Q3U435 (MMP25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Matrix metalloproteinase-25
Short name=MMP-25
EC=3.4.24.-

Gene names

Name:

Mmp25

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	615 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May activate progelatinase A By similarity.
Cofactor	Binds 1 zinc ion per subunit By similarity. Calcium By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor Potential.
Domain	The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Post-translational modification	The precursor is cleaved by a furin endopeptidase By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.
Caution	In contrast to the human ortholog it does not have a signal sequence as it has an additional 53 residue sequence at the N-terminus. At the position of the human initiation methionine there is a leucine (Leu-54).

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	hard palate development Inferred from mutant phenotype PubMed 20809987. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from electronic annotation. Source: Compara extracellular matrix Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 20809987. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 162	162	By similarity		PRO_0000288635
	Chain	163 – 593	431	Matrix metalloproteinase-25		PRO_0000288636
	Propeptide	594 – 615	22	Removed in mature form Potential		PRO_0000288637
Regions
	Transmembrane	53 – 73	21	Helical; Potential
	Domain	375 – 419	45	Hemopexin-like 1
	Domain	424 – 466	43	Hemopexin-like 2
	Domain	470 – 516	47	Hemopexin-like 3
	Domain	518 – 562	45	Hemopexin-like 4
	Motif	143 – 150	8	Cysteine switch By similarity
	Compositional bias	158 – 162	5	Poly-Arg
	Compositional bias	340 – 368	29	Pro-rich
Sites
	Active site	288	1	By similarity
	Metal binding	145	1	Zinc; in inhibited form By similarity
	Metal binding	287	1	Zinc; catalytic By similarity
	Metal binding	291	1	Zinc; catalytic By similarity
	Metal binding	297	1	Zinc; catalytic By similarity
Amino acid modifications
	Lipidation	593	1	GPI-anchor amidated alanine Potential
	Disulfide bond	371 ↔ 562		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3U435 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 7B0842CACF06382D	FASTA	615	68,496
	10 20 30 40 50 60 MCFPGSQISP ARLYYLVSAP WICTGSLTSS RLPRRRESGP LRVPPRSVQA ERILRLPAFG 70 80 90 100 110 120 LPLLALLLVP LLPVRAQNPD AKVVSMGVEW LTRYGYLPPA DPVHAQMQSL EKLQDAIKVM 130 140 150 160 170 180 QRFAGLPETG QMDPMTIKTM RKPRCSLPDV LGAAGLVRRR RRYSLSGSVW KKRTLTWSIR 190 200 210 220 230 240 SFSQKSQLSP QIVRTLLSYA LAVWATESGL TFQEVNSQYQ EPDIIIHFAR AYHQDSYPFD 250 260 270 280 290 300 GSGGTLAHAF FPGEHPISGD THFDDEETWT FGSTDDNGID LFAVAVHEFG HALGLGHSSA 310 320 330 340 350 360 PNSIMRPFYQ GPVGDPATYR LPQDDRDGLQ QLYGRVSQNP NARPTRKPLV PPPQPPAMPP 370 380 390 400 410 420 DSPATPVPDR CEGNFDAVAN IRGEIFLFKG PWFWRLQPSG QLVSPRPAGL HRFWEGLPTH 430 440 450 460 470 480 VKVIQAAYAR PLDGRIILFS GPQFWVFQER QLEGAARPLV EFGLPPGEDV DAVFSWPHNG 490 500 510 520 530 540 KTYLIRGQKY WRYDEVAARP DPGYPRALSL WDGAPFAPDD VTISNTGDTY FFKGTHFWRF 550 560 570 580 590 600 AEGSVKAESD SPQPIGPKWL DCPAPNSDPR VTSPPKTTSK TRSCDCHCEL NQASEQLSPL 610 LLPLLPLVAG EVFSY

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK154458 mRNA. Translation: BAE32600.1. BC112379 mRNA. Translation: AAI12380.1.
IPI	IPI00352773.
RefSeq	NP_001028511.1. NM_001033339.3.
UniGene	Mm.235343.
3D structure databases
HSSP	HSSP built from PDB template 1CGL based on UniProtKB P03956.
ProteinModelPortal	Q3U435.
SMR	Q3U435. Positions 113-564.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000024696.
Protein family/group databases
MEROPS	M10.024.
PTM databases
PhosphoSite	Q3U435.
Proteomic databases
PRIDE	Q3U435.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
GeneID	240047.
KEGG	mmu:240047.
UCSC	uc008asq.1. mouse.
Organism-specific databases
CTD	64386.
MGI	MGI:2443938. Mmp25.
Phylogenomic databases
eggNOG	NOG295915.
GeneTree	ENSGT00700000104196.
HOGENOM	HOG000217928.
HOVERGEN	HBG052484.
InParanoid	Q3U435.
KO	K08003.
OMA	HYWRFPK.
OrthoDB	EOG40VVPC.
Gene expression databases
Bgee	Q3U435.
CleanEx	MM_MMP25.
Genevestigator	Q3U435.
Family and domain databases
Gene3D	1.10.101.10. 1 hit. 2.110.10.10. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR016293. Pept_M10A_Metazoans. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. False negative. PS00024. HEMOPEXIN. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	384387.
SOURCE	Search...

Entry information

Entry name

MMP25_MOUSE

Accession

Primary (citable) accession number: Q3U435

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program