ID A0AAE0EHL6_9ROSI Unreviewed; 600 AA.
AC A0AAE0EHL6;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=Dsin_000280 {ECO:0000313|EMBL:KAK3228399.1};
OS Dipteronia sinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Sapindaceae; Hippocastanoideae; Acereae;
OC Dipteronia.
OX NCBI_TaxID=43782 {ECO:0000313|EMBL:KAK3228399.1, ECO:0000313|Proteomes:UP001281410};
RN [1] {ECO:0000313|EMBL:KAK3228399.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBL {ECO:0000313|EMBL:KAK3228399.1};
RX PubMed=37797086;
RA Feng Y., Comes H.P., Chen J., Zhu S., Lu R., Zhang X., Li P., Qiu J.,
RA Olsen K.M., Qiu Y.;
RT "Genome sequences and population genomics provide insights into the
RT demographic history, inbreeding, and mutation load of two 'living fossil'
RT tree species of Dipteronia.";
RL Plant J. 0:0-0(2023).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004471};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004471}; Extracellular
CC side {ECO:0000256|ARBA:ARBA00004471}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. Matrix
CC metalloproteinases (MMPs) subfamily. {ECO:0000256|ARBA:ARBA00009614}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK3228399.1}.
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DR EMBL; JANJYJ010000001; KAK3228399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE0EHL6; -.
DR Proteomes; UP001281410; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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:SF311; PEPTIDASE METALLOPEPTIDASE DOMAIN-CONTAINING PROTEIN; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
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:UP001281410};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR621190-2}.
FT DOMAIN 128..294
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT MOTIF 95..120
FT /note="Cysteine switch"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-5"
FT ACT_SITE 242
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT BINDING 97
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 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 222
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="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 245
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 251
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 260
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 600 AA; 67517 MW; A1342C00F5DC1163 CRC64;
MTRLPKTIQS KTHHIPNPFQ FIHTLENCQK GQQVKGLQHL KKYLQEFGYL NYNVDHHSEV
FDNLLESAIK TYQCSYGLNV TGILDSDTVN QMMKPRCGVP DYVNNGPQHG HDDKSPFHSV
AHYQFIPGTP RWSKSTLTYT FNSTAEVPDS LNIKSVFQST FQKWAGVTRF SFEEVPENSP
ADIMIGFHRL DHGDGNPFDG PKGVLAHAFP PSYGKCHFDS DEMWSRNPGP NELDLESVAM
HELGHILGLG HEPTKPEAIM FPTFGYGRIK RDLNIDDIQG CRDRLIVNSA DYALATYFEK
LVWLSRLDPI KQCFVRFSSL EAVVSSYDSR FFGNIMSSES TTLSPIFTWT PNGSGGEVDE
GAKSDTRDVE QQVSIADPLD VHPNKLGLME IGVVQPVTPC RHTHEKGRFT LCLRLGMKHF
VSELITKDER WKDIFFFAKG PLINGLFGKE KYIYILAFGV ELKKATIVAT NEKAIVVADD
LTFDFPPESS PLRTMKKRKV IEADPNRKVV EVASKGPDST LVLFPVGVST FNDPSIFLKK
SDNFLFPADE GYLKGKKTDN AVDAGSINVV AFEEKFHSQS TEMREALEDQ RFSQKGLRQA
//
