MMP10_MOUSE
ID MMP10_MOUSE Reviewed; 476 AA.
AC O55123;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, 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=Transin-2;
DE Flags: Precursor;
GN Name=Mmp10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9427548; DOI=10.1016/s0378-1119(97)00456-3;
RA Madlener M., Werner S.;
RT "cDNA cloning and expression of the gene encoding murine stromelysin-2
RT (MMP-10).";
RL Gene 202:75-81(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- TISSUE SPECIFICITY: Expressed in small intestine. Weak levels in heart
CC and lung.
CC -!- INDUCTION: By wounding.
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; Y13185; CAA73641.1; -; mRNA.
DR EMBL; AK020292; BAB32058.1; -; mRNA.
DR CCDS; CCDS22807.1; -.
DR PIR; JC6505; JC6505.
DR RefSeq; NP_062344.1; NM_019471.3.
DR AlphaFoldDB; O55123; -.
DR SMR; O55123; -.
DR STRING; 10090.ENSMUSP00000034488; -.
DR MEROPS; M10.011; -.
DR iPTMnet; O55123; -.
DR PhosphoSitePlus; O55123; -.
DR MaxQB; O55123; -.
DR PaxDb; O55123; -.
DR PRIDE; O55123; -.
DR ProteomicsDB; 291369; -.
DR DNASU; 17384; -.
DR Ensembl; ENSMUST00000034488; ENSMUSP00000034488; ENSMUSG00000047562.
DR GeneID; 17384; -.
DR KEGG; mmu:17384; -.
DR UCSC; uc009ocq.2; mouse.
DR CTD; 4319; -.
DR MGI; MGI:97007; Mmp10.
DR VEuPathDB; HostDB:ENSMUSG00000047562; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000159759; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; O55123; -.
DR OMA; YVWRKSP; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; O55123; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.22; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 17384; 0 hits in 73 CRISPR screens.
DR PRO; PR:O55123; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O55123; protein.
DR Bgee; ENSMUSG00000047562; Expressed in small intestine Peyer's patch and 16 other tissues.
DR ExpressionAtlas; O55123; baseline and differential.
DR Genevisible; O55123; MM.
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; IMP:MGI.
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_0000028766"
FT CHAIN 100..476
FT /note="Stromelysin-2"
FT /id="PRO_0000028767"
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; 53911 MW; 2EB1CC41468F0AC6 CRC64;
MEPLAILALL SLPICSAYPL HGAVTQGHPS MDLAQQYLEK YYNFKKNEKQ IFKRKDSSPV
VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF STFPGSPKWR KSHITYRIVN
YTPDLPRQSV DSAIEKALKV WEEVTPLTFS RISEGEADIM ISFAVGEHGD FYPFDGPGQS
LAHAYPPGPG FYGDVHFDDD EKWTLAPSGT NLFLVAAHEL GHSLGLFHSD KKESLMYPVY
RFSTSPANFH LSQDDIEGIQ SLYGAGPSSD ATVVPVLSVS PRPETPDKCD PALSFDSVST
LRGEVLFFKD RYFWRRSHWN PEPEFHLISA FWPTLPSDLD AAYEAHNTDS VLIFKGSQFW
AVRGNEVQAG YPKGIHTLGF PPTVKKIDAA VFEKEKKKTY FFVGDKYWRF DETRHVMDKG
FPRQITDDFP GIEPQVDAVL HEFGFFYFFR GSSQFEFDPN ARTVTHILKS NSWLLC
