4MMP_ARATH
ID 4MMP_ARATH Reviewed; 342 AA.
AC Q8GWW6; O65340;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Metalloendoproteinase 4-MMP {ECO:0000303|PubMed:10574937};
DE Short=At4-MMP {ECO:0000303|PubMed:10574937};
DE EC=3.4.24.- {ECO:0000305};
DE AltName: Full=Matrix metalloproteinase 1 {ECO:0000303|Ref.1};
DE Short=AtMMP1 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=4MMP {ECO:0000303|PubMed:10574937}; Synonyms=MMP1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At2g45040 {ECO:0000312|Araport:AT2G45040};
GN ORFNames=T14P1.15 {ECO:0000305};
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:BAC43190.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RA Liu C.Y., Xu H., Graham J.S.;
RT "Cloning and characterization of an Arabidopsis cDNA homologous to the
RT matrix metalloproteinases.";
RL (er) Plant Gene Register PGR98-130(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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 [7]
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 myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-
CC NH(2) (QF24) and beta-casein (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 5-9. {ECO:0000269|PubMed:24156403};
CC Temperature dependence:
CC Optimum temperature is 45-55 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 flowers and stems, and, to a
CC lower extent, in leaves and roots. {ECO:0000269|PubMed:10574937}.
CC -!- DEVELOPMENTAL STAGE: Starts to accumulate in 7-10 days old plant
CC leaves. {ECO:0000269|Ref.1}.
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}.
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DR EMBL; AF062640; AAC31167.1; -; mRNA.
DR EMBL; CP002685; AEC10499.1; -; Genomic_DNA.
DR EMBL; AK118590; BAC43190.1; -; mRNA.
DR EMBL; BT008782; AAP68221.1; -; mRNA.
DR PIR; G84885; G84885.
DR PIR; T51957; T51957.
DR RefSeq; NP_182030.1; NM_130068.3.
DR AlphaFoldDB; Q8GWW6; -.
DR SMR; Q8GWW6; -.
DR IntAct; Q8GWW6; 1.
DR STRING; 3702.AT2G45040.1; -.
DR MEROPS; M10.A02; -.
DR PaxDb; Q8GWW6; -.
DR PRIDE; Q8GWW6; -.
DR ProteomicsDB; 245158; -.
DR EnsemblPlants; AT2G45040.1; AT2G45040.1; AT2G45040.
DR GeneID; 819111; -.
DR Gramene; AT2G45040.1; AT2G45040.1; AT2G45040.
DR KEGG; ath:AT2G45040; -.
DR Araport; AT2G45040; -.
DR TAIR; locus:2055605; AT2G45040.
DR eggNOG; KOG1565; Eukaryota.
DR HOGENOM; CLU_015489_4_0_1; -.
DR InParanoid; Q8GWW6; -.
DR OMA; FEPSFWA; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q8GWW6; -.
DR PRO; PR:Q8GWW6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GWW6; baseline and differential.
DR Genevisible; Q8GWW6; 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: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; 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; 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..34
FT /evidence="ECO:0000255"
FT PROPEP 35..124
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P29136"
FT /id="PRO_0000433528"
FT CHAIN 125..317
FT /note="Metalloendoproteinase 4-MMP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433529"
FT PROPEP 318..342
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433530"
FT MOTIF 104..111
FT /note="Cysteine switch"
FT /evidence="ECO:0000255"
FT ACT_SITE 253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 106
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 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 317
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 161
FT /note="Missing (in Ref. 1; AAC31167)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="K -> E (in Ref. 1; AAC31167)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="T -> A (in Ref. 1; AAC31167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38506 MW; 1261DDD75B8E5ED6 CRC64;
MHHHHHPCNR KPFTTIFSFF LLYLNLHNQQ IIEARNPSQF TTNPSPDVSI PEIKRHLQQY
GYLPQNKESD DVSFEQALVR YQKNLGLPIT GKPDSDTLSQ ILLPRCGFPD DVEPKTAPFH
TGKKYVYFPG RPRWTRDVPL KLTYAFSQEN LTPYLAPTDI RRVFRRAFGK WASVIPVSFI
ETEDYVIADI KIGFFNGDHG DGEPFDGVLG VLAHTFSPEN GRLHLDKAET WAVDFDEEKS
SVAVDLESVA VHEIGHVLGL GHSSVKDAAM YPTLKPRSKK VNLNMDDVVG VQSLYGTNPN
FTLNSLLASE TSTNLADGSR IRSQGMIYST LSTVIALCFL NW
