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Database: UniProt
Entry: A0A1S3CA73_CUCME
LinkDB: A0A1S3CA73_CUCME
Original site: A0A1S3CA73_CUCME 
ID   A0A1S3CA73_CUCME        Unreviewed;       343 AA.
AC   A0A1S3CA73;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Metalloendoproteinase 2-MMP-like {ECO:0000313|RefSeq:XP_008458908.1};
GN   Name=LOC103498172 {ECO:0000313|RefSeq:XP_008458908.1};
GN   Synonyms=103498172 {ECO:0000313|EnsemblPlants:MELO3C021497.2.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008458908.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|EnsemblPlants:MELO3C021497.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008458908.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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. Matrix
CC       metalloproteinases (MMPs) subfamily. {ECO:0000256|ARBA:ARBA00009614}.
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DR   RefSeq; XP_008458908.1; XM_008460686.1.
DR   EnsemblPlants; MELO3C021497.2.1; MELO3C021497.2.1; MELO3C021497.2.
DR   GeneID; 103498172; -.
DR   Gramene; MELO3C021497.2.1; MELO3C021497.2.1; MELO3C021497.2.
DR   KEGG; cmo:103498172; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; A0A1S3CA73; -.
DR   OrthoDB; 391167at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF213; 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:ARBA00023180};
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:UP000089565};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR621190-2}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..343
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041054506"
FT   DOMAIN          152..304
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT   BINDING         121
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         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
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         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
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"
FT   BINDING         264
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         270
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         278
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   343 AA;  39328 MW;  7DF995B36585998E CRC64;
     MDFKSFYLQL FLLLTSLSLF HPISSRDLNH IHGPSQFLFP KYLLGSRKGH NIEGTHAIKT
     YLQHYGYLSK NYNIIDTNGV YNNAYDEQLE CSVKKYQKFF KLNESGILDR ETLSQMSQPR
     CSVPDIFESE DNETSITTSN LHIRSRYAFF PGRPKWSDSR NLTYSLIKNF PEKFEAAIVD
     AFMLWFLRSR FCFTYVSEGQ KSDITISFEV GDHGDGHPFK GGVLAHAFSP EDGRLHFNGD
     KSFSSDLEEG KYHIRTVAAH ELGHSLGLAH TNIEAAIMYP TLPSNFSKIL SQDDVDGLWN
     FYGQSEDSTK QDVISTIENN MKKYSDNMSV RIIRDKQELA KTQ
//
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