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Protein

Interstitial collagenase

Gene

MMP1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X.

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca2+ ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

Enzyme regulationi

Can be activated without removal of the activation peptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
Metal bindingi124 – 1241Calcium 1
Metal bindingi158 – 1581Calcium 2
Metal bindingi168 – 1681Zinc 1
Metal bindingi170 – 1701Zinc 1
Metal bindingi175 – 1751Calcium 3
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygen
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygen
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen
Metal bindingi183 – 1831Zinc 1
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygen
Metal bindingi192 – 1921Calcium 2; via carbonyl oxygen
Metal bindingi194 – 1941Calcium 2
Metal bindingi196 – 1961Zinc 1
Metal bindingi198 – 1981Calcium 3
Metal bindingi199 – 1991Calcium 1
Metal bindingi201 – 2011Calcium 3
Metal bindingi218 – 2181Zinc 2; catalytic
Active sitei219 – 2191PROSITE-ProRule annotation1 Publication
Metal bindingi222 – 2221Zinc 2; catalytic
Metal bindingi228 – 2281Zinc 2; catalytic
Metal bindingi285 – 2851Calcium 4; via carbonyl oxygen
Metal bindingi329 – 3291Calcium 4; via carbonyl oxygen
Metal bindingi378 – 3781Calcium 4; via carbonyl oxygen
Metal bindingi427 – 4271Calcium 4; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SSC-1442490. Collagen degradation.
R-SSC-1474228. Degradation of the extracellular matrix.
R-SSC-1592389. Activation of Matrix Metalloproteinases.
R-SSC-210991. Basigin interactions.
R-SSC-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Protein family/group databases

MEROPSiM10.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Interstitial collagenase (EC:3.4.24.7)
Alternative name(s):
Matrix metalloproteinase-1
Short name:
MMP-1
Cleaved into the following chain:
Gene namesi
Name:MMP1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 9

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Propeptidei20 – 9980Activation peptide1 PublicationPRO_0000028707Add
BLAST
Chaini100 – 469370Interstitial collagenasePRO_0000028708Add
BLAST
Chaini100 – 25815918 kDa interstitial collagenasePRO_0000028709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571PhosphoserineBy similarity
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence analysis
Modified residuei274 – 2741PhosphothreonineBy similarity
Disulfide bondi278 ↔ 466
Modified residuei360 – 3601Phosphotyrosine; by PKDCCBy similarity

Post-translational modificationi

Undergoes autolytic cleavage to produce a N-terminal fragment having reduced collagenolytic activity.
Tyrosine phosphorylated in platelets by PKDCC/VLK.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei258 – 2592Cleavage; by autolysis

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP21692.
PeptideAtlasiP21692.

Miscellaneous databases

PMAP-CutDBP21692.

Expressioni

Gene expression databases

ExpressionAtlasiP21692. differential.
GenevisibleiP21692. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015909.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi110 – 1189Combined sources
Helixi127 – 14216Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi158 – 1647Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi182 – 1843Combined sources
Turni190 – 1934Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi204 – 2096Combined sources
Helixi212 – 22312Combined sources
Beta strandi237 – 2393Combined sources
Helixi250 – 26011Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi285 – 2906Combined sources
Beta strandi293 – 2986Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi313 – 3164Combined sources
Helixi317 – 3204Combined sources
Beta strandi329 – 3346Combined sources
Turni335 – 3384Combined sources
Beta strandi339 – 3446Combined sources
Beta strandi347 – 3526Combined sources
Helixi364 – 3685Combined sources
Beta strandi379 – 3835Combined sources
Turni384 – 3874Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi396 – 4016Combined sources
Turni402 – 4043Combined sources
Helixi415 – 4184Combined sources
Beta strandi427 – 4326Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi443 – 4486Combined sources
Turni449 – 4524Combined sources
Beta strandi453 – 4597Combined sources
Helixi462 – 4643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBLX-ray2.50A100-469[»]
ProteinModelPortaliP21692.
SMRiP21692. Positions 31-466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati275 – 32450Hemopexin 1Add
BLAST
Repeati325 – 37147Hemopexin 2Add
BLAST
Repeati374 – 42249Hemopexin 3Add
BLAST
Repeati423 – 46644Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switchBy similarity

Domaini

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 similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP21692.
KOiK01388.
OMAiFPGIGHK.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSLLLLLLL LCNTGSHGFP AATSETQEQD VEIVQKYLKN YYNLNSDGVP
60 70 80 90 100
VEKKRNSGLV VEKLKQMQQF FGLKVTGKPD AETLNVMKQP RCGVPDVAEF
110 120 130 140 150
VLTPGNPRWE NTHLTYRIEN YTPDLSREDV DRAIEKAFQL WSNVSPLTFT
160 170 180 190 200
KVSEGQADIM ISFVRGDHRD NSPFDGPGGN LAHAFQPGPG IGGDAHFDED
210 220 230 240 250
ERWTKNFRDY NLYRVAAHEL GHSLGLSHST DIGALMYPNY IYTGDVQLSQ
260 270 280 290 300
DDIDGIQAIY GPSENPVQPS GPQTPQVCDS KLTFDAITTL RGELMFFKDR
310 320 330 340 350
FYMRTNSFYP EVELNFISVF WPQVPNGLQA AYEIADRDEV RFFKGNKYWA
360 370 380 390 400
VRGQDVLYGY PKDIHRSFGF PSTVKNIDAA VFEEDTGKTY FFVAHECWRY
410 420 430 440 450
DEYKQSMDTG YPKMIAEEFP GIGNKVDAVF QKDGFLYFFH GTRQYQFDFK
460
TKRILTLQKA NSWFNCRKN
Length:469
Mass (Da):53,666
Last modified:December 1, 1992 - v2
Checksum:i7952D72B2753F682
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54724 mRNA. Translation: CAA38526.1.
PIRiS15986. KCPGI.
RefSeqiNP_001159701.1. NM_001166229.1.
UniGeneiSsc.16013.

Genome annotation databases

EnsembliENSSSCT00000016348; ENSSSCP00000015909; ENSSSCG00000014985.
GeneIDi397320.
KEGGissc:397320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54724 mRNA. Translation: CAA38526.1.
PIRiS15986. KCPGI.
RefSeqiNP_001159701.1. NM_001166229.1.
UniGeneiSsc.16013.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBLX-ray2.50A100-469[»]
ProteinModelPortaliP21692.
SMRiP21692. Positions 31-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015909.

Protein family/group databases

MEROPSiM10.001.

Proteomic databases

PaxDbiP21692.
PeptideAtlasiP21692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000016348; ENSSSCP00000015909; ENSSSCG00000014985.
GeneIDi397320.
KEGGissc:397320.

Organism-specific databases

CTDi4312.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP21692.
KOiK01388.
OMAiFPGIGHK.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiR-SSC-1442490. Collagen degradation.
R-SSC-1474228. Degradation of the extracellular matrix.
R-SSC-1592389. Activation of Matrix Metalloproteinases.
R-SSC-210991. Basigin interactions.
R-SSC-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

EvolutionaryTraceiP21692.
PMAP-CutDBP21692.

Gene expression databases

ExpressionAtlasiP21692. differential.
GenevisibleiP21692. SS.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP1_PIG
AccessioniPrimary (citable) accession number: P21692
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: December 1, 1992
Last modified: September 7, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.