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Q3U435

- MMP25_MOUSE

UniProt

Q3U435 - MMP25_MOUSE

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Protein

Matrix metalloproteinase-25

Gene

Mmp25

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

May activate progelatinase A.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi145 – 1451Zinc; in inhibited formBy similarity
Metal bindingi287 – 2871Zinc; catalyticPROSITE-ProRule annotation
Active sitei288 – 2881PROSITE-ProRule annotation
Metal bindingi291 – 2911Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi297 – 2971Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. hard palate development Source: MGI
  2. inflammatory response Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.024.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-25 (EC:3.4.24.-)
Short name:
MMP-25
Gene namesi
Name:Mmp25
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:2443938. Mmp25.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei53 – 7321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. extracellular matrix Source: InterPro
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 162162By similarityPRO_0000288635Add
BLAST
Chaini163 – 593431Matrix metalloproteinase-25PRO_0000288636Add
BLAST
Propeptidei594 – 61522Removed in mature formSequence AnalysisPRO_0000288637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi371 ↔ 562By similarity
Lipidationi593 – 5931GPI-anchor amidated alanineSequence Analysis

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

Proteomic databases

PRIDEiQ3U435.

PTM databases

PhosphoSiteiQ3U435.

Expressioni

Gene expression databases

BgeeiQ3U435.
CleanExiMM_MMP25.
GenevestigatoriQ3U435.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024696.

Structurei

3D structure databases

ProteinModelPortaliQ3U435.
SMRiQ3U435. Positions 113-564.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati368 – 41750Hemopexin 1Add
BLAST
Repeati421 – 46646Hemopexin 2Add
BLAST
Repeati467 – 51549Hemopexin 3Add
BLAST
Repeati516 – 56247Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi143 – 1508Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi158 – 1625Poly-Arg
Compositional biasi340 – 36829Pro-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ3U435.
KOiK08003.
OMAiHYWRFPK.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ3U435.
TreeFamiTF315428.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028733. MMP25.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF21. PTHR10201:SF21. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U435-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCFPGSQISP ARLYYLVSAP WICTGSLTSS RLPRRRESGP LRVPPRSVQA
60 70 80 90 100
ERILRLPAFG LPLLALLLVP LLPVRAQNPD AKVVSMGVEW LTRYGYLPPA
110 120 130 140 150
DPVHAQMQSL EKLQDAIKVM QRFAGLPETG QMDPMTIKTM RKPRCSLPDV
160 170 180 190 200
LGAAGLVRRR RRYSLSGSVW KKRTLTWSIR SFSQKSQLSP QIVRTLLSYA
210 220 230 240 250
LAVWATESGL TFQEVNSQYQ EPDIIIHFAR AYHQDSYPFD GSGGTLAHAF
260 270 280 290 300
FPGEHPISGD THFDDEETWT FGSTDDNGID LFAVAVHEFG HALGLGHSSA
310 320 330 340 350
PNSIMRPFYQ GPVGDPATYR LPQDDRDGLQ QLYGRVSQNP NARPTRKPLV
360 370 380 390 400
PPPQPPAMPP DSPATPVPDR CEGNFDAVAN IRGEIFLFKG PWFWRLQPSG
410 420 430 440 450
QLVSPRPAGL HRFWEGLPTH VKVIQAAYAR PLDGRIILFS GPQFWVFQER
460 470 480 490 500
QLEGAARPLV EFGLPPGEDV DAVFSWPHNG KTYLIRGQKY WRYDEVAARP
510 520 530 540 550
DPGYPRALSL WDGAPFAPDD VTISNTGDTY FFKGTHFWRF AEGSVKAESD
560 570 580 590 600
SPQPIGPKWL DCPAPNSDPR VTSPPKTTSK TRSCDCHCEL NQASEQLSPL
610
LLPLLPLVAG EVFSY
Length:615
Mass (Da):68,496
Last modified:October 11, 2005 - v1
Checksum:i7B0842CACF06382D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154458 mRNA. Translation: BAE32600.1.
BC112379 mRNA. Translation: AAI12380.1.
CCDSiCCDS28452.1.
RefSeqiNP_001028511.1. NM_001033339.3.
UniGeneiMm.235343.

Genome annotation databases

EnsembliENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
GeneIDi240047.
KEGGimmu:240047.
UCSCiuc008asq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154458 mRNA. Translation: BAE32600.1 .
BC112379 mRNA. Translation: AAI12380.1 .
CCDSi CCDS28452.1.
RefSeqi NP_001028511.1. NM_001033339.3.
UniGenei Mm.235343.

3D structure databases

ProteinModelPortali Q3U435.
SMRi Q3U435. Positions 113-564.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000024696.

Protein family/group databases

MEROPSi M10.024.

PTM databases

PhosphoSitei Q3U435.

Proteomic databases

PRIDEi Q3U435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024696 ; ENSMUSP00000024696 ; ENSMUSG00000023903 .
GeneIDi 240047.
KEGGi mmu:240047.
UCSCi uc008asq.1. mouse.

Organism-specific databases

CTDi 64386.
MGIi MGI:2443938. Mmp25.

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi Q3U435.
KOi K08003.
OMAi HYWRFPK.
OrthoDBi EOG7XPZ57.
PhylomeDBi Q3U435.
TreeFami TF315428.

Miscellaneous databases

NextBioi 384387.
PROi Q3U435.
SOURCEi Search...

Gene expression databases

Bgeei Q3U435.
CleanExi MM_MMP25.
Genevestigatori Q3U435.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028733. MMP25.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF21. PTHR10201:SF21. 1 hit.
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiMMP25_MOUSE
AccessioniPrimary (citable) accession number: Q3U435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: November 26, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3