MMP11_RAT
ID MMP11_RAT Reviewed; 491 AA.
AC Q499S5; P97568;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Stromelysin-3;
DE Short=SL-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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND PROTEOLYTIC
RP PROCESSING.
RC STRAIN=Wistar;
RX PubMed=9055814; DOI=10.1016/s0378-1119(96)00615-4;
RA Okada A., Saez S., Misumi Y., Basset P.;
RT "Rat stromelysin 3: cDNA cloning from healing skin wound, activation by
RT furin and expression in rat tissues.";
RL Gene 185:187-193(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play an important role in the progression of epithelial
CC malignancies. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in ovary and uterus.
CC {ECO:0000269|PubMed:9055814}.
CC -!- INDUCTION: In skin fibroblasts of superficial dermis upon skin lesion
CC with highest level between days 5-10. {ECO:0000269|PubMed:9055814}.
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 -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC {ECO:0000269|PubMed:9055814}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH99781.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U46034; AAC53061.1; ALT_INIT; mRNA.
DR EMBL; BC099781; AAH99781.2; ALT_INIT; mRNA.
DR RefSeq; NP_037112.2; NM_012980.2.
DR RefSeq; XP_008772050.1; XM_008773828.2.
DR AlphaFoldDB; Q499S5; -.
DR SMR; Q499S5; -.
DR BioGRID; 247514; 2.
DR STRING; 10116.ENSRNOP00000035334; -.
DR MEROPS; M10.007; -.
DR PhosphoSitePlus; Q499S5; -.
DR PaxDb; Q499S5; -.
DR Ensembl; ENSRNOT00000031400; ENSRNOP00000035334; ENSRNOG00000028344.
DR GeneID; 25481; -.
DR KEGG; rno:25481; -.
DR UCSC; RGD:3099; rat.
DR CTD; 4320; -.
DR RGD; 3099; Mmp11.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000156340; -.
DR HOGENOM; CLU_015489_8_3_1; -.
DR InParanoid; Q499S5; -.
DR OMA; IYIFSGG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q499S5; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR PRO; PR:Q499S5; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000028344; Expressed in skeletal muscle tissue.
DR Genevisible; Q499S5; RN.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071711; P:basement membrane organization; ISO:RGD.
DR GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
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; 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; 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..35
FT /evidence="ECO:0000255"
FT PROPEP 36..101
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042649"
FT CHAIN 102..491
FT /note="Stromelysin-3"
FT /id="PRO_0000042650"
FT REPEAT 298..342
FT /note="Hemopexin 1"
FT REPEAT 343..385
FT /note="Hemopexin 2"
FT REPEAT 387..435
FT /note="Hemopexin 3"
FT REPEAT 436..483
FT /note="Hemopexin 4"
FT REGION 260..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..89
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 262..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 84
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"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 297..483
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 55511 MW; B0C5B191A623FD41 CRC64;
MARAACLLRA ISRALLLPLP LLLLLLLLLP PQLMARARPP ENHRHRPVKR VPQLLPAALP
NSLPSVPASH WVPGPASSSR PLRCGVPDPP DVLNARNRQK RFVLSGGRWE KTDLTYRILR
FPWQLVREQV RQTVAEALRV WSEVTPLTFT EVHEGRADIM IDFTRYWHGD NLPFDGPGGI
LAHAFFPKTH REGDVHFDYD ETWTIGDKGT DLLQVAAHEF GHVLGLQHTT AAKALMSPFY
TFRYPLSLSP DDRRGIQHLY GRPQLTPTSP TPTLSSQAGT DTNEIALQEP EVPPEVCETS
FDAVSTIRGE LFFFKAGFVW RLRSGQLQPG YPALASRHWQ GLPSPVDAAF EDAQGQIWFF
QGAQYWVYDG EKPVLGPAPL SKLGLQGSPV HAALVWGPEK NKIYFFRGGD YWRFHPRTQR
VDNPVPRRTT DWRGVPSEID AAFQDAEGYA YFLRGHLYWK FDPVKVKVLE SFPRPIGPDF
FDCAEPANTF R
