Reviewed, UniProtKB/Swiss-Prot P11838 (CARP_CRYPA)

Names and origin

Protein names

Recommended name:
    Endothiapepsin
    EC=3.4.23.22
Alternative name(s):
    Aspartate protease

Gene names

Name:	EAPA
Synonyms:	EPN-1

Organism

Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)

Taxonomic identifier

5116 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Diaporthales › Cryphonectriaceae › Cryphonectria-Endothia complex › Cryphonectria

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 20

20

Potential

Propeptide

21 – 89

69

Activation peptide

Chain

90 – 419

330

Endothiapepsin

Sites

Active site

124

1

Active site

288

1

Amino acid modifications

Disulfide bond

344 ↔ 379

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

419

Helix Strand Turn

Details...

Beta strand

92 – 100

9

Beta strand

106 – 112

7

Turn

113 – 116

4

Beta strand

117 – 124

8

Beta strand

130 – 132

3

Helix

139 – 141

3

Helix

150 – 152

3

Beta strand

157 – 167

11

Beta strand

173 – 185

13

Beta strand

188 – 201

14

Helix

203 – 207

5

Beta strand

213 – 216

4

Helix

220 – 222

3

Beta strand

226 – 228

3

Helix

233 – 237

5

Turn

238 – 240

3

Beta strand

241 – 249

9

Beta strand

252 – 254

3

Beta strand

256 – 261

6

Beta strand

267 – 270

4

Beta strand

273 – 276

4

Beta strand

285 – 293

9

Beta strand

299 – 307

9

Beta strand

313 – 316

4

Helix

318 – 325

8

Beta strand

332 – 334

3

Turn

335 – 338

4

Beta strand

339 – 343

5

Beta strand

351 – 355

5

Beta strand

358 – 362

5

Helix

364 – 367

4

Beta strand

368 – 373

6

Beta strand

377 – 386

10

Turn

387 – 389

3

Beta strand

390 – 394

5

Helix

396 – 399

4

Beta strand

402 – 407

6

Beta strand

409 – 411

3

Beta strand

413 – 418

6

Sequences

	Sequence		Length	Mass (Da)
	P11838-1 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 262D13F1D2F13296	FASTA	419	43,255
	10 20 30 40 50 60 MSSPLKNALV TAMLAGGALS SPTKQHVGIP VNASPEVGPG KYSFKQVRNP NYKFNGPLSV 70 80 90 100 110 120 KKTYLKYGVP IPAWLEDAVQ NSTSGLAERS TGSATTTPID SLDDAYITPV QIGTPAQTLN 130 140 150 160 170 180 LDFDTGSSDL WVFSSETTAS EVDGQTIYTP SKSTTAKLLS GATWSISYGD GSSSSGDVYT 190 200 210 220 230 240 DTVSVGGLTV TGQAVESAKK VSSSFTEDST IDGLLGLAFS TLNTVSPTQQ KTFFDNAKAS 250 260 270 280 290 300 LDSPVFTADL GYHAPGTYNF GFIDTTAYTG SITYTAVSTK QGFWEWTSTG YAVGSGTFKS 310 320 330 340 350 360 TSIDGIADTG TTLLYLPATV VSAYWAQVSG AKSSSSVGGY VFPCSATLPS FTFGVGSARI 370 380 390 400 410 VIPGDYIDFG PISTGSSSCF GGIQSSAGIG INIFGDVALK AAFVVFNGAT TPTLGFASK

References

[1]	"Cloning and mutation of the gene encoding endothiapepsin from Cryphonectria parasitica." Razanamparany V., Jara P., Legoux R., Delmas P., Msayeh F., Kaghad M., Loison G. Curr. Genet. 21:455-461(1992) [PubMed: 1617734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular analysis and overexpression of the gene encoding endothiapepsin, an aspartic protease from Cryphonectria parasitica." Choi G.H., Pawlyk D.M., Rae B., Shapira R., Nuss D.L. Gene 125:135-141(1993) [PubMed: 8462868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38755 / EP155.
[3]	"Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica." Barkholt V. Eur. J. Biochem. 167:327-338(1987) [PubMed: 3305016] [Abstract] Cited for: PROTEIN SEQUENCE OF 90-419.
[4]	"Homology among acid proteases: comparison of crystal structures at 3-A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica." Subramanian E., Swan I.D.A., Liu M., Davies D.R., Jenkins J.A., Tickle I.J., Blundell T.L. Proc. Natl. Acad. Sci. U.S.A. 74:556-559(1977) [PubMed: 322132] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[5]	"X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1-A resolution of endothiapepsin." Blundell T.L., Jenkins J.A., Sewell B.T., Pearl L.H., Cooper J.B., Tickle I.J., Veerapandian B., Wood S.P. J. Mol. Biol. 211:919-941(1990) [PubMed: 2179568] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]	"High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme." Sali A., Veerapandian B., Cooper J.B., Foundling S.I., Hoover D.J., Blundell T.L. EMBO J. 8:2179-2188(1989) [PubMed: 2676515] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X63351 Genomic DNA. Translation: CAA44952.1.
X53997 Genomic DNA. Translation: CAA37944.1.

PIR

S22136.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E5O	X-ray	2.05	E	90-419	[»]
1E80	X-ray	2.05	E	90-419	[»]
1E81	X-ray	2.05	E	90-419	[»]
1E82	X-ray	2.05	E	90-419	[»]
1EED	X-ray	2.00	P	90-419	[»]
1ENT	X-ray	1.90	E	90-419	[»]
1EPL	X-ray	2.00	E	90-419	[»]
1EPM	X-ray	1.60	E	90-419	[»]
1EPN	X-ray	1.60	E	90-419	[»]
1EPO	X-ray	2.00	E	90-419	[»]
1EPP	X-ray	1.90	E	90-419	[»]
1EPQ	X-ray	1.90	E	90-419	[»]
1EPR	X-ray	2.30	E	90-419	[»]
1ER8	X-ray	2.00	E	90-419	[»]
1GKT	neutron diffraction	2.10	A	90-419	[»]
1GVT	X-ray	0.98	A	90-419	[»]
1GVU	X-ray	0.94	A	90-419	[»]
1GVV	X-ray	1.05	A	90-419	[»]
1GVW	X-ray	1.00	A	90-419	[»]
1GVX	X-ray	1.00	A	90-419	[»]
1OD1	X-ray	1.37	A	90-419	[»]
1OEW	X-ray	0.90	A	90-419	[»]
1OEX	X-ray	1.10	A	90-419	[»]
2ER0	X-ray	3.00	E	90-419	[»]
2ER6	X-ray	2.00	E	90-419	[»]
2ER7	X-ray	1.60	E	90-419	[»]
2ER9	X-ray	2.20	E	90-419	[»]
2JJI	X-ray	1.57	A	90-419	[»]
2JJJ	X-ray	1.00	A	90-419	[»]
2V00	X-ray	1.55	A	90-419	[»]
2VS2	neutron diffraction	2.00	A	90-419	[»]
3ER3	X-ray	2.00	E	90-419	[»]
3ER5	X-ray	1.80	E	90-419	[»]
4APE	X-ray	2.10	A	90-419	[»]
4ER1	X-ray	2.00	E	90-419	[»]
4ER2	X-ray	2.00	E	90-419	[»]
4ER4	X-ray	2.10	E	90-419	[»]
5ER1	X-ray	2.00	E	90-419	[»]
5ER2	X-ray	1.80	E	90-419	[»]

ModBase

Search...

Protein family/group databases

MEROPS

A01.017.

Family and domain databases

InterPro

IPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
[Graphical view]

Gene3D

G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.

PANTHER

PTHR13683. Peptidase_A1. 1 hit.

Pfam

PF00026. Asp. 1 hit.
[Graphical view]

PRINTS

PR00792. PEPSIN.

PROSITE

PS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

BLOCKS

Search...

Other Resources

LinkHub

P11838.

ProtoNet

Search...

Entry information

Entry name

CARP_CRYPA

Accession

Primary (citable) accession number: P11838

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1993
Last modified:	October 14, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)