MMP25_MOUSE
ID MMP25_MOUSE Reviewed; 615 AA.
AC Q3U435;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Matrix metalloproteinase-25;
DE Short=MMP-25;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Mmp25;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 activate progelatinase A. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {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 -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- CAUTION: In contrast to the human ortholog it does not have a signal
CC sequence as it has an additional 53 residue sequence at the N-terminus.
CC At the position of the human initiation methionine there is a leucine
CC (Leu-54). {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; AK154458; BAE32600.1; -; mRNA.
DR EMBL; BC112379; AAI12380.1; -; mRNA.
DR CCDS; CCDS28452.1; -.
DR RefSeq; NP_001028511.1; NM_001033339.4.
DR AlphaFoldDB; Q3U435; -.
DR SMR; Q3U435; -.
DR STRING; 10090.ENSMUSP00000024696; -.
DR MEROPS; M10.024; -.
DR PhosphoSitePlus; Q3U435; -.
DR MaxQB; Q3U435; -.
DR PaxDb; Q3U435; -.
DR PRIDE; Q3U435; -.
DR ProteomicsDB; 295690; -.
DR Antibodypedia; 10685; 308 antibodies from 29 providers.
DR DNASU; 240047; -.
DR Ensembl; ENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
DR GeneID; 240047; -.
DR KEGG; mmu:240047; -.
DR UCSC; uc008asq.1; mouse.
DR CTD; 64386; -.
DR MGI; MGI:2443938; Mmp25.
DR VEuPathDB; HostDB:ENSMUSG00000023903; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000159799; -.
DR HOGENOM; CLU_015489_8_2_1; -.
DR InParanoid; Q3U435; -.
DR OMA; FFFKGPY; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q3U435; -.
DR TreeFam; TF315428; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 240047; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Mmp25; mouse.
DR PRO; PR:Q3U435; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3U435; protein.
DR Bgee; ENSMUSG00000023903; Expressed in granulocyte and 29 other tissues.
DR ExpressionAtlas; Q3U435; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0016504; F:peptidase activator activity; ISO:MGI.
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:0060022; P:hard palate development; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; ISO: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; 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; 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; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Zinc;
KW Zymogen.
FT PROPEP 1..162
FT /evidence="ECO:0000250"
FT /id="PRO_0000288635"
FT CHAIN 163..593
FT /note="Matrix metalloproteinase-25"
FT /id="PRO_0000288636"
FT PROPEP 594..615
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000288637"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 368..417
FT /note="Hemopexin 1"
FT REPEAT 421..466
FT /note="Hemopexin 2"
FT REPEAT 467..515
FT /note="Hemopexin 3"
FT REPEAT 516..562
FT /note="Hemopexin 4"
FT REGION 336..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..150
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 345..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 145
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 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 593
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT DISULFID 371..562
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 68496 MW; 7B0842CACF06382D CRC64;
MCFPGSQISP ARLYYLVSAP WICTGSLTSS RLPRRRESGP LRVPPRSVQA ERILRLPAFG
LPLLALLLVP LLPVRAQNPD AKVVSMGVEW LTRYGYLPPA DPVHAQMQSL EKLQDAIKVM
QRFAGLPETG QMDPMTIKTM RKPRCSLPDV LGAAGLVRRR RRYSLSGSVW KKRTLTWSIR
SFSQKSQLSP QIVRTLLSYA LAVWATESGL TFQEVNSQYQ EPDIIIHFAR AYHQDSYPFD
GSGGTLAHAF FPGEHPISGD THFDDEETWT FGSTDDNGID LFAVAVHEFG HALGLGHSSA
PNSIMRPFYQ GPVGDPATYR LPQDDRDGLQ QLYGRVSQNP NARPTRKPLV PPPQPPAMPP
DSPATPVPDR CEGNFDAVAN IRGEIFLFKG PWFWRLQPSG QLVSPRPAGL HRFWEGLPTH
VKVIQAAYAR PLDGRIILFS GPQFWVFQER QLEGAARPLV EFGLPPGEDV DAVFSWPHNG
KTYLIRGQKY WRYDEVAARP DPGYPRALSL WDGAPFAPDD VTISNTGDTY FFKGTHFWRF
AEGSVKAESD SPQPIGPKWL DCPAPNSDPR VTSPPKTTSK TRSCDCHCEL NQASEQLSPL
LLPLLPLVAG EVFSY
