Reviewed, UniProtKB/Swiss-Prot P13943 (MMP1_RABIT)

Names and origin

Protein names

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

Gene names

Name:

MMP1

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	468 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.
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.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
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	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 – 18	18
	Propeptide	19 – 98	80	Activation peptide		PRO_0000028710
	Chain	99 – 468	370	Interstitial collagenase		PRO_0000028711
Regions
	Domain	283 – 325	43	Hemopexin-like 1
	Domain	327 – 371	45	Hemopexin-like 2
	Domain	376 – 423	48	Hemopexin-like 3
	Domain	425 – 465	41	Hemopexin-like 4
	Motif	89 – 96	8	Cysteine switch By similarity
Sites
	Active site	218	1	By similarity
	Metal binding	91	1	Zinc 2; in inhibited form By similarity
	Metal binding	123	1	Calcium 1 By similarity
	Metal binding	157	1	Calcium 2 By similarity
	Metal binding	167	1	Zinc 1 By similarity
	Metal binding	169	1	Zinc 1 By similarity
	Metal binding	174	1	Calcium 3 By similarity
	Metal binding	175	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	177	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	179	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	182	1	Zinc 1 By similarity
	Metal binding	189	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	191	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	193	1	Calcium 2 By similarity
	Metal binding	195	1	Zinc 1 By similarity
	Metal binding	197	1	Calcium 3 By similarity
	Metal binding	198	1	Calcium 1 By similarity
	Metal binding	200	1	Calcium 3 By similarity
	Metal binding	217	1	Zinc 2; catalytic By similarity
	Metal binding	221	1	Zinc 2; catalytic By similarity
	Metal binding	227	1	Zinc 2; catalytic By similarity
	Metal binding	284	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	328	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	377	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	426	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	119	1	N-linked (GlcNAc...) Probable
	Disulfide bond	277 ↔ 465		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13943-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: DA90538919952B8C	FASTA	468	53,740
	10 20 30 40 50 60 MPGLPLLLLL LWGVGSHGFP AASETQEQDV EMVQKYLENY YNLKDDWRKI PKQRGNGLAV 70 80 90 100 110 120 EKLKQMQEFF GLKVTGKPDA ETLKMMKQPR CGVPDVAQFV LTPGNPRWEQ THLTYRIENY 130 140 150 160 170 180 TPDLSRADVD NAIEKAFQLW SNVTPLTFTK VSKGQADIMI SFVRGDHRDN SPFDGPEGQL 190 200 210 220 230 240 AHAFQPGLGI GGDVHFDEDD RWTKDFRNYN LYRVAAHELG HSLGLSHSTD IGALMYPNYM 250 260 270 280 290 300 FSGDVQLAQD DIDGIQAIYG PSQNPSQPVG PQTPKVCDSK LTFDAITTIR GEIMFFKDRF 310 320 330 340 350 360 YMRANPYYSE VELNFISVFW PHLPNGLQAA YEVAHRDEIL FFKGNKYWTV QGQNELPGYP 370 380 390 400 410 420 KDIHSSFGFP RSVNHIDAAV SEEDTGKTYF FVANKYWRYD EYKRSMDAGY PKMIEYDFPG 430 440 450 460 IGNKVDAVFK KDGFFYFFHG TRQYKFDPKT KRILTLQKAN SWFNCRKN

References

[1]	"A gene for rabbit synovial cell collagenase: member of a family of metalloproteinases that degrade the connective tissue matrix." Fini M.E., Plucinska I.M., Mayer A.S., Gross R.H., Brinckerhoff C.E. Biochemistry 26:6156-6165(1987) [PubMed: 2825772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Synovial cell.
[2]	"Homology between exon-containing portions of rabbit genomic clones for synovial cell collagenase and human foreskin and synovial cell mRNAs." Fini M.E., Austin S.D., Holt P.T., Ruby P.L., Gross R.H., White H.D., Brinckerhoff C.E. Coll. Relat. Res. 6:239-248(1986) [PubMed: 3021384] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 449-468. Strain: New Zealand white.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M17823 , M17820, M17821, M17822, M19240 mRNA. Translation: AAB88016.1. M25663 mRNA. Translation: AAA31203.1.
PIR	KCRBI. A27500.
UniGene	Ocu.2695
3D structure databases
HSSP	HSSP built from PDB template 1CGL based on UniProtKB P03956.
SMR	P13943. Positions 31-465.
ModBase	Search...
Protein-protein interaction databases
STRING	P13943.
Protein family/group databases
MEROPS	M10.001.
Phylogenomic databases
HOVERGEN	P13943.
Enzyme and pathway databases
BRENDA	3.4.24.7. 255.
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...

Entry information

Entry name

MMP1_RABIT

Accession

Primary (citable) accession number: P13943

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	September 22, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)