MMP10_RAT
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 03-AUG-2022, entry version 169.
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}.
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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 PaxDb; P07152; -.
DR PRIDE; P07152; -.
DR GeneID; 117061; -.
DR KEGG; rno:117061; -.
DR UCSC; RGD:620192; rat.
DR CTD; 4319; -.
DR RGD; 620192; Mmp10.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P07152; -.
DR OrthoDB; 1075463at2759; -.
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:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 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; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
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; SSF47090; SSF47090; 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 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
