MMP11_XENLA
ID MMP11_XENLA Reviewed; 477 AA.
AC Q11005;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Stromelysin-3;
DE Short=ST3;
DE EC=3.4.24.-;
DE AltName: Full=Matrix metalloproteinase-11;
DE Short=MMP-11;
DE Flags: Precursor;
GN Name=mmp11;
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 [MRNA], AND ZINC-BINDING SITES CYS-65; HIS-203; HIS-207
RP AND HIS-213.
RC TISSUE=Intestine;
RX PubMed=7851646; DOI=10.1006/dbio.1995.1021;
RA Patterton D., Hayes W.P., Shi Y.B.;
RT "Transcriptional activation of the matrix metalloproteinase gene
RT stromelysin-3 coincides with thyroid hormone-induced cell death during frog
RT metamorphosis.";
RL Dev. Biol. 167:252-262(1995).
CC -!- FUNCTION: May be involved in the modification of the extracellular
CC matrix during metamorphic apoptosis.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in fibroblast cells that are activated by
CC thyroid hormone. High levels in resorbing tail.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; Z27093; CAA81616.1; -; mRNA.
DR PIR; I51645; I51645.
DR RefSeq; NP_001079811.1; NM_001086342.1.
DR AlphaFoldDB; Q11005; -.
DR SMR; Q11005; -.
DR MEROPS; M10.007; -.
DR PRIDE; Q11005; -.
DR DNASU; 379501; -.
DR GeneID; 379501; -.
DR KEGG; xla:379501; -.
DR CTD; 379501; -.
DR Xenbase; XB-GENE-865255; mmp11.L.
DR OrthoDB; 1075463at2759; -.
DR BRENDA; 3.4.24.B3; 6725.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379501; Expressed in internal ear and 3 other tissues.
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; 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; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR028705; Stromelysin-3.
DR PANTHER; PTHR10201:SF20; PTHR10201:SF20; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Collagen degradation;
KW Disulfide bond; Extracellular matrix; 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..85
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028774"
FT CHAIN 86..477
FT /note="Stromelysin-3"
FT /id="PRO_0000028775"
FT REPEAT 280..324
FT /note="Hemopexin 1"
FT REPEAT 325..369
FT /note="Hemopexin 2"
FT REPEAT 370..418
FT /note="Hemopexin 3"
FT REPEAT 419..466
FT /note="Hemopexin 4"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT DISULFID 279..466
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 54442 MW; AAE4178E08CB6CA0 CRC64;
MHLLILLPAL CVLGAHSAPL SYTYLQHRIQ EKPQKDHGRL QFNSLHYPHI KGLLNAHGSW
NPPRCGVPDI PAPPDSSSGR NRQKRFVLSG GRWDKTNLTY KIIRFPWQLS KVKVRRTIAE
ALKVWSEVTP LTFTEVHEGR SDIIIDFTRY WHGDNLPFDG PGGILAHAFF PKTHREGDVH
FDYDEAWTIG NNIGTDLLQV AAHEFGHMLG LQHSSISKSL MSPFYTFRYP LSLSADDKHG
IQFLYGAPRP PTPSPTPRVE VNQVENESNE IPAAEPDACK TNFDAVSTIR GELFFFKSGY
VWRLRGGKLQ NGYPALASRH WRGIPDTVDA AFEDSVGNIW FFYGSQFWVF DGKLQASGPF
PITDIGISVT QIQAAFVWGT EKNKKTYLFR GGEYWRFNPE TRRVESRHSR RIGDWRGVPK
GIDAAFQDEQ GYAYFVKGRQ YWKFDPFKVR VMDGYPHLIS QDFFNCQASS TFVNSLR
