1MMP_ARATH
ID 1MMP_ARATH Reviewed; 364 AA.
AC O23507; Q84W77; Q8LET7;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Metalloendoproteinase 1-MMP {ECO:0000303|PubMed:10574937};
DE Short=At1-MMP {ECO:0000303|PubMed:10574937};
DE EC=3.4.24.- {ECO:0000305};
DE Flags: Precursor;
GN Name=1MMP {ECO:0000303|PubMed:10574937};
GN OrderedLocusNames=At4g16640 {ECO:0000312|Araport:AT4G16640};
GN ORFNames=dl4345c {ECO:0000312|EMBL:CAB10439.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 (PubMed:10574937). Can
CC cleave myelin basic protein as well as fluorigenic peptide substrates,
CC McaPLANvaDpaAR-NH(2) and McaPChaGNvaHADpa-NH(2) 4-fold more efficiently
CC than McaPLGLDpaAR-NH(2) (QF24) (PubMed:10574937). Active on myelin
CC basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24)
CC and beta-casein (PubMed:24156403). {ECO:0000269|PubMed:10574937,
CC ECO:0000269|PubMed:24156403, ECO:0000303|PubMed:10574937}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P03956};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P03956};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P03956};
CC -!- ACTIVITY REGULATION: Inhibited by human TIMP-1 and TIMP-2 and by the
CC peptide hydroxamate inhibitor (BB-94) (PubMed:10574937). Repressed by
CC acetohydroxamic acid (AHA) (PubMed:24156403).
CC {ECO:0000269|PubMed:10574937, 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 45-55 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, roots and stems, and,
CC to a lower extent, in leaves. {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; Z97341; CAB10439.1; -; Genomic_DNA.
DR EMBL; AL161544; CAB78706.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83779.1; -; Genomic_DNA.
DR EMBL; BT004141; AAO42162.1; -; mRNA.
DR EMBL; AY085244; AAM62476.1; -; mRNA.
DR PIR; E71433; E71433.
DR RefSeq; NP_193397.1; NM_117765.4.
DR AlphaFoldDB; O23507; -.
DR SMR; O23507; -.
DR STRING; 3702.AT4G16640.1; -.
DR MEROPS; M10.A04; -.
DR PaxDb; O23507; -.
DR PRIDE; O23507; -.
DR ProteomicsDB; 243264; -.
DR EnsemblPlants; AT4G16640.1; AT4G16640.1; AT4G16640.
DR GeneID; 827365; -.
DR Gramene; AT4G16640.1; AT4G16640.1; AT4G16640.
DR KEGG; ath:AT4G16640; -.
DR Araport; AT4G16640; -.
DR TAIR; locus:2130928; AT4G16640.
DR eggNOG; KOG1565; Eukaryota.
DR HOGENOM; CLU_015489_4_0_1; -.
DR InParanoid; O23507; -.
DR OMA; NATRHDF; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; O23507; -.
DR PRO; PR:O23507; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23507; baseline and differential.
DR Genevisible; O23507; 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..28
FT /evidence="ECO:0000255"
FT PROPEP 29..149
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P29136"
FT /id="PRO_0000433519"
FT CHAIN 150..339
FT /note="Metalloendoproteinase 1-MMP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433520"
FT PROPEP 340..364
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433521"
FT MOTIF 128..135
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03956,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03956,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03956,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 339
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 30
FT /note="N -> I (in Ref. 4; AAO42162)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="N -> K (in Ref. 5; AAM62476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40528 MW; 844C5D612EAED662 CRC64;
MSRNLIYRRN RALCFVLILF CFPYRFGARN TPEAEQSTAK ATQIIHVSNS TWHDFSRLVD
VQIGSHVSGV SELKRYLHRF GYVNDGSEIF SDVFDGPLES AISLYQENLG LPITGRLDTS
TVTLMSLPRC GVSDTHMTIN NDFLHTTAHY TYFNGKPKWN RDTLTYAISK THKLDYLTSE
DVKTVFRRAF SQWSSVIPVS FEEVDDFTTA DLKIGFYAGD HGDGLPFDGV LGTLAHAFAP
ENGRLHLDAA ETWIVDDDLK GSSEVAVDLE SVATHEIGHL LGLGHSSQES AVMYPSLRPR
TKKVDLTVDD VAGVLKLYGP NPKLRLDSLT QSEDSIKNGT VSHRFLSGNF IGYVLLVVGL
ILFL
