Reviewed, UniProtKB/Swiss-Prot P43231 (CARP2_RHINI)

Names and origin

Protein names	Recommended name:     Rhizopuspepsin-2     EC=3.4.23.21 Alternative name(s):     Aspartate protease
Organism	Rhizopus niveus
Taxonomic identifier	4844 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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
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 Potential		PRO_0000025885
	Chain	69 – 391	323	Rhizopuspepsin-2		PRO_0000025886
Sites
	Active site	102	1	By similarity
	Active site	285	1	By similarity
Amino acid modifications
	Disulfide bond	115 ↔ 118		By similarity
	Disulfide bond	319 ↔ 352		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43231-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 3F34230659DEA960	FASTA	391	41,234
	10 20 30 40 50 60 MKLTLISSCV ALAFMALATE AAPSGKKLSI PLTKNTNYKP SAKNAIQKAL AKYHRFRTTS 70 80 90 100 110 120 SSNSTSTEGT GSVPVTDYYN DIEYYGKVTV GTPGVTLKLD FDTGSSDLWF ASTLCTNCGS 130 140 150 160 170 180 SQTKYNPNQS STYAKDGRTW SISYGDGSSA SGILGTDTVT LGGLKITKQT IELAKREATS 190 200 210 220 230 240 FQSGPSYGLL GLGFDTITTV RGVKTPVDNL ISQGLISKPI FGVYLGKESN GGGGEYIFGG 250 260 270 280 290 300 YDSSKYSGSL TTIPVDNSNG WYGITIKGTT IGSSKVSSSF SAILDTGTTL LILPNNVASA 310 320 330 340 350 360 VARSYGASDN GDGTYTIDCD TSSFKPLVFS IGSSTFEVPA DSLVFEQDGS TCYAGFGYGD 370 380 390 YDFAIFGDVF LKNNYVVFNQ EVPEVQIAPI A

References

[1]	Horiuchi H., Nakamura H., Okazaki T., Yano K., Takagi M. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IFO 4810 / AS 3.4817.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56964 Genomic DNA. Translation: CAA40284.1.
3D structure databases
SMR	P43231. Positions 69-391.
ModBase	Search...
Protein family/group databases
MEROPS	A01.012.
Enzyme and pathway databases
BRENDA	3.4.23.21. 18853.
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

CARP2_RHINI

Accession

Primary (citable) accession number: P43231

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)