5MMP_ARATH
ID 5MMP_ARATH Reviewed; 360 AA.
AC Q9ZUJ5;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Metalloendoproteinase 5-MMP {ECO:0000303|PubMed:10574937};
DE Short=At5-MMP {ECO:0000303|PubMed:10574937};
DE EC=3.4.24.- {ECO:0000305};
DE Flags: Precursor;
GN Name=5MMP {ECO:0000303|PubMed:10574937};
GN OrderedLocusNames=At1g59970 {ECO:0000312|Araport:AT1G59970};
GN ORFNames=T2K10.2 {ECO:0000312|EMBL:AAD14473.1};
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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). Active
CC on Mca-KESAbuNLFVLKDpaR-NH(2) (QF75) and, to some extent, on
CC McaPLGLDpaAR-NH(2) (QF24), myelin basic protein (MBP) and beta-casein
CC (PubMed:24156403). {ECO:0000250|UniProtKB:O23507,
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 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, roots and stems, and,
CC to a lower extent, in flowers. {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}.
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DR EMBL; AC005966; AAD14473.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33645.1; -; Genomic_DNA.
DR EMBL; AK176709; BAD44472.1; -; mRNA.
DR EMBL; BT025260; ABF19013.1; -; mRNA.
DR RefSeq; NP_176205.1; NM_104689.4.
DR AlphaFoldDB; Q9ZUJ5; -.
DR SMR; Q9ZUJ5; -.
DR STRING; 3702.AT1G59970.1; -.
DR MEROPS; M10.038; -.
DR PaxDb; Q9ZUJ5; -.
DR PRIDE; Q9ZUJ5; -.
DR ProteomicsDB; 243308; -.
DR EnsemblPlants; AT1G59970.1; AT1G59970.1; AT1G59970.
DR GeneID; 842291; -.
DR Gramene; AT1G59970.1; AT1G59970.1; AT1G59970.
DR KEGG; ath:AT1G59970; -.
DR Araport; AT1G59970; -.
DR TAIR; locus:2025891; AT1G59970.
DR eggNOG; KOG1565; Eukaryota.
DR HOGENOM; CLU_015489_4_0_1; -.
DR InParanoid; Q9ZUJ5; -.
DR OMA; CHIGENI; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q9ZUJ5; -.
DR PRO; PR:Q9ZUJ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZUJ5; baseline and differential.
DR Genevisible; Q9ZUJ5; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..142
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P29136"
FT /id="PRO_0000433531"
FT CHAIN 143..337
FT /note="Metalloendoproteinase 5-MMP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433532"
FT PROPEP 338..360
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433533"
FT REGION 312..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..124
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 119
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 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
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 LIPID 337
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 36
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 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 360 AA; 39760 MW; 5F2B89474358505B CRC64;
MRTLLLTILI FFFTVNPISA KFYTNVSSIP PLQFLNATQN AWETFSKLAG CHIGENINGL
SKLKQYFRRF GYITTTGNCT DDFDDVLQSA INTYQKNFNL KVTGKLDSST LRQIVKPRCG
NPDLIDGVSE MNGGKILRTT EKYSFFPGKP RWPKRKRDLT YAFAPQNNLT DEVKRVFSRA
FTRWAEVTPL NFTRSESILR ADIVIGFFSG EHGDGEPFDG AMGTLAHASS PPTGMLHLDG
DEDWLISNGE ISRRILPVTT VVDLESVAVH EIGHLLGLGH SSVEDAIMFP AISGGDRKVE
LAKDDIEGIQ HLYGGNPNGD GGGSKPSRES QSTGGDSVRR WRGWMISLSS IATCIFLISV
