P10602 (CARP1_RHINI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rhizopuspepsin-1
EC=3.4.23.21

Alternative name(s):
Aspartate protease

Gene names

Name:

RNAP

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	389 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	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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 – 66	45	Activation peptide		PRO_0000025883
	Chain	67 – 389	323	Rhizopuspepsin-1		PRO_0000025884
Sites
	Active site	100	1	By similarity
	Active site	283	1	By similarity
Amino acid modifications
	Disulfide bond	113 ↔ 116		By similarity
	Disulfide bond	317 ↔ 350		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10602 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: AFEC0AA3903DBFB2	FASTA	389	40,802
	10 20 30 40 50 60 MKFTLISSCV ALAAMTLAVE AAPNGKKINI PLAKNNSYKP SAKNALNKAL AKYNRRKVGS 70 80 90 100 110 120 GGITTEASGS VPMVDYENDV EYYGEVTVGT PGIKLKLDFD TGSSDMWFAS TLCSSCSNSH 130 140 150 160 170 180 TKYDPKKSST YAADGRTWSI SYGDGSSASG ILATDNVNLG GLLIKKQTIE LAKRESSAFA 190 200 210 220 230 240 TDVIDGLLGL GFNTITTVRG VKTPVDNLIS QGLISRPIFG VYLGKQSNGG GGEYIFGGYD 250 260 270 280 290 300 SSKFKGSLTT VPIDNSEGFW GVTVKSTKIG GTTVSASFDA ILDTGTTLLL LPDDVAAKVA 310 320 330 340 350 360 RSYGASDNGD GTYSITCDTS KLQPLVFTLG SSTFEVPSDS LIFEKDGNKC IAGFAAGGDL 370 380 AILGDVFLKN NYVVFNQEVP EVQIAPVAN

References

[1]	"Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus." Horiuchi H., Yanai K., Okazaki T., Takagi M., Yano K. J. Bacteriol. 170:272-278(1988) [PubMed: 3275615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: NBRC 4810 / AS 3.4817.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19100 Genomic DNA. Translation: AAA33882.1.
PIR	A28672.
3D structure databases
ProteinModelPortal	P10602.
SMR	P10602. Positions 69-388.
ModBase	Search...
Protein family/group databases
MEROPS	A01.012.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARP1_RHINI

Accession

Primary (citable) accession number: P10602

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program