3MMP_ARATH
ID 3MMP_ARATH Reviewed; 384 AA.
AC Q5XF51; O48680;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Metalloendoproteinase 3-MMP {ECO:0000303|PubMed:10574937};
DE Short=At3-MMP {ECO:0000303|PubMed:10574937};
DE EC=3.4.24.- {ECO:0000305};
DE Flags: Precursor;
GN Name=3MMP {ECO:0000303|PubMed:10574937};
GN OrderedLocusNames=At1g24140 {ECO:0000312|Araport:AT1G24140};
GN ORFNames=F3I6.6 {ECO:0000312|EMBL:AAC00572.1};
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|EMBL:AAU90055.1};
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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (OCT-2004) 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, 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). Active
CC on McaPLGLDpaAR-NH(2) (QF24) and beta-casein and, to some extent, on
CC myelin basic protein (MBP) (PubMed:24156403).
CC {ECO:0000250|UniProtKB:O23507, 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 35 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 leaves and roots, and, to a
CC lower extent, in flowers and stems. {ECO:0000269|PubMed:10574937}.
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 -!- SIMILARITY: Belongs to the peptidase M10A family. Matrix
CC metalloproteinases (MMPs) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00572.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002396; AAC00572.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE30482.1; -; Genomic_DNA.
DR EMBL; BT015765; AAU90055.1; -; mRNA.
DR PIR; T00643; T00643.
DR RefSeq; NP_173824.2; NM_102260.4.
DR AlphaFoldDB; Q5XF51; -.
DR SMR; Q5XF51; -.
DR STRING; 3702.AT1G24140.1; -.
DR MEROPS; M10.A05; -.
DR PaxDb; Q5XF51; -.
DR PRIDE; Q5XF51; -.
DR ProteomicsDB; 244491; -.
DR EnsemblPlants; AT1G24140.1; AT1G24140.1; AT1G24140.
DR GeneID; 839026; -.
DR Gramene; AT1G24140.1; AT1G24140.1; AT1G24140.
DR KEGG; ath:AT1G24140; -.
DR Araport; AT1G24140; -.
DR TAIR; locus:2032467; AT1G24140.
DR eggNOG; KOG1565; Eukaryota.
DR HOGENOM; CLU_015489_4_0_1; -.
DR InParanoid; Q5XF51; -.
DR OMA; TQQRDTG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q5XF51; -.
DR PRO; PR:Q5XF51; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XF51; baseline and differential.
DR Genevisible; Q5XF51; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..158
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P29136"
FT /id="PRO_0000433525"
FT CHAIN 159..358
FT /note="Metalloendoproteinase 3-MMP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433526"
FT PROPEP 359..384
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433527"
FT REGION 330..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 121..128
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 330..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 123
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 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 358
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 384 AA; 43017 MW; E6EF6661C98A790C CRC64;
MVRICVFMVF LLFFAPSPVS AGFYTNSSAI PPQLLRNATG NPWNSFLNFT GCHAGKKYDG
LYMLKQYFQH FGYITETNLS GNFTDDFDDI LKNAVEMYQR NFQLNVTGVL DELTLKHVVI
PRCGNPDVVN GTSTMHSGRK TFEVSFAGRG QRFHAVKHYS FFPGEPRWPR NRRDLTYAFD
PRNALTEEVK SVFSRAFTRW EEVTPLTFTR VERFSTSDIS IGFYSGEHGD GEPFDGPMRT
LAHAFSPPTG HFHLDGEENW IVSGEGGDGF ISVSEAVDLE SVAVHEIGHL LGLGHSSVEG
SIMYPTIRTG RRKVDLTTDD VEGVQYLYGA NPNFNGSRSP PPSTQQRDTG DSGAPGRSDG
SRSVLTNLLQ YYFWIIFGLF LYLV
