ID MMP10_RAT Reviewed; 476 AA. AC P07152; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 24-JAN-2024, entry version 175. DE RecName: Full=Stromelysin-2; DE Short=SL-2; DE EC=3.4.24.22; DE AltName: Full=Matrix metalloproteinase-10; DE Short=MMP-10; DE AltName: Full=Transformation-associated protein 34A; DE AltName: Full=Transin-2; DE Flags: Precursor; GN Name=Mmp10; 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]. RX PubMed=3547333; DOI=10.1093/nar/15.3.1139; RA Breathnach R., Matrisian L.M., Gesnel M.-C., Staub A., Leroy P.; RT "Sequences coding for part of oncogene-induced transin are highly conserved RT in a related rat gene."; RL Nucleic Acids Res. 15:1139-1151(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1370458; DOI=10.1016/s0021-9258(18)48401-3; RA Chan J.C., Scanlon M., Zhang H.Z., Jia L.B., Yu D., Hung M.C., French M., RA Eastman E.M.; RT "Molecular cloning and characterization of v-mos-activated transformation- RT associated proteins."; RL J. Biol. Chem. 267:1099-1103(1992). CC -!- FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; CC weakly collagens III, IV, and V. Activates procollagenase. CC -!- CATALYTIC ACTIVITY: CC Reaction=Similar to stromelysin 1, but action on collagen types III, IV CC and V is weak.; EC=3.4.24.22; 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; 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. CC -!- SIMILARITY: Belongs to the peptidase M10A family. {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; X05083; CAA28739.1; -; mRNA. DR EMBL; M65253; AAA42202.1; -; mRNA. DR PIR; B26403; KCRTS2. DR RefSeq; NP_598198.1; NM_133514.1. DR AlphaFoldDB; P07152; -. DR SMR; P07152; -. DR IntAct; P07152; 1. DR STRING; 10116.ENSRNOP00000013118; -. DR MEROPS; M10.011; -. DR PhosphoSitePlus; P07152; -. DR PaxDb; 10116-ENSRNOP00000013118; -. DR Ensembl; ENSRNOT00055009724; ENSRNOP00055007511; ENSRNOG00055006001. DR Ensembl; ENSRNOT00060027066; ENSRNOP00060021704; ENSRNOG00060015811. DR GeneID; 117061; -. DR KEGG; rno:117061; -. DR UCSC; RGD:620192; rat. DR AGR; RGD:620192; -. DR CTD; 4319; -. DR RGD; 620192; Mmp10. DR eggNOG; KOG1565; Eukaryota. DR InParanoid; P07152; -. DR OrthoDB; 391167at2759; -. DR PhylomeDB; P07152; -. DR Reactome; R-RNO-1442490; Collagen degradation. DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix. DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases. DR PRO; PR:P07152; -. DR Proteomes; UP000002494; Unplaced. 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: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 GO; GO:0030334; P:regulation of cell migration; ISO:RGD. 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; IPR021158; Pept_M10A_Zn_BS. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR002477; Peptidoglycan-bd-like. DR InterPro; IPR036365; PGBD-like_sf. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. DR PANTHER; PTHR10201:SF129; STROMELYSIN-2; 1. DR Pfam; PF00045; Hemopexin; 4. 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; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 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 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:0000305" FT PROPEP 18..99 FT /note="Activation peptide" FT /evidence="ECO:0000250" FT /id="PRO_0000028768" FT CHAIN 100..476 FT /note="Stromelysin-2" FT /id="PRO_0000028769" FT REPEAT 286..335 FT /note="Hemopexin 1" FT REPEAT 336..382 FT /note="Hemopexin 2" FT REPEAT 384..432 FT /note="Hemopexin 3" FT REPEAT 433..476 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 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 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 289..476 FT /evidence="ECO:0000250" SQ SEQUENCE 476 AA; 54222 MW; B556B6FB1D8BA7EE CRC64; MEPLAILVLL CFPICSAYPL HGAVRQDHST MDLAQQYLEK YYNFRKNEKQ FFKRKDSSPV VKKIEEMQKF LGLEMTGKLD SNTVEMMHKP RCGVPDVGGF STFPGSPKWR KNHISYRIVN YTLDLPRESV DSAIERALKV WEEVTPLTFS RISEGEADIM ISFAVGEHGD FYPFDGVGQS LAHAYPPGPG FYGDAHFDDD EKWSLGPSGT NLFLVAAHEL GHSLGLFHSN NKESLMYPVY RFSTSQANIR LSQDDIEGIQ SLYGARPSSD ATVVPVPSVS PKPETPVKCD PALSFDAVTM LRGEFLFFKD RHFWRRTQWN PEPEFHLISA FWPSLPSGLD AAYEANNKDR VLIFKGSQFW AVRGNEVQAG YPKRIHTLGF PPTVKKIDAA VFEKEKKKTY FFVGDKYWRF DETRQLMDKG FPRLITDDFP GIEPQVDAVL HAFGFFYFFC GSSQFEFDPN ARTVTHTLKS NSWLLC //