.M., Schroeder W.P., Funk C.
    Biochem. J. 457:335-346(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, GENE FAMILY.
    Strain: cv. Columbia.

Entry informationi

Entry namei1MMP_ARATH
AccessioniPrimary (citable) accession number: O23507
Secondary accession number(s): Q84W77, Q8LET7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.