MMPC_CAEEL
ID MMPC_CAEEL Reviewed; 579 AA.
AC G5EBU3;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Matrix metalloproteinase-C {ECO:0000305|PubMed:9573338};
DE Short=MMP-C {ECO:0000305|PubMed:9573338};
DE Short=MMP-C31 {ECO:0000303|PubMed:9573338};
DE EC=3.4.24.- {ECO:0000269|PubMed:9573338};
DE AltName: Full=Zinc metalloprotease 3 {ECO:0000312|WormBase:C31B8.8};
DE Flags: Precursor;
GN Name=zmp-3 {ECO:0000312|WormBase:C31B8.8};
GN ORFNames=C31B8.8 {ECO:0000312|WormBase:C31B8.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAA28351.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:BAA28351.1};
RX PubMed=9573338; DOI=10.1016/s0378-1119(98)00076-6;
RA Wada K., Sato H., Kinoh H., Kajita M., Yamamoto H., Seiki M.;
RT "Cloning of three Caenorhabditis elegans genes potentially encoding novel
RT matrix metalloproteinases.";
RL Gene 211:57-62(1998).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Metalloproteinase. {ECO:0000269|PubMed:9573338}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P03956};
CC -!- ACTIVITY REGULATION: Inhibited by human TIMP1 and TIMP2 and the broad
CC MMP inhibitors BB94 (Batimastat) and CT543.
CC {ECO:0000269|PubMed:9573338}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme. {ECO:0000250|UniProtKB:P03956}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000255}.
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DR EMBL; AB007815; BAA28351.1; -; mRNA.
DR EMBL; BX284605; CCD66298.1; -; Genomic_DNA.
DR PIR; T37248; T37248.
DR RefSeq; NP_503790.1; NM_071389.4.
DR AlphaFoldDB; G5EBU3; -.
DR SMR; G5EBU3; -.
DR STRING; 6239.C31B8.8; -.
DR MEROPS; M10.A07; -.
DR EPD; G5EBU3; -.
DR PaxDb; G5EBU3; -.
DR PeptideAtlas; G5EBU3; -.
DR EnsemblMetazoa; C31B8.8.1; C31B8.8.1; WBGene00016283.
DR GeneID; 178748; -.
DR KEGG; cel:CELE_C31B8.8; -.
DR CTD; 178748; -.
DR WormBase; C31B8.8; CE26674; WBGene00016283; zmp-3.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00970000196003; -.
DR HOGENOM; CLU_015489_0_0_1; -.
DR InParanoid; G5EBU3; -.
DR OMA; RTDFSHY; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; G5EBU3; -.
DR Reactome; R-CEL-1442490; Collagen degradation.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CEL-210991; Basigin interactions.
DR Reactome; R-CEL-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5EBU3; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00016283; Expressed in larva and 2 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
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; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
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 Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 3.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 2.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..129
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P22757"
FT /id="PRO_0000439233"
FT CHAIN 130..579
FT /note="Matrix metalloproteinase-C"
FT /evidence="ECO:0000305"
FT /id="PRO_5007915027"
FT REPEAT 395..437
FT /note="Hemopexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01011"
FT REPEAT 438..490
FT /note="Hemopexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01011"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..127
FT /note="Cysteine switch"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /evidence="ECO:0000250|UniProtKB:P09238"
FT BINDING 122
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:0000250|UniProtKB:P03956"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 579 AA; 62540 MW; 14C82FEF02D66693 CRC64;
MRLIYVIAIL LVSTCQAGFF SSLVSRFTGG GNSSPSSSSS SSSFSNSRKP SLSDEKARSY
LQTFGYVPPS NSLQSRNGMA GDIQSAEQVF KSAIRKFQEF AGIAKTGFLD AATKAKMALS
RCGVTDAPLA LTSGSSQFKW SKTRLTYSIE SWSSDLSKDD VRRAISEAYG LWSKVTPLEF
SEVPAGSTSD IKIRFGVRNH NDPWPFDGEG GVLAHATMPE SGMFHFDDDE NWTYKDARKI
HNNEATDLLA VAIHEGGHTL GLEHSRDENA IMAPFYQKTT DSSGNYVYPN LKSDDISAIQ
AIYGAGSGRS SSGSDFGGSS GGGSRTTARP TTTTRSWFGR FFGDDDDDVR SRTTTRRTTL
WPTTQSPFSG DDWGSGSGSS GRGGSSSGSS GGGCPSHIDA YTPSSSFSYA FSGSQVYTIS
GTKVTKVQSI HDLFPSAPTP VNAALWNPIS GSMLLFSSNR VYSYYFSNIR QIFQMDSGFP
KTLPSDLGFS VSGALRWING HQILMSSGDE FAVYDEFWNQ VTLKNRISSY FPNLPRGVKG
VESPAGSVIT AFTSNQVFEY NSRTKSIGRQ SGFSSYIAC
