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Protein

Interstitial collagenase

Gene

MMP1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Can be activated without removal of the activation peptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Zinc 2; in inhibited formBy similarity
Metal bindingi123 – 1231Calcium 1By similarity
Metal bindingi157 – 1571Calcium 2By similarity
Metal bindingi167 – 1671Zinc 1By similarity
Metal bindingi169 – 1691Zinc 1By similarity
Metal bindingi174 – 1741Calcium 3By similarity
Metal bindingi175 – 1751Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi177 – 1771Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi179 – 1791Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi182 – 1821Zinc 1By similarity
Metal bindingi189 – 1891Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi191 – 1911Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi193 – 1931Calcium 2By similarity
Metal bindingi195 – 1951Zinc 1By similarity
Metal bindingi197 – 1971Calcium 3By similarity
Metal bindingi198 – 1981Calcium 1By similarity
Metal bindingi200 – 2001Calcium 3By similarity
Metal bindingi217 – 2171Zinc 2; catalyticBy similarity
Active sitei218 – 2181PROSITE-ProRule annotation
Metal bindingi221 – 2211Zinc 2; catalyticBy similarity
Metal bindingi227 – 2271Zinc 2; catalyticBy similarity
Metal bindingi284 – 2841Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi328 – 3281Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi377 – 3771Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi426 – 4261Calcium 4; via carbonyl oxygenBy similarity

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

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
Gene namesi
Name:MMP1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 1

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 – 1818Add
BLAST
Propeptidei19 – 9880Activation peptidePRO_0000028710Add
BLAST
Chaini99 – 468370Interstitial collagenasePRO_0000028711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)Curated
Modified residuei273 – 2731PhosphothreonineBy similarity
Disulfide bondi277 ↔ 465By similarity
Modified residuei359 – 3591Phosphotyrosine; by PKDCCBy similarity

Post-translational modificationi

Tyrosine phosphorylated in platelets by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015428.

Structurei

3D structure databases

ProteinModelPortaliP13943.
SMRiP13943. Positions 30-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati274 – 32350Hemopexin 1Add
BLAST
Repeati324 – 37047Hemopexin 2Add
BLAST
Repeati373 – 42149Hemopexin 3Add
BLAST
Repeati422 – 46544Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 968Cysteine 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.
InParanoidiP13943.
KOiK01388.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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.

P13943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGLPLLLLL LWGVGSHGFP AASETQEQDV EMVQKYLENY YNLKDDWRKI
60 70 80 90 100
PKQRGNGLAV EKLKQMQEFF GLKVTGKPDA ETLKMMKQPR CGVPDVAQFV
110 120 130 140 150
LTPGNPRWEQ THLTYRIENY TPDLSRADVD NAIEKAFQLW SNVTPLTFTK
160 170 180 190 200
VSKGQADIMI SFVRGDHRDN SPFDGPEGQL AHAFQPGLGI GGDVHFDEDD
210 220 230 240 250
RWTKDFRNYN LYRVAAHELG HSLGLSHSTD IGALMYPNYM FSGDVQLAQD
260 270 280 290 300
DIDGIQAIYG PSQNPSQPVG PQTPKVCDSK LTFDAITTIR GEIMFFKDRF
310 320 330 340 350
YMRANPYYSE VELNFISVFW PHLPNGLQAA YEVAHRDEIL FFKGNKYWTV
360 370 380 390 400
QGQNELPGYP KDIHSSFGFP RSVNHIDAAV SEEDTGKTYF FVANKYWRYD
410 420 430 440 450
EYKRSMDAGY PKMIEYDFPG IGNKVDAVFK KDGFFYFFHG TRQYKFDPKT
460
KRILTLQKAN SWFNCRKN
Length:468
Mass (Da):53,740
Last modified:January 1, 1990 - v1
Checksum:iDA90538919952B8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17823
, M17820, M17821, M17822, M19240 mRNA. Translation: AAB88016.1.
M25663 mRNA. Translation: AAA31203.1.
PIRiA27500. KCRBI.
RefSeqiNP_001164610.1. NM_001171139.2.
UniGeneiOcu.2695.

Genome annotation databases

EnsembliENSOCUT00000017958; ENSOCUP00000015428; ENSOCUG00000017958.
GeneIDi100009110.
KEGGiocu:100009110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17823
, M17820, M17821, M17822, M19240 mRNA. Translation: AAB88016.1.
M25663 mRNA. Translation: AAA31203.1.
PIRiA27500. KCRBI.
RefSeqiNP_001164610.1. NM_001171139.2.
UniGeneiOcu.2695.

3D structure databases

ProteinModelPortaliP13943.
SMRiP13943. Positions 30-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015428.

Protein family/group databases

MEROPSiM10.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000017958; ENSOCUP00000015428; ENSOCUG00000017958.
GeneIDi100009110.
KEGGiocu:100009110.

Organism-specific databases

CTDi4312.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP13943.
KOiK01388.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 449-468.
    Strain: New Zealand white.

Entry informationi

Entry nameiMMP1_RABIT
AccessioniPrimary (citable) accession number: P13943
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 8, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.