COGS_LEPPG
ID COGS_LEPPG Reviewed; 226 AA.
AC P00771;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Brachyurin;
DE EC=3.4.21.32;
DE AltName: Full=Collagenolytic protease;
OS Leptuca pugilator (Atlantic sand fiddler crab) (Uca pugilator).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Ocypodoidea; Ocypodidae; Gelasiminae; Leptuca.
OX NCBI_TaxID=6772;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Hepatopancreas;
RX PubMed=6252953; DOI=10.1021/bi00561a018;
RA Grant G.A., Henderson K.O., Eisen A.Z., Bradshaw R.A.;
RT "Amino acid sequence of a collagenolytic protease from the hepatopancreas
RT of the fiddler crab, Uca pugilator.";
RL Biochemistry 19:4653-4659(1980).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SEQUENCE REVISION.
RC TISSUE=Hepatopancreas;
RX PubMed=9154920; DOI=10.1021/bi9617522;
RA Perona J.J., Tsu C.A., Craik C.S., Fletterick R.J.;
RT "Crystal structure of an ecotin-collagenase complex suggests a model for
RT recognition and cleavage of the collagen triple helix.";
RL Biochemistry 36:5381-5392(1997).
CC -!- FUNCTION: This enzyme is a serine protease capable of degrading the
CC native triple helix of collagen.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, with broad specificity for peptide
CC bonds. Native collagen is cleaved about 75% of the length of the
CC molecule from the N-terminus. Low activity on small molecule
CC substrates of both trypsin and chymotrypsin.; EC=3.4.21.32;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR PIR; A00958; KCUF.
DR PDB; 1AZZ; X-ray; 2.30 A; A/B=1-226.
DR PDBsum; 1AZZ; -.
DR AlphaFoldDB; P00771; -.
DR SMR; P00771; -.
DR MEROPS; S01.122; -.
DR EvolutionaryTrace; P00771; -.
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; Serine protease.
FT CHAIN 1..226
FT /note="Brachyurin"
FT /id="PRO_0000088664"
FT DOMAIN 1..223
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 41
FT /note="Charge relay system"
FT ACT_SITE 87
FT /note="Charge relay system"
FT ACT_SITE 178
FT /note="Charge relay system"
FT DISULFID 26..42
FT DISULFID 151..164
FT DISULFID 174..200
FT CONFLICT 91
FT /note="I -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..148
FT /note="SN -> NS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:1AZZ"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1AZZ"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1AZZ"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1AZZ"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1AZZ"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:1AZZ"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1AZZ"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1AZZ"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:1AZZ"
SQ SEQUENCE 226 AA; 23511 MW; E45591CAF332CE8C CRC64;
IVGGVEAVPN SWPHQAALFI DDMYFCGGSL ISPEWILTAA HCMDGAGFVD VVLGAHNIRE
DEATQVTIQS TDFTVHENYN SFVISNDIAV IRLPVPVTLT AAIATVGLPS TDVGVGTVVT
PTGWGLPSDS ALGISDVLRQ VDVPIMSNAD CDAVYGIVTD GNICIDSTGG KGTCNGDSGG
PLNYNGLTYG ITSFGAAAGC EAGYPDAFTR VTYFLDWIQT QTGITP
