Reviewed, UniProtKB/Swiss-Prot Q9EPL6 (MMP1B_MOUSE)

Names and origin

Protein names

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

Gene names

Name:	Mmp1b
Synonyms:	McolB

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	463 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)

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_0000042647
	Chain	97 – 463	367	Interstitial collagenase B		PRO_0000042648
Regions
	Domain	281 – 323	43	Hemopexin-like 1
	Domain	325 – 369	45	Hemopexin-like 2
	Domain	374 – 421	48	Hemopexin-like 3
	Domain	423 – 463	41	Hemopexin-like 4
	Region	95 – 273	179	Metalloprotease By similarity
	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	193	1	Zinc 1 By similarity
	Metal binding	195	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	282	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	375	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	424	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	370	1	N-linked (GlcNAc...) Potential
	Disulfide bond	275 ↔ 463		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9EPL6-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 46013AB9D106C3F1	FASTA	463	53,492
	10 20 30 40 50 60 MPSLPLLLRL WAASSYSFPV IQDGLQKNVK TVWKYLENYY NLGKNMQAKN VNGKEVMAEK 70 80 90 100 110 120 LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT HNNPRWTKTH LTYSILNYTP 130 140 150 160 170 180 YLSKAVVEDA IARAFRVWSD VTPLTFQRVF EEEGDIVLSF HRGDHGDLYT FDGSKYHFAH 190 200 210 220 230 240 AFLPGLGLGG NVHYDLDQKW TDNNEDFNLF YVTAHELGHS LGLSHSNDEE ALMFPSYTWS 250 260 270 280 290 300 NKDFVLNQDD INRIQALYGP SPNPIQLTDA TLDPCNSGLT FDAIITYRGE VIFFKDRFYI 310 320 330 340 350 360 RVISFLPEPL IDVIDLTWPN LPGKFDAAYE VSGVDELRFF KGSKVWAVQE QNVLEGFPMD 370 380 390 400 410 420 IQSFFGFPSN VTNIDAAVCE EETGKTYFFV DHMYWRYDEN TRSMDPGYPR LIAEDFPGID 430 440 450 460 YKVDDVIQKE DNFYFFHQSI QYRFNLKTRR IDDSSDINTW FNC

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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ278461 mRNA. Translation: CAC18879.1.
IPI	IPI00110076.
UniGene	Mm.379271
3D structure databases
SMR	Q9EPL6. Positions 30-463.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9EPL6.
Protein family/group databases
MEROPS	M10.034.
Proteomic databases
PRIDE	Q9EPL6.
Genome annotation databases
Ensembl	ENSMUST00000047888; ENSMUSP00000047261; ENSMUSG00000041620; Mus musculus. [Genome view]
UCSC	uc009ocn.1. mouse.
Organism-specific databases
MGI	MGI:1933847. Mmp1b.
Phylogenomic databases
HOGENOM	HBG747685.
HOVERGEN	Q9EPL6.
InParanoid	Q9EPL6.
Enzyme and pathway databases
BRENDA	3.4.24.7. 244.
Gene expression databases
ArrayExpress	Q9EPL6.
Bgee	Q9EPL6.
Genevestigator	Q9EPL6.
GermOnline	ENSMUSG00000041620. 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. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00045. Hemopexin. 2 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
SOURCE	Search...

Entry information

Entry name

MMP1B_MOUSE

Accession

Primary (citable) accession number: Q9EPL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	March 1, 2001
Last modified:	January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)