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   24-JAN-2024, entry version 141.
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}.
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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; 10090-ENSMUSP00000024696; -.
DR   ProteomicsDB; 295690; -.
DR   Antibodypedia; 10685; 335 antibodies from 29 providers.
DR   DNASU; 240047; -.
DR   Ensembl; ENSMUST00000024696.9; ENSMUSP00000024696.8; ENSMUSG00000023903.9.
DR   GeneID; 240047; -.
DR   KEGG; mmu:240047; -.
DR   UCSC; uc008asq.1; mouse.
DR   AGR; MGI:2443938; -.
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; PYYQGSV; -.
DR   OrthoDB; 2225278at2759; -.
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 79 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 31 other cell types or tissues.
DR   ExpressionAtlas; Q3U435; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; 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; 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   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF142; MATRIX METALLOPROTEINASE-25; 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; 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
//