ID A0A3B5ZWG1_WHEAT Unreviewed; 357 AA.
AC A0A3B5ZWG1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=CFC21_011952 {ECO:0000313|EMBL:KAF6995455.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS1D02G223000.1};
RN [1] {ECO:0000313|EMBL:KAF6995455.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF6995455.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS1D02G223000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS1D02G223000.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS1D02G223000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF6995455.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF6995455.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC Note=Can bind about 5 Ca(2+) ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR621190-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-
CC 2};
CC -!- SIMILARITY: Belongs to the peptidase M10A family. Matrix
CC metalloproteinases (MMPs) subfamily. {ECO:0000256|ARBA:ARBA00009614}.
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DR EMBL; CM022213; KAF6995455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B5ZWG1; -.
DR SMR; A0A3B5ZWG1; -.
DR STRING; 4565.A0A3B5ZWG1; -.
DR EnsemblPlants; TraesCS1D02G223000.1; TraesCS1D02G223000.1; TraesCS1D02G223000.
DR Gramene; TraesCS1D02G223000.1; TraesCS1D02G223000.1; TraesCS1D02G223000.
DR Gramene; TraesCS1D03G0553200.1; TraesCS1D03G0553200.1.CDS; TraesCS1D03G0553200.
DR OMA; ATKHFTY; -.
DR Proteomes; UP000019116; Chromosome 1D.
DR Proteomes; UP000815260; Chromosome 1D.
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; Collagenase (Catalytic Domain); 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 PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF249; METALLOENDOPROTEINASE 1-MMP; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR621190-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR621190-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR621190-2}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..357
FT /note="Peptidase metallopeptidase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039988569"
FT DOMAIN 154..325
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT MOTIF 126..146
FT /note="Cysteine switch"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-5"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT BINDING 128
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:0000256|PIRSR:PIRSR621190-2"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
SQ SEQUENCE 357 AA; 38310 MW; 63AA01ED35F606E1 CRC64;
MVPCRPARAA ACLPLVLILC LLSCAAARPA PAPAPVHGRH HGQGWHSFKR LLDAQRGTRV
TGLGDLKRYL AMFGYMPKHA GPEHGGDPTD AFDEHLEAAV KRYQSRLSLP VTGRLDVVTL
DQMMSPRCGV QDDHGASVSP EHGGAVSRFT FFKGKPRWTR RSDPDPVVLT YAVSPTATVG
YLPDDDVRAV FRRAFERWAR VIPVAFVETD DYDEADIKVG FYGGSHGDGV PFDGPLGVLG
HAFSPKNGRL HLDAAERWAV DFAGETKASA AIDLESVATH EIGHVLGLGH STSPQAVMYP
SIKPLEKKAD LTVDDVEGVQ LLYGSNPDFK LSSLYDATDT SGSPAGSSWA ASSASVC
//
