MMP18_XENLA
ID MMP18_XENLA Reviewed; 467 AA.
AC O13065;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Matrix metalloproteinase-18;
DE Short=MMP-18;
DE EC=3.4.24.-;
DE AltName: Full=Collagenase-4;
DE Short=xCol4;
DE Flags: Precursor;
GN Name=mmp18; Synonyms=col4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Intestine;
RX PubMed=8898355; DOI=10.1091/mbc.7.10.1471;
RA Stolow M.A., Bauzon D.D., Li J., Sedgwick T., Liang V.C.-T., Sang Q.A.,
RA Shi Y.-B.;
RT "Identification and characterization of a novel collagenase in Xenopus
RT laevis: possible roles during frog development.";
RL Mol. Biol. Cell 7:1471-1483(1996).
CC -!- FUNCTION: Cleaves collagen type I. May play a role in larval tissue
CC degeneration and adult organogenesis during amphibian metamorphosis.
CC May be involved in tail resorption.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Up-regulated in the tail by thyroid hormone.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed only transiently in whole animal, at time
CC when tadpole feeding begins.
CC -!- DEVELOPMENTAL STAGE: Expressed at high level as the tadpole tail
CC resorbs and during hindlimb morphogenesis and intestinal remodeling.
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.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; L76275; AAB53148.1; -; Genomic_DNA.
DR AlphaFoldDB; O13065; -.
DR SMR; O13065; -.
DR MEROPS; M10.018; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; 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:UniProtKB-KW.
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; PF00045; Hemopexin; 3.
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; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen degradation; Disulfide bond; Extracellular matrix;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..99
FT /evidence="ECO:0000250"
FT /id="PRO_0000028824"
FT CHAIN 100..467
FT /note="Matrix metalloproteinase-18"
FT /id="PRO_0000028825"
FT REPEAT 277..326
FT /note="Hemopexin 1"
FT REPEAT 327..373
FT /note="Hemopexin 2"
FT REPEAT 375..423
FT /note="Hemopexin 3"
FT REPEAT 424..467
FT /note="Hemopexin 4"
FT MOTIF 90..97
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 280..467
FT /evidence="ECO:0000255"
SQ SEQUENCE 467 AA; 52813 MW; 4623F6CEF3454051 CRC64;
MNSLLLKLLL CVAITAAFPA DKQDEPPATK EEMAENYLKR FYSLGTDGGP VGRKKHIQPF
TEKLEQMQKF FGLKVTGTLD PKTVEVMEKP RCGVYDVGQY STVAKSSAWQ KKDLTYRILN
FTPDLPQADV ETAIQRAFKV WSDVTPLTFT RIYNEVSDIE ISFTAGDHKD NSPFDGSGGI
LAHAFQPGNG IGGDAHFDED ETWTKTSEIY NLFLVAAHEF GHSLGLSHST DQGALMYPTY
SNTDPKTFQL PQDDINAIQY LYGKSSNPVQ PTGPSTPSRC DPNVVFNAVT TMRGELIFFV
KRFLWRKHPQ ASEAELMFVQ AFWPSLPTNI DAAYENPITE QILVFKGSKY TALDGFDVVQ
GYPRNIYSLG FPKTVKRIDA AVHIEQLGKT YFFAAKKYWS YDEDKKQMDK GFPKQISNDF
PGIPDKIDAA FYYRGRLYFF IGRSQFEYNI NSKRIVQVLR SNSWLGC
