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Collagenase (EC 3.4.21.49) (Hypodermin C) (HC)

 COGS_HYPLI              Reviewed;         260 AA.
P08897; Q25083; Q9BPQ4;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
12-SEP-2018, entry version 102.
RecName: Full=Collagenase;
EC=3.4.21.49;
AltName: Full=Hypodermin C;
Short=HC;
Flags: Precursor;
Hypoderma lineatum (Early cattle grub) (Common cattle grub).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Oestroidea; Oestridae; Hypodermatinae; Hypoderma.
NCBI_TaxID=7389;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7808473; DOI=10.1016/0166-6851(94)90150-3;
Moire N., Bigot Y., Periquet G., Boulard C.;
"Sequencing and gene expression of hypodermins A, B, C in larval
stages of Hypoderma lineatum.";
Mol. Biochem. Parasitol. 66:233-240(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11470181; DOI=10.1016/S0304-4017(01)00457-5;
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.;
"Detection of antibodies to Hypoderma lineatum in cattle by Western
blotting with recombinant hypodermin C antigen.";
Vet. Parasitol. 99:147-154(2001).
[3]
PROTEIN SEQUENCE OF 31-260.
PubMed=3034899;
Lecroisey A., Gilles A.-M., de Wolf A., Keil B.;
"Complete amino acid sequence of the collagenase from the insect
Hypoderma lineatum.";
J. Biol. Chem. 262:7546-7551(1987).
[4]
PROTEIN SEQUENCE OF 31-62.
TISSUE=Larva;
PubMed=6249306; DOI=10.1016/0006-291X(80)90555-0;
Lecroisey A., De Wolf A., Keil B.;
"Sequential homology of the collagenase from eucaryote Hypoderma
lineatum with the proteinases of the trypsin family.";
Biochem. Biophys. Res. Commun. 94:1261-1265(1980).
[5]
PROTEIN SEQUENCE OF 204-216.
TISSUE=Larva;
PubMed=6303340; DOI=10.1016/0006-291X(83)91703-5;
Lecroisey A., Keil B.;
"Structural study on the active site of the collagenase from Hypoderma
lineatum.";
Biochem. Biophys. Res. Commun. 112:907-910(1983).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=230030; DOI=10.1111/j.1432-1033.1979.tb19730.x;
Lecroisey A., Boulard C., Keil B.;
"Chemical and enzymatic characterization of the collagenase from the
insect Hypoderma lineatum.";
Eur. J. Biochem. 101:385-393(1979).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2995028; DOI=10.1111/j.1432-1033.1985.tb09171.x;
Lecroisey A., Keil B.;
"Specificity of the collagenase from the insect Hypoderma lineatum.";
Eur. J. Biochem. 152:123-130(1985).
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SEQUENCE REVISION TO
167-168.
PubMed=15299709; DOI=10.1107/S090744499501184X;
Broutin I., Arnoux B., Riche C., Lecroisey A., Keil B., Pascard C.,
Ducruix A.;
"1.8-A structure of Hypoderma lineatum collagenase: a member of the
serine proteinase family.";
Acta Crystallogr. D 52:380-392(1996).
-!- FUNCTION: 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. {ECO:0000269|PubMed:230030,
ECO:0000269|PubMed:2995028}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins including native
collagen at Xaa-|-Ala bond leaving an N-terminal (75%) and a C-
terminal (25%) fragment. {ECO:0000269|PubMed:230030,
ECO:0000269|PubMed:2995028}.
-!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate.
{ECO:0000269|PubMed:230030}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0-8.5. Reversibly inactivated below pH 4.5.
{ECO:0000269|PubMed:2995028};
Temperature dependence:
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.
{ECO:0000269|PubMed:2995028};
-!- SUBCELLULAR LOCATION: Secreted.
-!- DEVELOPMENTAL STAGE: Larval-specific.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; X74306; CAA52359.1; -; mRNA.
EMBL; AB054066; BAB20995.1; -; mRNA.
PIR; A27802; A27802.
PDB; 1HYL; X-ray; 1.80 A; A/B=31-258.
PDB; 2HLC; X-ray; 1.70 A; A/B=31-258.
PDBsum; 1HYL; -.
PDBsum; 2HLC; -.
ProteinModelPortal; P08897; -.
SMR; P08897; -.
MEROPS; S01.121; -.
KEGG; ag:CAA52359; -.
KO; K20752; -.
BRENDA; 3.4.21.49; 2751.
EvolutionaryTrace; P08897; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Collagen degradation; Direct protein sequencing;
Disulfide bond; Hydrolase; Protease; Secreted; Serine protease;
Signal; Zymogen.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 30 {ECO:0000269|PubMed:3034899,
ECO:0000269|PubMed:6249306}.
/FTId=PRO_0000027622.
CHAIN 31 260 Collagenase.
/FTId=PRO_0000027623.
DOMAIN 31 257 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 75 75 Charge relay system.
ACT_SITE 118 118 Charge relay system.
ACT_SITE 210 210 Charge relay system.
DISULFID 60 76
DISULFID 181 196
DISULFID 206 234
CONFLICT 54 54 D -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 56 57 RR -> QD (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 200 200 C -> S (in Ref. 2; BAB20995 and 3; AA
sequence). {ECO:0000305}.
CONFLICT 215 216 VL -> SK (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 259 259 I -> K (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 45 52 {ECO:0000244|PDB:2HLC}.
STRAND 57 66 {ECO:0000244|PDB:2HLC}.
STRAND 69 72 {ECO:0000244|PDB:2HLC}.
HELIX 74 77 {ECO:0000244|PDB:2HLC}.
STRAND 80 88 {ECO:0000244|PDB:2HLC}.
STRAND 96 100 {ECO:0000244|PDB:2HLC}.
STRAND 102 106 {ECO:0000244|PDB:2HLC}.
TURN 112 115 {ECO:0000244|PDB:2HLC}.
STRAND 120 123 {ECO:0000244|PDB:2HLC}.
HELIX 141 145 {ECO:0000244|PDB:2HLC}.
STRAND 152 159 {ECO:0000244|PDB:2HLC}.
STRAND 169 176 {ECO:0000244|PDB:2HLC}.
HELIX 178 182 {ECO:0000244|PDB:2HLC}.
STRAND 194 197 {ECO:0000244|PDB:2HLC}.
STRAND 213 216 {ECO:0000244|PDB:2HLC}.
TURN 217 220 {ECO:0000244|PDB:2HLC}.
STRAND 221 228 {ECO:0000244|PDB:2HLC}.
STRAND 240 244 {ECO:0000244|PDB:2HLC}.
HELIX 245 248 {ECO:0000244|PDB:2HLC}.
HELIX 249 256 {ECO:0000244|PDB:2HLC}.
SEQUENCE 260 AA; 28579 MW; F8B1AF6350F2D74E CRC64;
MKFLLVFALA LATTSAFQHP ASIFELREGR IINGYEAYTG LFPYQAGLDI TLQDQRRVWC
GGSLIDNKWI LTAAHCVHDA VSVVVYLGSA VQYEGEAVVN SERIISHSMF NPDTYLNDVA
LIKIPHVEYT DNIQPIRLPS GEELNNKFEN IWATVSGWGQ SNTDTVILQY TYNLVIDNDR
CAQEYPPGII VESTICGDTC DGKSPCFGDS GGPFVLSDKN LLIGVVSFVS GAGCESGKPV
GFSRVTSYMD WIQQNTGIIF


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