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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)DescriptionActionsGraphical viewLength
Metal bindingi92Zinc 2; in inhibited formBy similarity1
Metal bindingi124Calcium 11
Metal bindingi158Calcium 21
Metal bindingi168Zinc 11
Metal bindingi170Zinc 11
Metal bindingi175Calcium 31
Metal bindingi176Calcium 3; via carbonyl oxygen1
Metal bindingi178Calcium 3; via carbonyl oxygen1
Metal bindingi180Calcium 3; via carbonyl oxygen1
Metal bindingi183Zinc 11
Metal bindingi190Calcium 2; via carbonyl oxygen1
Metal bindingi192Calcium 2; via carbonyl oxygen1
Metal bindingi194Calcium 21
Metal bindingi196Zinc 11
Metal bindingi198Calcium 31
Metal bindingi199Calcium 11
Metal bindingi201Calcium 31
Metal bindingi218Zinc 2; catalytic1
Active sitei219PROSITE-ProRule annotation1 Publication1
Metal bindingi222Zinc 2; catalytic1
Metal bindingi228Zinc 2; catalytic1
Metal bindingi285Calcium 4; via carbonyl oxygen1
Metal bindingi329Calcium 4; via carbonyl oxygen1
Metal bindingi378Calcium 4; via carbonyl oxygen1
Metal bindingi427Calcium 4; via carbonyl oxygen1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
PropeptideiPRO_000002870720 – 99Activation peptide1 PublicationAdd BLAST80
ChainiPRO_0000028708100 – 469Interstitial collagenaseAdd BLAST370
ChainiPRO_0000028709100 – 25818 kDa interstitial collagenaseAdd BLAST159

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei57PhosphoserineBy similarity1
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Modified residuei274PhosphothreonineBy similarity1
Disulfide bondi278 ↔ 466
Modified residuei360Phosphotyrosine; by PKDCCBy similarity1

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)DescriptionActionsGraphical viewLength
Sitei258 – 259Cleavage; by autolysis2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP21692.
PeptideAtlasiP21692.
PRIDEiP21692.

Miscellaneous databases

PMAP-CutDBP21692.

Expressioni

Gene expression databases

ExpressionAtlasiP21692. baseline.
GenevisibleiP21692. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015909.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi110 – 118Combined sources9
Helixi127 – 142Combined sources16
Beta strandi148 – 155Combined sources8
Beta strandi158 – 164Combined sources7
Beta strandi169 – 171Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi182 – 184Combined sources3
Turni190 – 193Combined sources4
Beta strandi195 – 198Combined sources4
Beta strandi204 – 209Combined sources6
Helixi212 – 223Combined sources12
Beta strandi237 – 239Combined sources3
Helixi250 – 260Combined sources11
Beta strandi264 – 267Combined sources4
Beta strandi285 – 290Combined sources6
Beta strandi293 – 298Combined sources6
Beta strandi301 – 305Combined sources5
Beta strandi313 – 316Combined sources4
Helixi317 – 320Combined sources4
Beta strandi329 – 334Combined sources6
Turni335 – 338Combined sources4
Beta strandi339 – 344Combined sources6
Beta strandi347 – 352Combined sources6
Helixi364 – 368Combined sources5
Beta strandi379 – 383Combined sources5
Turni384 – 387Combined sources4
Beta strandi388 – 393Combined sources6
Beta strandi396 – 401Combined sources6
Turni402 – 404Combined sources3
Helixi415 – 418Combined sources4
Beta strandi427 – 432Combined sources6
Beta strandi435 – 440Combined sources6
Beta strandi443 – 448Combined sources6
Turni449 – 452Combined sources4
Beta strandi453 – 459Combined sources7
Helixi462 – 464Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP21692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati275 – 324Hemopexin 1Add BLAST50
Repeati325 – 371Hemopexin 2Add BLAST47
Repeati374 – 422Hemopexin 3Add BLAST49
Repeati423 – 466Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi90 – 97Cysteine switchBy similarity8

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

CDDicd00094. HX. 1 hit.
cd04278. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBLX-ray2.50A100-469[»]
ProteinModelPortaliP21692.
SMRiP21692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015909.

Protein family/group databases

MEROPSiM10.001.

Proteomic databases

PaxDbiP21692.
PeptideAtlasiP21692.
PRIDEiP21692.

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. baseline.
GenevisibleiP21692. SS.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. 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: November 30, 2016
This is version 149 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.