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Database: UniProt
Entry: A0A3B4ECU3_PYGNA
LinkDB: A0A3B4ECU3_PYGNA
Original site: A0A3B4ECU3_PYGNA 
ID   A0A3B4ECU3_PYGNA        Unreviewed;       623 AA.
AC   A0A3B4ECU3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Matrix metallopeptidase 15 {ECO:0000313|Ensembl:ENSPNAP00000033518.1};
GN   Name=MMP15 {ECO:0000313|Ensembl:ENSPNAP00000033518.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000033518.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000033518.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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.
CC       {ECO:0000256|ARBA:ARBA00010370}.
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DR   AlphaFoldDB; A0A3B4ECU3; -.
DR   Ensembl; ENSPNAT00000024434.1; ENSPNAP00000033518.1; ENSPNAG00000022228.1.
DR   GeneTree; ENSGT00940000156939; -.
DR   OMA; YHSHEAV; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0016020; C: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00094; HX; 1.
DR   CDD; cd04278; ZnMc_MMP; 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; IPR021805; Pept_M10A_metallopeptidase_C.
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   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF25; MATRIX METALLOPROTEINASE-15; 1.
DR   Pfam; PF11857; DUF3377; 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; PS00546; CYSTEINE_SWITCH; 1.
DR   PROSITE; PS00024; HEMOPEXIN; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 4.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR621190-2};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          91..261
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   REPEAT          310..358
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REPEAT          359..404
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REPEAT          406..454
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REPEAT          455..503
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REGION          256..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           67..83
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-5"
FT   COMPBIAS        276..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT   BINDING         69
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         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         170
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         188
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
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="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         219
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         225
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         233
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         318
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         363
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         365
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         412
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   MOD_RES         393
FT                   /note="Phosphotyrosine; by PKDCC"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-4"
SQ   SEQUENCE   623 AA;  72214 MW;  DF6C40D59253E7AF CRC64;
     PQGLCGTHRN TGSWLRMYGY LPQASRQMST MRSAQILSNA ISDMQRFYGL EITGVMDSAT
     MEAMKRPRCG VPDKFGGQIK TNVRRKRYAL TGHKWDKTHL TFSIQNYTPK IGEYNSYEAI
     RRAFTVWEKV TPLTFEEIPY MEVKYGRRKE PDIMIFFASG FHGDSSPFDG EGGFLAHAYF
     PGPGMGGDTH FDSDEPWTIG NQNLQGNDLF LVAVHELGHA LGLEHSNNPM AIMAPFYQWM
     DTDNFQLPED DLRGIQQIYG PPVSTPTQAL PTVKPRHPNH PKDPPRDPPR APPRRPDRPR
     TTDRPDQYGP NICEGNFDTV TMLRGEMFVF KGRWFWRVRR NRVLDNYPMP IGHFWRGLPG
     DIDAAYERHD GRFVFFKGGQ YWLFREANLE PGYPQELMDY GRDIPYDKIE TAIWWEPSGY
     TYFFKEDRYW RFNEQLRAVD QGYPKPISVW DSSVPVSPKG AFLSDDGAYT YFYKGSKYWK
     FDNHRMKSEP GYPKSILRDF MGCSVDLDPD RDTDVDPGRK WPDRPPFNPD AGRDKDKEKD
     KDKERDRTND VDYKEATEEE TNEVDVVLKI DETERTMNII MVAVPLVLVL CILGLIYAII
     NTLQRKGAPK YLVYCKRSLQ EWV
//
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