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 24-JAN-2024, entry version 132. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10116-ENSRNOP00000035334; -. DR Ensembl; ENSRNOT00000031400.6; ENSRNOP00000035334.4; ENSRNOG00000028344.6. DR Ensembl; ENSRNOT00055035607; ENSRNOP00055028876; ENSRNOG00055020844. DR Ensembl; ENSRNOT00060043628; ENSRNOP00060036175; ENSRNOG00060025154. DR Ensembl; ENSRNOT00065041673; ENSRNOP00065034060; ENSRNOG00065024284. DR GeneID; 25481; -. DR KEGG; rno:25481; -. DR UCSC; RGD:3099; rat. DR AGR; RGD:3099; -. 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; YWRFNPH; -. DR OrthoDB; 2225278at2759; -. 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 GO; GO:0031012; C:extracellular matrix; ISO:RGD. 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; 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; 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; IPR006026; Peptidase_Metallo. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. DR PANTHER; PTHR10201:SF20; STROMELYSIN-3; 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; Hemopexin-like domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS00024; HEMOPEXIN; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; Q499S5; RN. 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 //