Interstitial collagenase precursor

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Reviewed, UniProtKB/Swiss-Prot P28053 (MMP1_BOVIN)

Last modified September 22, 2009. Version 83. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	MMP1
Synonyms:	CLG

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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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
Technical term	Direct protein sequencing
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Ref.2

Propeptide

19 – 99

Activation peptide

PRO_0000028699

Chain

100 – 469

370

Interstitial collagenase

PRO_0000028700

Regions

Domain

284 – 326

Hemopexin-like 1

Domain

328 – 372

Hemopexin-like 2

Domain

377 – 424

Hemopexin-like 3

Domain

426 – 466

Hemopexin-like 4

Motif

90 – 97

Cysteine switch By similarity

Sites

Active site

219

By similarity

Metal binding

Zinc 2; in inhibited form By similarity

Metal binding

124

Calcium 1 By similarity

Metal binding

158

Calcium 2 By similarity

Metal binding

168

Zinc 1 By similarity

Metal binding

170

Zinc 1 By similarity

Metal binding

175

Calcium 3 By similarity

Metal binding

176

Calcium 3; via carbonyl oxygen By similarity

Metal binding

178

Calcium 3; via carbonyl oxygen By similarity

Metal binding

180

Calcium 3; via carbonyl oxygen By similarity

Metal binding

183

Zinc 1 By similarity

Metal binding

190

Calcium 2; via carbonyl oxygen By similarity

Metal binding

192

Calcium 2; via carbonyl oxygen By similarity

Metal binding

194

Calcium 2 By similarity

Metal binding

196

Zinc 1 By similarity

Metal binding

198

Calcium 3 By similarity

Metal binding

199

Calcium 1 By similarity

Metal binding

201

Calcium 3 By similarity

Metal binding

218

Zinc 2; catalytic By similarity

Metal binding

222

Zinc 2; catalytic By similarity

Metal binding

228

Zinc 2; catalytic By similarity

Metal binding

285

Calcium 4; via carbonyl oxygen By similarity

Metal binding

329

Calcium 4; via carbonyl oxygen By similarity

Metal binding

378

Calcium 4; via carbonyl oxygen By similarity

Metal binding

427

Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

120

N-linked (GlcNAc...) Potential

Disulfide bond

278 ↔ 466

By similarity

Experimental info

Sequence conflict

22 – 23

AT → FP AA sequence Ref.2

Sequence conflict

D → L AA sequence Ref.2

Sequence conflict

35 – 36

KK → LL AA sequence Ref.2

Sequence conflict

N → F AA sequence Ref.2

Sequence conflict

106 – 108

KSC → NPR AA sequence Ref.2

Sequence conflict

113

N → D AA sequence Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P28053-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B4A5504CE24BD7B5
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FASTA

469

53,354

        10         20         30         40         50         60 
MPRLPLLLLL LWGTGSHGFP AATSETQEQD VETVKKYLEN YYNLNSNGKK VERQRNGGLI 

        70         80         90        100        110        120 
TEKLKQMQKF FGLRVTGKPD AETLNVMKQP RCGVPDVAPF VLTPGKSCWE NTNLTYRIEN 

       130        140        150        160        170        180 
YTPDLSRADV DQAIEKAFQL WSNVTPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN 

       190        200        210        220        230        240 
LAHAFQPGAG IGGDAHFDDD EWWTSNFQDY NLYRVAAHEF GHSLGLAHST DIGALMYPSY 

       250        260        270        280        290        300 
TFSGDVQLSQ DDIDGIQAIY GPSQNPTQPV GPQTPEVCDS KLTFDAITTI RGEVMFFKDR 

       310        320        330        340        350        360 
FYMRTNPLYP EVELNFISVF WPQLPNGLQA AYEVADRDEV RFFKGNKYWA VKGQDVLRGY 

       370        380        390        400        410        420 
PRDIYRSFGF PRTVKSIDAA VSEEDTGKTY FFVANKCWRY DEYKQSMDAG YPKMIAEDFP 

       430        440        450        460 
GIGNKVDAVF QKGGFFYFFH GRRQYKFDPQ TKRILTLLKA NSWFNCRKN

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References

[1]	"Primary structure of bovine interstitial collagenase deduced from cDNA sequence." Tamura M., Shimokawa H., Sasaki S. DNA Seq. 5:63-66(1994) [PubMed: 7894061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Periodontium fibroblast.
[2]	"Purification and characterization of bovine interstitial collagenase and tissue inhibitor of metalloproteinases." Sudbeck B.D., Jeffrey J.J., Welgus H.G., Mecham R.P., McCourt D., Parks W.C. Arch. Biochem. Biophys. 293:370-376(1992) [PubMed: 1311165] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-39 AND 85-125.

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Cross-references

Sequence databases
	X58256 mRNA. Translation: CAA41210.1.
IPI	IPI00707864.
PIR	KCBOI. S14654.
RefSeq	NP_776537.1.
UniGene	Bt.3417
3D structure databases
HSSP	HSSP built from PDB template 1HFC based on UniProtKB P03956.
ModBase	Search...
Protein-protein interaction databases
STRING	P28053.
Protein family/group databases
MEROPS	M10.001.
Genome annotation databases
Ensembl	ENSBTAT00000021014; ENSBTAP00000021014; ENSBTAG00000015818; Bos taurus. [Genome view] ENSBTAT00000049622; ENSBTAP00000046488; ENSBTAG00000015818; Bos taurus. [Genome view]
GeneID	281308.
KEGG	bta:281308.
Organism-specific databases
CTD	281308.
Phylogenomic databases
HOVERGEN	P28053.
Enzyme and pathway databases
BRENDA	3.4.24.7. 251.
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...

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Entry information

Entry name

MMP1_BOVIN

Accession

Primary (citable) accession number: P28053

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	September 22, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents