2MMP_ARATH
ID 2MMP_ARATH Reviewed; 378 AA.
AC O04529; Q0WVU1;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Metalloendoproteinase 2-MMP {ECO:0000303|PubMed:10574937};
DE Short=At2-MMP {ECO:0000303|PubMed:10574937};
DE EC=3.4.24.- {ECO:0000305};
DE Flags: Precursor;
GN Name=2MMP {ECO:0000303|PubMed:10574937};
GN Synonyms=MMP {ECO:0000312|EMBL:AEE35027.1};
GN OrderedLocusNames=At1g70170 {ECO:0000312|Araport:AT1G70170};
GN ORFNames=F20P5.11 {ECO:0000312|EMBL:AAB61099.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10574937; DOI=10.1074/jbc.274.49.34706;
RA Maidment J.M., Moore D., Murphy G.P., Murphy G., Clark I.M.;
RT "Matrix metalloproteinase homologues from Arabidopsis thaliana. Expression
RT and activity.";
RL J. Biol. Chem. 274:34706-34710(1999).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY METHYL JASMONATE AND CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=11726650; DOI=10.1074/jbc.m106197200;
RA Golldack D., Popova O.V., Dietz K.-J.;
RT "Mutation of the matrix metalloproteinase At2-MMP inhibits growth and
RT causes late flowering and early senescence in Arabidopsis.";
RL J. Biol. Chem. 277:5541-5547(2002).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND GENE
RP FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24156403; DOI=10.1042/bj20130196;
RA Marino G., Huesgen P.F., Eckhard U., Overall C.M., Schroeder W.P., Funk C.;
RT "Family-wide characterization of matrix metalloproteinases from Arabidopsis
RT thaliana reveals their distinct proteolytic activity and cleavage site
RT specificity.";
RL Biochem. J. 457:335-346(2014).
CC -!- FUNCTION: Matrix metalloproteinases (MMPs) or matrixins may play a role
CC in the degradation and remodeling of the extracellular matrix (ECM)
CC during development or in response to stresses (By similarity). Required
CC for plant growth, morphogenesis, and development with particular
CC relevance for flowering and senescence (PubMed:11726650). Active on
CC McaPLGLDpaAR-NH(2) (QF24) and myelin basic protein (MBP) and, to some
CC extent, on beta-casein (PubMed:24156403).
CC {ECO:0000250|UniProtKB:O23507, ECO:0000269|PubMed:11726650,
CC ECO:0000269|PubMed:24156403}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Repressed by acetohydroxamic acid (AHA).
CC {ECO:0000269|PubMed:24156403}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:24156403};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:24156403};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}; Extracellular side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC in flowers, leaves and stems. {ECO:0000269|PubMed:10574937,
CC ECO:0000269|PubMed:11726650}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during aging. Expressed in leaves and
CC roots of young seedlings and in leaves, roots, and inflorescences of
CC mature flowering plants. In leaves, present in the phloem, in
CC developing xylem elements, epidermal cells, and neighboring mesophyll
CC cell layers. In flowers, localized in pistils, ovules, and receptacles.
CC {ECO:0000269|PubMed:11726650}.
CC -!- INDUCTION: Induced in seedling rosette leaves by methyl jasmonate
CC (MeJA) and cadmium (Cd). Induced in seedling roots by salt stress
CC (NaCl). Inhibited in leaves and inflorescences of adult plants by
CC exposure to cadmium. {ECO:0000269|PubMed:11726650}.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme. {ECO:0000250|UniProtKB:P29136}.
CC -!- DISRUPTION PHENOTYPE: Growth inhibition, due to inhibited onset of
CC shoots, reduced growth of roots, leaves and shoots, late flowering,
CC fast degradation of chlorophyll in leaves and early senescence.
CC {ECO:0000269|PubMed:11726650}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. Matrix
CC metalloproteinases (MMPs) subfamily. {ECO:0000305}.
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DR EMBL; AC002062; AAB61099.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35027.1; -; Genomic_DNA.
DR EMBL; AK226646; BAE98757.1; -; mRNA.
DR PIR; E96724; E96724.
DR RefSeq; NP_177174.1; NM_105685.4.
DR AlphaFoldDB; O04529; -.
DR SMR; O04529; -.
DR STRING; 3702.AT1G70170.1; -.
DR MEROPS; M10.A01; -.
DR PaxDb; O04529; -.
DR PRIDE; O04529; -.
DR ProteomicsDB; 243265; -.
DR EnsemblPlants; AT1G70170.1; AT1G70170.1; AT1G70170.
DR GeneID; 843353; -.
DR Gramene; AT1G70170.1; AT1G70170.1; AT1G70170.
DR KEGG; ath:AT1G70170; -.
DR Araport; AT1G70170; -.
DR TAIR; locus:2020548; AT1G70170.
DR eggNOG; KOG1565; Eukaryota.
DR HOGENOM; CLU_015489_4_0_1; -.
DR InParanoid; O04529; -.
DR OMA; MHGGRRK; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; O04529; -.
DR PRO; PR:O04529; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04529; baseline and differential.
DR Genevisible; O04529; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0080186; P:developmental vegetative growth; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:1900056; P:negative regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..154
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P29136"
FT /id="PRO_0000433522"
FT CHAIN 155..349
FT /note="Metalloendoproteinase 2-MMP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433523"
FT PROPEP 350..378
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433524"
FT MOTIF 118..125
FT /note="Cysteine switch"
FT /evidence="ECO:0000255"
FT ACT_SITE 281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 349
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 356
FT /note="G -> D (in Ref. 3; BAE98757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42006 MW; 9B493CA01AC24672 CRC64;
MRFCVFGFLS LFLIVSPASA WFFPNSTAVP PSLRNTTRVF WDAFSNFTGC HHGQNVDGLY
RIKKYFQRFG YIPETFSGNF TDDFDDILKA AVELYQTNFN LNVTGELDAL TIQHIVIPRC
GNPDVVNGTS LMHGGRRKTF EVNFSRTHLH AVKRYTLFPG EPRWPRNRRD LTYAFDPKNP
LTEEVKSVFS RAFGRWSDVT ALNFTLSESF STSDITIGFY TGDHGDGEPF DGVLGTLAHA
FSPPSGKFHL DADENWVVSG DLDSFLSVTA AVDLESVAVH EIGHLLGLGH SSVEESIMYP
TITTGKRKVD LTNDDVEGIQ YLYGANPNFN GTTSPPSTTK HQRDTGGFSA AWRIDGSSRS
TIVSLLLSTV GLVLWFLP
