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Protein

Collagenase

Gene
N/A
Organism
Hypoderma lineatum (Early cattle grub) (Common cattle grub)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.2 Publications

Catalytic activityi

Hydrolysis of proteins including native collagen at Xaa-|-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment.2 Publications

Enzyme regulationi

Inhibited by diisopropylfluorophosphate.1 Publication

pH dependencei

Optimum pH is 8.0-8.5. Reversibly inactivated below pH 4.5.1 Publication

Temperature dependencei

Thermostable. No loss of activity occurs after incubation for 2 hours at 60 degrees Celsius. Inactivated after incubation for 2 hours at 75 degrees Celsius, however 45% of activity remains after incubation for 20 minutes at 75 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751Charge relay system
Active sitei118 – 1181Charge relay system
Active sitei210 – 2101Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Collagen degradation

Enzyme and pathway databases

BRENDAi3.4.21.49. 2751.

Protein family/group databases

MEROPSiS01.121.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagenase (EC:3.4.21.49)
Alternative name(s):
Hypodermin C
Short name:
HC
OrganismiHypoderma lineatum (Early cattle grub) (Common cattle grub)
Taxonomic identifieri7389 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaOestroideaOestridaeHypodermatinaeHypoderma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Propeptidei17 – 30142 PublicationsPRO_0000027622Add
BLAST
Chaini31 – 260230CollagenasePRO_0000027623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 76
Disulfide bondi181 ↔ 196
Disulfide bondi206 ↔ 234

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Developmental stagei

Larval-specific.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 528Combined sources
Beta strandi57 – 6610Combined sources
Beta strandi69 – 724Combined sources
Helixi74 – 774Combined sources
Beta strandi80 – 889Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi102 – 1065Combined sources
Turni112 – 1154Combined sources
Beta strandi120 – 1234Combined sources
Helixi141 – 1455Combined sources
Beta strandi152 – 1598Combined sources
Beta strandi169 – 1768Combined sources
Helixi178 – 1825Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi213 – 2164Combined sources
Turni217 – 2204Combined sources
Beta strandi221 – 2288Combined sources
Beta strandi240 – 2445Combined sources
Helixi245 – 2484Combined sources
Helixi249 – 2568Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYLX-ray1.80A/B31-258[»]
2HLCX-ray1.70A/B31-258[»]
ProteinModelPortaliP08897.
SMRiP08897. Positions 31-260.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08897.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 257227Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08897-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLLVFALA LATTSAFQHP ASIFELREGR IINGYEAYTG LFPYQAGLDI
60 70 80 90 100
TLQDQRRVWC GGSLIDNKWI LTAAHCVHDA VSVVVYLGSA VQYEGEAVVN
110 120 130 140 150
SERIISHSMF NPDTYLNDVA LIKIPHVEYT DNIQPIRLPS GEELNNKFEN
160 170 180 190 200
IWATVSGWGQ SNTDTVILQY TYNLVIDNDR CAQEYPPGII VESTICGDTC
210 220 230 240 250
DGKSPCFGDS GGPFVLSDKN LLIGVVSFVS GAGCESGKPV GFSRVTSYMD
260
WIQQNTGIIF
Length:260
Mass (Da):28,579
Last modified:July 15, 1998 - v3
Checksum:iF8B1AF6350F2D74E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541D → E AA sequence (PubMed:6249306).Curated
Sequence conflicti56 – 572RR → QD AA sequence (PubMed:6249306).Curated
Sequence conflicti200 – 2001C → S in BAB20995 (PubMed:11470181).Curated
Sequence conflicti200 – 2001C → S AA sequence (PubMed:3034899).Curated
Sequence conflicti215 – 2162VL → SK AA sequence (PubMed:6303340).Curated
Sequence conflicti259 – 2591I → K AA sequence (PubMed:3034899).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74306 mRNA. Translation: CAA52359.1.
AB054066 mRNA. Translation: BAB20995.1.
PIRiA27802.

Genome annotation databases

KEGGiag:CAA52359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74306 mRNA. Translation: CAA52359.1.
AB054066 mRNA. Translation: BAB20995.1.
PIRiA27802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYLX-ray1.80A/B31-258[»]
2HLCX-ray1.70A/B31-258[»]
ProteinModelPortaliP08897.
SMRiP08897. Positions 31-260.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.121.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA52359.

Enzyme and pathway databases

BRENDAi3.4.21.49. 2751.

Miscellaneous databases

EvolutionaryTraceiP08897.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequencing and gene expression of hypodermins A, B, C in larval stages of Hypoderma lineatum."
    Moire N., Bigot Y., Periquet G., Boulard C.
    Mol. Biochem. Parasitol. 66:233-240(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Detection of antibodies to Hypoderma lineatum in cattle by Western blotting with recombinant hypodermin C antigen."
    Boldbaatar D., Xuan X., Kimbita E., Huang X., Igarashi I., Byambaa B., Battsetseg B., Battur B., Battsetseg G., Batsukh Z., Nagasawa H., Fujisaki K., Mikami T.
    Vet. Parasitol. 99:147-154(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum."
    Lecroisey A., Gilles A.-M., de Wolf A., Keil B.
    J. Biol. Chem. 262:7546-7551(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-260.
  4. "Sequential homology of the collagenase from eucaryote Hypoderma lineatum with the proteinases of the trypsin family."
    Lecroisey A., De Wolf A., Keil B.
    Biochem. Biophys. Res. Commun. 94:1261-1265(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-62.
    Tissue: Larva.
  5. "Structural study on the active site of the collagenase from Hypoderma lineatum."
    Lecroisey A., Keil B.
    Biochem. Biophys. Res. Commun. 112:907-910(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 204-216.
    Tissue: Larva.
  6. "Chemical and enzymatic characterization of the collagenase from the insect Hypoderma lineatum."
    Lecroisey A., Boulard C., Keil B.
    Eur. J. Biochem. 101:385-393(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  7. "Specificity of the collagenase from the insect Hypoderma lineatum."
    Lecroisey A., Keil B.
    Eur. J. Biochem. 152:123-130(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "1.8-A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family."
    Broutin I., Arnoux B., Riche C., Lecroisey A., Keil B., Pascard C., Ducruix A.
    Acta Crystallogr. D 52:380-392(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SEQUENCE REVISION TO 167-168.

Entry informationi

Entry nameiCOGS_HYPLI
AccessioniPrimary (citable) accession number: P08897
Secondary accession number(s): Q25083, Q9BPQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 15, 1998
Last modified: March 16, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.