MEP1_SOYBN
ID MEP1_SOYBN Reviewed; 305 AA.
AC P29136;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Metalloendoproteinase 1;
DE EC=3.4.24.-;
DE AltName: Full=SMEP1;
DE Flags: Precursor;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Williams 82; TISSUE=Leaf;
RX PubMed=9119080; DOI=10.1016/s0014-5793(97)00141-5;
RA Pak J.H., Liu C.Y., Huangpu J., Graham J.S.;
RT "Construction and characterization of the soybean leaf metalloproteinase
RT cDNA.";
RL FEBS Lett. 404:283-288(1997).
RN [2]
RP PROTEIN SEQUENCE OF 134-305.
RC STRAIN=cv. Williams 82; TISSUE=Leaf;
RX PubMed=16668986; DOI=10.1104/pp.99.3.1179;
RA McGeehan G., Burkhart W., Anderegg R., Becherer D.J., Gillikin J.W.,
RA Graham J.S.;
RT "Sequencing and characterization of the soybean leaf metalloproteinase.";
RL Plant Physiol. 99:1179-1183(1992).
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.
CC {ECO:0000250|UniProtKB:O23507}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. Matrix
CC metalloproteinases (MMPs) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U63725; AAB26959.1; -; mRNA.
DR PIR; T08836; T08836.
DR RefSeq; NP_001235535.1; NM_001248606.1.
DR AlphaFoldDB; P29136; -.
DR SMR; P29136; -.
DR STRING; 3847.GLYMA02G37990.1; -.
DR MEROPS; M10.012; -.
DR PRIDE; P29136; -.
DR GeneID; 547880; -.
DR KEGG; gmx:547880; -.
DR eggNOG; KOG1565; Eukaryota.
DR OrthoDB; 1075463at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProt.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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; 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 Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..133
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:16668986"
FT /id="PRO_0000028867"
FT CHAIN 134..305
FT /note="Metalloendoproteinase 1"
FT /id="PRO_0000028868"
FT MOTIF 111..118
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 113
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 258
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 BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 305 AA; 34044 MW; 8146944A983267F4 CRC64;
MTLRNHQELL VALATLYFLA TSLPSVSAHG PYAWDGEATY KFTTYHPGQN YKGLSNVKNY
FHHLGYIPNA PHFDDNFDDT LVSAIKTYQK NYNLNVTGKF DINTLKQIMT PRCGVPDIII
NTNKTTSFGM ISDYTFFKDM PRWQAGTTQL TYAFSPEPRL DDTFKSAIAR AFSKWTPVVN
IAFQETTSYE TANIKILFAS KNHGDPYPFD GPGGILGHAF APTDGRCHFD ADEYWVASGD
VTKSPVTSAF DLESVAVHEI GHLLGLGHSS DLRAIMYPSI PPRTRKVNLA QDDIDGIRKL
YGINP
