ID A0A7F5R4U9_AGRPL Unreviewed; 584 AA.
AC A0A7F5R4U9;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Matrix metalloproteinase-14 isoform X1 {ECO:0000313|RefSeq:XP_025830613.1};
GN Name=LOC108741148 {ECO:0000313|RefSeq:XP_025830613.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_025830613.1};
RN [1] {ECO:0000313|RefSeq:XP_025830613.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_025830613.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00010370}.
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DR RefSeq; XP_025830613.1; XM_025974828.1.
DR AlphaFoldDB; A0A7F5R4U9; -.
DR FunCoup; A0A7F5R4U9; 30.
DR GeneID; 108741148; -.
DR KEGG; apln:108741148; -.
DR InParanoid; A0A7F5R4U9; -.
DR OrthoDB; 406838at2759; -.
DR Proteomes; UP000192223; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
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; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR FunFam; 3.40.390.10:FF:000022; Matrix metalloproteinase 1, isoform C; 1.
DR FunFam; 2.110.10.10:FF:000007; stromelysin-3 isoform X2; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.110.10.10; Hemopexin-like domain; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
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:SF291; MATRIX METALLOPROTEINASE 1, ISOFORM C-RELATED; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50923; Hemopexin-like domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 ECO:0000313|RefSeq:XP_025830613.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR621190-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..584
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028899239"
FT DOMAIN 109..265
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REPEAT 298..343
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 344..389
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 390..439
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REGION 264..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..95
FT /note="Cysteine switch"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-5"
FT COMPBIAS 537..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT BINDING 89
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 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 197
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 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 220
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 224
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 230
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 238
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 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT MOD_RES 378
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-4"
SQ SEQUENCE 584 AA; 64668 MW; 376DBA8DAB2837D2 CRC64;
MSRFVISAVV LFIVRITECA SLGSETSALF YLSQYGYLDP GVRNTGNSSN LIDGRVINKA
IAEFQSFAGL DVTGELDEET VKTMSLPRCG VKDKVGTASD TRSKRYALQG SRWKVKNLTY
KISKYPKKLV KKDVDAEIAK AFAVWSEFTD LKFKPSKGQV HIEISFETGE HGDGDPFDGP
GGTLAHAYFP VFGGDAHFDN QEHWTISSYR GTNLFQVAAH EFGHSLGLSH SDVRSALMAP
FYRGYDPAFS LDIDDIEGIQ SLYGEKTDKT DNDDSDGGES VGKPTAMTPT EDKELCNDPR
IDTIFNSADG ETYAFKGDKY WKLTREAVAP GYPKLISEGW PGLPGDIDAA FTYKNGKTYF
FKGKQYWRYN GKRVDGDYPK DISEGFTGIP DDIDAAMVWS GNGKIYFFKG SKFWRFDPSQ
RPPVKGTYPK PISNWEGLPN NLDAAFQWTN GYTYFYKDNA YYRFNDRQFA VDSANPAFPR
STAYWWFGCK SSPRGTIGTR FTSNGWLLAD ESDFNGIPQI DSSTGDDIFD TDEHQKSNPT
GESSDGPSNE PRTSQGNDDS GVDHVTSSLI VITVAALAVA HLGS
//
