Reviewed, UniProtKB/Swiss-Prot Q9EPL5 (MMP1A_MOUSE)

Names and origin

Protein names

Recommended name:
    Interstitial collagenase A
    EC=3.4.24.7
Alternative name(s):
    Mcol-A
    Matrix metalloproteinase-1a
      Short name=MMP-1a

Gene names

Name:	Mmp1a
Synonyms:	McolA

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	464 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	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.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – 96	79	Activation peptide By similarity		PRO_0000042645
	Chain	97 – 464	368	Interstitial collagenase A		PRO_0000042646
Regions
	Domain	282 – 324	43	Hemopexin-like 1
	Domain	326 – 370	45	Hemopexin-like 2
	Domain	375 – 422	48	Hemopexin-like 3
	Domain	424 – 464	41	Hemopexin-like 4
	Region	95 – 274	180	Metalloprotease
	Motif	87 – 94	8	Cysteine switch By similarity
Sites
	Active site	216	1	By similarity
	Metal binding	89	1	Zinc 2; in inhibited form By similarity
	Metal binding	155	1	Calcium 2 By similarity
	Metal binding	165	1	Zinc 1 By similarity
	Metal binding	167	1	Zinc 1 By similarity
	Metal binding	172	1	Calcium 3 By similarity
	Metal binding	173	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	180	1	Zinc 1 By similarity
	Metal binding	187	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	189	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	191	1	Calcium 2 By similarity
	Metal binding	193	1	Zinc 1 By similarity
	Metal binding	195	1	Calcium 3 By similarity
	Metal binding	198	1	Calcium 3 By similarity
	Metal binding	215	1	Zinc 2; catalytic By similarity
	Metal binding	219	1	Zinc 2; catalytic By similarity
	Metal binding	225	1	Zinc 2; catalytic By similarity
	Metal binding	283	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	376	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	425	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	202	1	N-linked (GlcNAc...) Potential
	Glycosylation	371	1	N-linked (GlcNAc...) Potential
	Disulfide bond	276 ↔ 464		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9EPL5-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 09FFC0470E5F9948	FASTA	464	53,488
	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

References

	« Hide 'large scale' referencesShow '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: 11113146] [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. , 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ278462 mRNA. Translation: CAC18880.1. AK049552 mRNA. Translation: BAC33807.1. AY211543 Genomic DNA. Translation: AAO37582.1. BC117756 mRNA. Translation: AAI17757.1.
IPI	IPI00110075.
RefSeq	NP_114395.1.
UniGene	Mm.156952
3D structure databases
HSSP	HSSP built from PDB template 1HY7 based on UniProtKB P08254.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9EPL5.
Protein family/group databases
MEROPS	M10.033.
Proteomic databases
PRIDE	Q9EPL5.
Genome annotation databases
Ensembl	ENSMUST00000034492; ENSMUSP00000034492; ENSMUSG00000043089; Mus musculus. [Genome view]
GeneID	83995.
KEGG	mmu:83995.
Organism-specific databases
CTD	83995.
MGI	MGI:1933846. Mmp1a.
Phylogenomic databases
HOGENOM	Q9EPL5.
HOVERGEN	Q9EPL5.
Enzyme and pathway databases
BRENDA	3.4.24.7. 244.
Gene expression databases
ArrayExpress	Q9EPL5.
Bgee	Q9EPL5.
Genevestigator	Q9EPL5.
GermOnline	ENSMUSG00000043089. Mus musculus.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
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]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	350854.
SOURCE	Search...

Entry information

Entry name

MMP1A_MOUSE

Accession

Primary (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:	October 13, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)