COGS_HYPLI
ID COGS_HYPLI Reviewed; 260 AA.
AC P08897; Q25083; Q9BPQ4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Collagenase;
DE EC=3.4.21.49;
DE AltName: Full=Hypodermin C;
DE Short=HC;
DE Flags: Precursor;
OS Hypoderma lineatum (Early cattle grub) (Common cattle grub).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Oestridae; Hypodermatinae; Hypoderma.
OX NCBI_TaxID=7389;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7808473; DOI=10.1016/0166-6851(94)90150-3;
RA Moire N., Bigot Y., Periquet G., Boulard C.;
RT "Sequencing and gene expression of hypodermins A, B, C in larval stages of
RT Hypoderma lineatum.";
RL Mol. Biochem. Parasitol. 66:233-240(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11470181; DOI=10.1016/s0304-4017(01)00457-5;
RA Boldbaatar D., Xuan X., Kimbita E., Huang X., Igarashi I., Byambaa B.,
RA Battsetseg B., Battur B., Battsetseg G., Batsukh Z., Nagasawa H.,
RA Fujisaki K., Mikami T.;
RT "Detection of antibodies to Hypoderma lineatum in cattle by Western
RT blotting with recombinant hypodermin C antigen.";
RL Vet. Parasitol. 99:147-154(2001).
RN [3]
RP PROTEIN SEQUENCE OF 31-260.
RX PubMed=3034899; DOI=10.1016/s0021-9258(18)47600-4;
RA Lecroisey A., Gilles A.-M., de Wolf A., Keil B.;
RT "Complete amino acid sequence of the collagenase from the insect Hypoderma
RT lineatum.";
RL J. Biol. Chem. 262:7546-7551(1987).
RN [4]
RP PROTEIN SEQUENCE OF 31-62.
RC TISSUE=Larva;
RX PubMed=6249306; DOI=10.1016/0006-291x(80)90555-0;
RA Lecroisey A., De Wolf A., Keil B.;
RT "Sequential homology of the collagenase from eucaryote Hypoderma lineatum
RT with the proteinases of the trypsin family.";
RL Biochem. Biophys. Res. Commun. 94:1261-1265(1980).
RN [5]
RP PROTEIN SEQUENCE OF 204-216.
RC TISSUE=Larva;
RX PubMed=6303340; DOI=10.1016/0006-291x(83)91703-5;
RA Lecroisey A., Keil B.;
RT "Structural study on the active site of the collagenase from Hypoderma
RT lineatum.";
RL Biochem. Biophys. Res. Commun. 112:907-910(1983).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=230030; DOI=10.1111/j.1432-1033.1979.tb19730.x;
RA Lecroisey A., Boulard C., Keil B.;
RT "Chemical and enzymatic characterization of the collagenase from the insect
RT Hypoderma lineatum.";
RL Eur. J. Biochem. 101:385-393(1979).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2995028; DOI=10.1111/j.1432-1033.1985.tb09171.x;
RA Lecroisey A., Keil B.;
RT "Specificity of the collagenase from the insect Hypoderma lineatum.";
RL Eur. J. Biochem. 152:123-130(1985).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SEQUENCE REVISION TO 167-168.
RX PubMed=15299709; DOI=10.1107/s090744499501184x;
RA Broutin I., Arnoux B., Riche C., Lecroisey A., Keil B., Pascard C.,
RA Ducruix A.;
RT "1.8-A structure of Hypoderma lineatum collagenase: a member of the serine
RT proteinase family.";
RL Acta Crystallogr. D 52:380-392(1996).
CC -!- FUNCTION: This enzyme is a serine protease capable of degrading the
CC native triple helix of collagen. Also cleaves the B chain of insulin at
CC the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but
CC not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl
CC phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl
CC myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-
CC cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.
CC {ECO:0000269|PubMed:230030, ECO:0000269|PubMed:2995028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins including native collagen at Xaa-|-Ala
CC bond leaving an N-terminal (75%) and a C-terminal (25%) fragment.;
CC EC=3.4.21.49; Evidence={ECO:0000269|PubMed:230030,
CC ECO:0000269|PubMed:2995028};
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate.
CC {ECO:0000269|PubMed:230030}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-8.5. Reversibly inactivated below pH 4.5.
CC {ECO:0000269|PubMed:2995028};
CC Temperature dependence:
CC Thermostable. No loss of activity occurs after incubation for 2 hours
CC at 60 degrees Celsius. Inactivated after incubation for 2 hours at 75
CC degrees Celsius, however 45% of activity remains after incubation for
CC 20 minutes at 75 degrees Celsius. {ECO:0000269|PubMed:2995028};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Larval-specific.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; X74306; CAA52359.1; -; mRNA.
DR EMBL; AB054066; BAB20995.1; -; mRNA.
DR PIR; A27802; A27802.
DR PDB; 1HYL; X-ray; 1.80 A; A/B=31-258.
DR PDB; 2HLC; X-ray; 1.70 A; A/B=31-258.
DR PDBsum; 1HYL; -.
DR PDBsum; 2HLC; -.
DR AlphaFoldDB; P08897; -.
DR SMR; P08897; -.
DR MEROPS; S01.121; -.
DR PRIDE; P08897; -.
DR KEGG; ag:CAA52359; -.
DR BRENDA; 3.4.21.49; 2751.
DR EvolutionaryTrace; P08897; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Collagen degradation; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..30
FT /evidence="ECO:0000269|PubMed:3034899,
FT ECO:0000269|PubMed:6249306"
FT /id="PRO_0000027622"
FT CHAIN 31..260
FT /note="Collagenase"
FT /id="PRO_0000027623"
FT DOMAIN 31..257
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 75
FT /note="Charge relay system"
FT ACT_SITE 118
FT /note="Charge relay system"
FT ACT_SITE 210
FT /note="Charge relay system"
FT DISULFID 60..76
FT DISULFID 181..196
FT DISULFID 206..234
FT CONFLICT 54
FT /note="D -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..57
FT /note="RR -> QD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="C -> S (in Ref. 2; BAB20995 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..216
FT /note="VL -> SK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="I -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2HLC"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2HLC"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2HLC"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2HLC"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2HLC"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:2HLC"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:2HLC"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2HLC"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2HLC"
SQ 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
