Reviewed, UniProtKB/Swiss-Prot P06026 (CARP_RHICH)

Names and origin

Protein names	Recommended name:     Rhizopuspepsin     EC=3.4.23.21
Organism	Rhizopus chinensis (Bread mold)
Taxonomic identifier	4843 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus

Protein attributes

Sequence length	393 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 broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 68

47

Activation peptide Probable

PRO_0000025881

Chain

69 – 393

325

Rhizopuspepsin

PRO_0000025882

Sites

Active site

103

1

By similarity

Active site

286

1

By similarity

Amino acid modifications

Disulfide bond

116 ↔ 119

Disulfide bond

320 ↔ 353

Natural variations

Natural variant

83

1

V → I

Natural variant

129

1

K → N

Natural variant

184

1

N → S

Natural variant

230

1

S → K

Natural variant

298

1

V → I

Natural variant

309

1

S → Y

Natural variant

361

1

N → D

Natural variant

393

1

Q → E

Secondary structure

1

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393

Helix Strand Turn

Details...

Beta strand

73 – 79

7

Turn

80 – 83

4

Beta strand

84 – 91

8

Turn

92 – 95

4

Beta strand

96 – 103

8

Beta strand

110 – 113

4

Helix

128 – 130

3

Beta strand

135 – 144

10

Beta strand

150 – 162

13

Beta strand

165 – 178

14

Helix

180 – 183

4

Beta strand

188 – 192

5

Helix

196 – 198

3

Helix

207 – 213

7

Beta strand

218 – 226

9

Helix

229 – 231

3

Beta strand

235 – 239

5

Beta strand

252 – 255

4

Beta strand

264 – 272

9

Beta strand

275 – 285

11

Beta strand

290 – 295

6

Helix

296 – 306

11

Beta strand

312 – 314

3

Beta strand

316 – 318

3

Helix

322 – 324

3

Beta strand

328 – 332

5

Beta strand

335 – 339

5

Helix

341 – 344

4

Beta strand

345 – 349

5

Beta strand

352 – 361

10

Beta strand

363 – 367

5

Helix

369 – 372

4

Beta strand

375 – 380

6

Turn

381 – 384

4

Beta strand

385 – 391

7

Sequences

	Sequence		Length	Mass (Da)
	P06026-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 479BBDB3D001D25C	FASTA	393	41,327
	10 20 30 40 50 60 MKFTLISSCI AIAALAVAVD AAPGEKKISI PLAKNPNYKP SAKNAIQKAI AKYNKHKINT 70 80 90 100 110 120 STGGIVPDAG VGTVPMTDYG NDVEYYGQVT IGTPGKKFNL DFDTGSSDLW IASTLCTNCG 130 140 150 160 170 180 SRQTKYDPKQ SSTYQADGRT WSISYGDGSS ASGILAKDNV NLGGLLIKGQ TIELAKREAA 190 200 210 220 230 240 SFANGPNDGL LGLGFDTITT VRGVKTPMDN LISQGLISRP IFGVYLGKAS NGGGGEYIFG 250 260 270 280 290 300 GYDSTKFKGS LTTVPIDNSR GWWGITVDRA TVGTSTVASS FDGILDTGTT LLILPNNVAA 310 320 330 340 350 360 SVARAYGASD NGDGTYTISC DTSRFKPLVF SINGASFQVS PDSLVFEEYQ GQCIAGFGYG 370 380 390 NFDFAIIGDT FLKNNYVVFN QGVPEVQIAP VAQ

References

[1]	Gregoli P.A., Delaney R. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Amino acid sequence of rhizopuspepsin isozyme pI 5." Delaney R., Wong R.N.S., Meng G.-Z., Wu N.-H., Tang J. J. Biol. Chem. 262:1461-1467(1987) [PubMed: 3027093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-393.
[3]	"The amino acid sequence of rhizopuspepsin, an aspartic proteinase from Rhizopus chinensis." Takahashi K. J. Biol. Chem. 262:1468-1478(1987) [PubMed: 3100534] [Abstract] Cited for: PROTEIN SEQUENCE OF 69-393.
[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) OF 69-392.
[5]	"Structure and refinement at 1.8-A resolution of the aspartic proteinase from Rhizopus chinensis." Suguna K., Bott R.R., Padlan E.A., Subramanian E., Sheriff S., Cohen G.H., Davies D.R. J. Mol. Biol. 196:877-900(1987) [PubMed: 3316666] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 69-392.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L33859 Genomic DNA. Translation: AAB59306.1.
L33858 Genomic DNA. Translation: AAB59305.1.
J02651 mRNA. Translation: AAA33879.1.

PIR

A26681.
A41415.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UH7	X-ray	2.10	A	69-392	[»]
1UH8	X-ray	2.30	A	69-392	[»]
1UH9	X-ray	2.00	A	69-392	[»]
2APR	X-ray	1.80	A	69-392	[»]
3APR	X-ray	1.80	E	69-392	[»]
4APR	X-ray	2.50	E	69-392	[»]
5APR	X-ray	2.10	E	69-392	[»]
6APR	X-ray	2.50	E	69-392	[»]

ModBase

Search...

Protein family/group databases

MEROPS

A01.012.

Enzyme and pathway databases

BRENDA

3.4.23.21. 3608.

Family and domain databases

InterPro

IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[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]

ProtoNet

Search...

Entry information

Entry name

CARP_RHICH

Accession

Primary (citable) accession number: P06026

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)