Q03700 (CARP4_RHINI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Rhizopuspepsin-4 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	398 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: 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 – 74	53	Activation peptide Potential		PRO_0000025889
	Chain	75 – 398	324	Rhizopuspepsin-4		PRO_0000025890
Regions
	Compositional bias	58 – 67	10	Poly-Ser
	Compositional bias	237 – 240	4	Poly-Gly
Sites
	Active site	108	1	By similarity
	Active site	291	1	By similarity
Amino acid modifications
	Disulfide bond	121 ↔ 124		By similarity
	Disulfide bond	325 ↔ 358		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03700 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 70CA63FEFB5C05D5	FASTA	398	41,409
	10 20 30 40 50 60 MKFTLISSCV ALACMALAVE AAPSGKKINV PLSKNANYKP NAKRAIEKAN AKYARFRSSS 70 80 90 100 110 120 SSSSSSSCGS AGTESSGSVP VTDDGNDIEY YGEVTVGTPG IKLKLDFDTG SSDLWFASTL 130 140 150 160 170 180 CTNCGSSQTK YDPSQSSTYA KDGRTWSISY GDGSSASGIL GKDTVNLGGL KIKNQIIELA 190 200 210 220 230 240 KREASSFSSG PSDGLLGLGF DSITTVSGVQ TPMDNLISQG LISNPVFGVY LGKESNGGGG 250 260 270 280 290 300 EYIFGGYDSS KFSGDLTTIA VDNSNGWYGI TIDGASISGS QVSDSFSAIL DTGTTLLILP 310 320 330 340 350 360 SNVASSVAQA YNANDNGDGT YNINCDTSEL QPLVFTIGGS TFEVPTDSLI FEQDGNTCVA 370 380 390 GFGYGQDDFA IFGDVFLKNN YVVFNPQVPQ VQIAPISN

References

[1]	Horiuchi H., Nakamura H., Okazaki T., Yano K., Takagi M. Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NBRC 4810 / AS 3.4817.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56992 Genomic DNA. Translation: CAA40309.1.
3D structure databases
ProteinModelPortal	Q03700.
SMR	Q03700. Positions 77-397.
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

CARP4_RHINI

Accession

Primary (citable) accession number: Q03700

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program