P00771 (COGS_UCAPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Brachyurin EC=3.4.21.32 Alternative name(s): Collagenolytic protease
Organism	Uca pugilator (Atlantic sand fiddler crab) (Celuca pugilator)
Taxonomic identifier	6772 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Brachyura › Eubrachyura › Ocypodoidea › Ocypodidae › Ocypodinae › Uca complex › Celuca

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme is a serine protease capable of degrading the native triple helix of collagen.
Catalytic activity	Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Collagen degradation
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 226

226

Brachyurin

PRO_0000088664

Regions

Domain

1 – 223

223

Peptidase S1

Sites

Active site

41

1

Charge relay system

Active site

87

1

Charge relay system

Active site

178

1

Charge relay system

Amino acid modifications

Disulfide bond

26 ↔ 42

Disulfide bond

151 ↔ 164

Disulfide bond

174 ↔ 200

Experimental info

Sequence conflict

91

1

I → V AA sequence Ref.1

Sequence conflict

147 – 148

2

SN → NS AA sequence Ref.1

Sequence conflict

175

1

N → D AA sequence Ref.1

Sequence conflict

185

1

N → D AA sequence Ref.1

Secondary structure

1

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226

Helix Strand Turn

Details...

Beta strand

15 – 20

6

Turn

21 – 23

3

Beta strand

24 – 32

9

Beta strand

35 – 38

4

Helix

40 – 43

4

Beta strand

49 – 54

6

Beta strand

56 – 60

5

Beta strand

66 – 70

5

Beta strand

73 – 75

3

Turn

81 – 84

4

Beta strand

89 – 92

4

Beta strand

101 – 103

3

Beta strand

118 – 125

8

Beta strand

132 – 134

3

Beta strand

143 – 146

4

Helix

148 – 155

8

Beta strand

162 – 165

4

Turn

168 – 170

3

Beta strand

181 – 184

4

Beta strand

187 – 196

10

Beta strand

206 – 211

6

Helix

212 – 214

3

Helix

215 – 222

8

Sequences

	Sequence		Length	Mass (Da)
	P00771 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: E45591CAF332CE8C	FASTA	226	23,511
	10 20 30 40 50 60 IVGGVEAVPN SWPHQAALFI DDMYFCGGSL ISPEWILTAA HCMDGAGFVD VVLGAHNIRE 70 80 90 100 110 120 DEATQVTIQS TDFTVHENYN SFVISNDIAV IRLPVPVTLT AAIATVGLPS TDVGVGTVVT 130 140 150 160 170 180 PTGWGLPSDS ALGISDVLRQ VDVPIMSNAD CDAVYGIVTD GNICIDSTGG KGTCNGDSGG 190 200 210 220 PLNYNGLTYG ITSFGAAAGC EAGYPDAFTR VTYFLDWIQT QTGITP

References

[1]	"Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator." Grant G.A., Henderson K.O., Eisen A.Z., Bradshaw R.A. Biochemistry 19:4653-4659(1980) [PubMed: 6252953] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Hepatopancreas.
[2]	"Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix." Perona J.J., Tsu C.A., Craik C.S., Fletterick R.J. Biochemistry 36:5381-5392(1997) [PubMed: 9154920] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SEQUENCE REVISION. Tissue: Hepatopancreas.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

KCUF. A00958.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZZ	X-ray	2.30	A/B	1-226	[»]

ProteinModelPortal

P00771.

SMR

P00771. Positions 1-226.

ModBase

Search...

Protein family/group databases

MEROPS

S01.122.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

COGS_UCAPU

Accession

Primary (citable) accession number: P00771

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 15, 1998
Last modified:	November 16, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)