O04057 (ASPR_CUCPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Aspartic proteinase EC=3.4.23.-
Organism	Cucurbita pepo (Vegetable marrow) (Summer squash)
Taxonomic identifier	3663 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucurbiteae › Cucurbita

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles By similarity.
Subunit structure	Heterodimer of a 32 kDa subunit and a 16 kDa subunit.
Subcellular location	Vacuole By similarity.
Sequence similarities	Belongs to the peptidase A1 family. Contains 1 saposin B-type domain.

Ontologies

Keywords
Cellular component	Vacuole
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological_process	lipid metabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 24	24	Potential
	Propeptide	25 – 72	48	Activation peptide Potential		PRO_0000025901
	Chain	73 – 513	441	Aspartic proteinase		PRO_0000025902
Regions
	Domain	319 – 424	106	Saposin B-type
Sites
	Active site	108	1	By similarity
	Active site	294	1	By similarity
Amino acid modifications
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Glycosylation	404	1	N-linked (GlcNAc...) Potential
	Disulfide bond	120 ↔ 126		By similarity
	Disulfide bond	285 ↔ 289		By similarity
	Disulfide bond	324 ↔ 418		By similarity
	Disulfide bond	349 ↔ 390		By similarity
	Disulfide bond	355 ↔ 387		By similarity
	Disulfide bond	432 ↔ 469		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O04057 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 083FB7064CE02DC2	FASTA	513	55,856
	10 20 30 40 50 60 MASYHSKAAF LCLFLLVSFN IVSSASNDGL LRVGLKKIKL DPENRLAARV ESKDAEILKA 70 80 90 100 110 120 AFRKYNPKGN LGESSDTDIV ALKNYLDAQY YGEIAIGTPP QKFTVIFDTG SSNLWVLCEC 130 140 150 160 170 180 LFSVACHFHA RYKSSRSSSY KKNGTSASIR YGTGAVSGFF SYDNVKVGDL VVKEQVFIEA 190 200 210 220 230 240 TREPSLTFLV AKFDGLLGLG FQEIAVGNAV PVWYNMVEQG LVKEPVFSFW LNRNVEEEEG 250 260 270 280 290 300 GEIVFGGVDP KHYRGKHTYV PVTQKGYWQF DMGDVLIDGE PTGFCDGGCS AIADSGTSLL 310 320 330 340 350 360 AGPTPVITMI NHAIGAKGVV SQQCKAVVAQ YGQTIMDLLL SEADPKKICS QINLCTFDGT 370 380 390 400 410 420 RGVSMGIESV VDENAGKSSD SLHDGMCSVC EMTVVWMQNQ LRQNQTKERI INYINELCDR 430 440 450 460 470 480 MPSPMGQSAV DCGQLSSMPT VSFTIGGKIF DLAPEEYILK VGEGPVAQCI SGFTAFDIPP 490 500 510 PRGPLWILGD VFMGRYHTVF DFGKLRVGSA EAA

References

[1]	"An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles of plants." Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I. Eur. J. Biochem. 246:133-141(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB002695 mRNA. Translation: BAA19607.1.
PIR	T09739.
3D structure databases
ProteinModelPortal	O04057.
SMR	O04057. Positions 31-513.
ModBase	Search...
Protein family/group databases
MEROPS	A01.020.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.225.10. 2 hits. 2.40.70.10. 3 hits.
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR007856. SapB_1. IPR008138. SapB_2. IPR011001. Saposin-like. IPR008139. SaposinB. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 1 hit.
Pfam	PF00026. Asp. 1 hit. PF05184. SapB_1. 1 hit. PF03489. SapB_2. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SMART	SM00741. SapB. 1 hit. [Graphical view]
SUPFAM	SSF50630. Pept_Aspartic. 1 hit. SSF47862. Saposin_like. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. PS50015. SAP_B. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPR_CUCPE

Accession

Primary (citable) accession number: O04057

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program