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Protein

Interstitial collagenase B

Gene

Mmp1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Zinc 2; in inhibited formBy similarity
Metal bindingi155 – 1551Calcium 2By similarity
Metal bindingi165 – 1651Zinc 1By similarity
Metal bindingi167 – 1671Zinc 1By similarity
Metal bindingi172 – 1721Calcium 3By similarity
Metal bindingi173 – 1731Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi180 – 1801Zinc 1By similarity
Metal bindingi187 – 1871Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi189 – 1891Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi193 – 1931Zinc 1By similarity
Metal bindingi195 – 1951Calcium 3By similarity
Metal bindingi215 – 2151Zinc 2; catalyticBy similarity
Active sitei216 – 2161PROSITE-ProRule annotation
Metal bindingi219 – 2191Zinc 2; catalyticBy similarity
Metal bindingi225 – 2251Zinc 2; catalyticBy similarity
Metal bindingi282 – 2821Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi375 – 3751Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi424 – 4241Calcium 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

MEROPSiM10.034.

Names & Taxonomyi

Protein namesi
Recommended name:
Interstitial collagenase B (EC:3.4.24.7)
Alternative name(s):
Matrix metalloproteinase-1b
Short name:
MMP-1b
Mcol-B
Gene namesi
Name:Mmp1b
Synonyms:McolB
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1933847. Mmp1b.

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 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 9679Activation peptideBy similarityPRO_0000042647Add
BLAST
Chaini97 – 463367Interstitial collagenase BPRO_0000042648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi275 ↔ 463By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9EPL6.
PRIDEiQ9EPL6.

PTM databases

PhosphoSiteiQ9EPL6.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047261.

Structurei

3D structure databases

ProteinModelPortaliQ9EPL6.
SMRiQ9EPL6. Positions 29-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati278 – 32144Hemopexin 1Add
BLAST
Repeati322 – 36847Hemopexin 2Add
BLAST
Repeati371 – 41949Hemopexin 3Add
BLAST
Repeati420 – 46344Hemopexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 273179MetalloproteaseBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi87 – 948Cysteine 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.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9EPL6.
PhylomeDBiQ9EPL6.

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. 2 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.

Q9EPL6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSLPLLLRL WAASSYSFPV IQDGLQKNVK TVWKYLENYY NLGKNMQAKN
60 70 80 90 100
VNGKEVMAEK LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT
110 120 130 140 150
HNNPRWTKTH LTYSILNYTP YLSKAVVEDA IARAFRVWSD VTPLTFQRVF
160 170 180 190 200
EEEGDIVLSF HRGDHGDLYT FDGSKYHFAH AFLPGLGLGG NVHYDLDQKW
210 220 230 240 250
TDNNEDFNLF YVTAHELGHS LGLSHSNDEE ALMFPSYTWS NKDFVLNQDD
260 270 280 290 300
INRIQALYGP SPNPIQLTDA TLDPCNSGLT FDAIITYRGE VIFFKDRFYI
310 320 330 340 350
RVISFLPEPL IDVIDLTWPN LPGKFDAAYE VSGVDELRFF KGSKVWAVQE
360 370 380 390 400
QNVLEGFPMD IQSFFGFPSN VTNIDAAVCE EETGKTYFFV DHMYWRYDEN
410 420 430 440 450
TRSMDPGYPR LIAEDFPGID YKVDDVIQKE DNFYFFHQSI QYRFNLKTRR
460
IDDSSDINTW FNC
Length:463
Mass (Da):53,492
Last modified:March 1, 2001 - v1
Checksum:i46013AB9D106C3F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278461 mRNA. Translation: CAC18879.1.
CCDSiCCDS22805.1.
UniGeneiMm.379271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278461 mRNA. Translation: CAC18879.1.
CCDSiCCDS22805.1.
UniGeneiMm.379271.

3D structure databases

ProteinModelPortaliQ9EPL6.
SMRiQ9EPL6. Positions 29-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047261.

Protein family/group databases

MEROPSiM10.034.

PTM databases

PhosphoSiteiQ9EPL6.

Proteomic databases

PaxDbiQ9EPL6.
PRIDEiQ9EPL6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1933847. Mmp1b.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9EPL6.
PhylomeDBiQ9EPL6.

Miscellaneous databases

PROiQ9EPL6.
SOURCEiSearch...

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. 2 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 nameiMMP1B_MOUSE
AccessioniPrimary (citable) accession number: Q9EPL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 98 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.