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Q9EPL5 (MMP1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interstitial collagenase A
EC=3.4.24.7
Alternative name(s):
Matrix metalloproteinase-1a
Short name=MMP-1a
Mcol-A
Gene names
Name:Mmp1a
Synonyms:McolA
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X By similarity. Able to degrade synthetic peptides and type I and II fibrillar collagen.

Catalytic activity

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

Cofactor

Binds 4 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Can be activated without removal of the activation peptide By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix Probable.

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.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 9679Activation peptide By similarity
PRO_0000042645
Chain97 – 464368Interstitial collagenase A
PRO_0000042646

Regions

Domain282 – 32443Hemopexin-like 1
Domain326 – 37045Hemopexin-like 2
Domain375 – 42248Hemopexin-like 3
Domain424 – 46441Hemopexin-like 4
Region95 – 274180Metalloprotease
Motif87 – 948Cysteine switch By similarity

Sites

Active site2161 By similarity
Metal binding891Zinc 2; in inhibited form By similarity
Metal binding1551Calcium 2 By similarity
Metal binding1651Zinc 1 By similarity
Metal binding1671Zinc 1 By similarity
Metal binding1721Calcium 3 By similarity
Metal binding1731Calcium 3; via carbonyl oxygen By similarity
Metal binding1801Zinc 1 By similarity
Metal binding1871Calcium 2; via carbonyl oxygen By similarity
Metal binding1891Calcium 2; via carbonyl oxygen By similarity
Metal binding1911Calcium 2 By similarity
Metal binding1931Zinc 1 By similarity
Metal binding1951Calcium 3 By similarity
Metal binding1981Calcium 3 By similarity
Metal binding2151Zinc 2; catalytic By similarity
Metal binding2191Zinc 2; catalytic By similarity
Metal binding2251Zinc 2; catalytic By similarity
Metal binding2831Calcium 4; via carbonyl oxygen By similarity
Metal binding3761Calcium 4; via carbonyl oxygen By similarity
Metal binding4251Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Disulfide bond276 ↔ 464 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9EPL5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 09FFC0470E5F9948

FASTA46453,488
        10         20         30         40         50         60 
MPSLPLLLLL WAASSYSFPV FHNGDRQNVE TVWKYLENYY NLGKNMQAKN VNGKEMMAEK 

        70         80         90        100        110        120 
LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT HNNPRWTKTH LTYSILNYTP 

       130        140        150        160        170        180 
YLPKAVVEDA IARAFRVWSD VTPLTFQRVF EEEGDIVLSF HRGDHGDNNP FDGPNYKLAH 

       190        200        210        220        230        240 
TFQPGPGLGG DVHYDLDETW TNSSENFNLF YVTAHELGHS LGLTHSSDIG ALMFPSYTWY 

       250        260        270        280        290        300 
TEDFVLNQDD INRIQDLYGP SPNPIQPTGA TTPHPCNGDL TFDAITTFRG EVFFFKGRFY 

       310        320        330        340        350        360 
IRVNRFMPEP ELNLIGILWP NLPVKLDAAY EASMIDQVRY FKGSKVWAVQ EQSVLRGFPR 

       370        380        390        400        410        420 
DIHSFFGFPS NVTHIDAAVC EEETGKTYFF VDHMYWRYDE NTQSMDPGYP RLTAEDFPGI 

       430        440        450        460 
DDKVDDVFQK GENFYFFHQS VQHRFNLQIR RVDDSRDSST WFNC

« Hide

References

« Hide 'large scale' references
[1]"Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation."
Balbin M., Fueyo A., Knauper V., Lopez J.M., Alvarez J., Sanchez L.M., Quesada V., Bordallo J., Murphy G., Lopez-Otin C.
J. Biol. Chem. 276:10253-10262(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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: C57BL/6J.
[3]"Genomic sequence analysis in the mouse T-complex region."
Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129/SvJ.
[4]"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		AJ278462 mRNA. Translation: CAC18880.1.
AK049552 mRNA. Translation: BAC33807.1.
AY211543 Genomic DNA. Translation: AAO37582.1.
BC117756 mRNA. Translation: AAI17757.1.
IPIIPI00110075.
RefSeqNP_114395.1. NM_032006.3.
UniGeneMm.156952.

3D structure databases

ProteinModelPortalQ9EPL5.
SMRQ9EPL5. Positions 29-463.
ModBaseSearch...

Protein family/group databases

MEROPSM10.033.

PTM databases

PhosphoSiteQ9EPL5.

Proteomic databases

PRIDEQ9EPL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83995.
KEGGmmu:83995.
UCSCuc009ocp.1. mouse.

Organism-specific databases

CTD83995.
MGIMGI:1933846. Mmp1a.

Phylogenomic databases

eggNOGNOG258253.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ149J4.
KOK01388.
OrthoDBEOG4X97GX.

Gene expression databases

ArrayExpressQ9EPL5.
BgeeQ9EPL5.
GenevestigatorQ9EPL5.
GermOnlineENSMUSG00000043089. Mus musculus.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_Metazoans.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350854.
SOURCESearch...

Entry information

Entry nameMMP1A_MOUSE
AccessionPrimary (citable) accession number: Q9EPL5
Secondary accession number(s): Q149J4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents