P46925 (PLM2_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Plasmepsin-2 EC=3.4.23.39 Alternative name(s): Aspartic hemoglobinase II PFAPD
Organism	Plasmodium falciparum
Taxonomic identifier	5833 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	453 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 the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr.
Subcellular location	Vacuole.
Developmental stage	Erythrocytic stages.
Sequence similarities	Belongs to the peptidase A1 family.
Caution	It is uncertain whether Met-1 or Met-51 is the initiator.
Sequence caution	The sequence AAA68217.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Vacuole
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	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 – ?

Potential

Propeptide

? – 124

Activation peptide

PRO_0000025930

Chain

125 – 453

329

Plasmepsin-2

PRO_0000025931

Sites

Active site

158

1

By similarity

Active site

338

1

By similarity

Amino acid modifications

Glycosylation

219

1

N-linked (GlcNAc...) Potential

Glycosylation

374

1

N-linked (GlcNAc...) Potential

Glycosylation

441

1

N-linked (GlcNAc...) Potential

Disulfide bond

171 ↔ 176

Disulfide bond

373 ↔ 409

Secondary structure

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453

Helix Strand Turn

Details...

Beta strand

80 – 87

8

Helix

89 – 99

11

Helix

103 – 113

11

Turn

114 – 116

3

Beta strand

118 – 120

3

Beta strand

127 – 135

9

Turn

136 – 138

3

Beta strand

139 – 146

8

Turn

147 – 150

4

Beta strand

151 – 158

8

Beta strand

164 – 168

5

Helix

176 – 178

3

Helix

184 – 186

3

Beta strand

191 – 200

10

Beta strand

202 – 217

16

Beta strand

220 – 231

12

Helix

233 – 235

3

Helix

238 – 241

4

Beta strand

246 – 249

4

Helix

253 – 255

3

Beta strand

256 – 258

3

Helix

263 – 269

7

Beta strand

272 – 275

4

Beta strand

277 – 281

5

Turn

285 – 287

3

Beta strand

290 – 296

7

Helix

299 – 301

3

Beta strand

302 – 313

12

Turn

314 – 317

4

Beta strand

318 – 325

8

Beta strand

328 – 337

10

Beta strand

343 – 346

4

Helix

348 – 354

7

Turn

355 – 357

3

Beta strand

358 – 362

5

Beta strand

364 – 366

3

Beta strand

369 – 372

4

Beta strand

381 – 384

4

Beta strand

389 – 392

4

Helix

394 – 397

4

Beta strand

398 – 400

3

Turn

402 – 404

3

Beta strand

408 – 411

4

Beta strand

413 – 415

3

Beta strand

422 – 425

4

Helix

427 – 432

6

Beta strand

433 – 438

6

Turn

439 – 442

4

Beta strand

443 – 449

7

Sequences

	Sequence		Length	Mass (Da)
	P46925 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 0D78A8A65D0C80B5	FASTA	453	51,490
	10 20 30 40 50 60 MDITVREHDF KHGFIKSNST FDGLNIDNSK NKKKIQKGFQ ILYVLLFCSV MCGLFYYVYE 70 80 90 100 110 120 NVWLQRDNEM NEILKNSEHL TIGFKVENAH DRILKTIKTH KLKNYIKESV NFLNSGLTKT 130 140 150 160 170 180 NYLGSSNDNI ELVDFQNIMF YGDAEVGDNQ QPFTFILDTG SANLWVPSVK CTTAGCLTKH 190 200 210 220 230 240 LYDSSKSRTY EKDGTKVEMN YVSGTVSGFF SKDLVTVGNL SLPYKFIEVI DTNGFEPTYT 250 260 270 280 290 300 ASTFDGILGL GWKDLSIGSV DPIVVELKNQ NKIENALFTF YLPVHDKHTG FLTIGGIEER 310 320 330 340 350 360 FYEGPLTYEK LNHDLYWQIT LDAHVGNIML EKANCIVDSG TSAITVPTDF LNKMLQNLDV 370 380 390 400 410 420 IKVPFLPFYV TLCNNSKLPT FEFTSENGKY TLEPEYYLQH IEDVGPGLCM LNIIGLDFPV 430 440 450 PTFILGDPFM RKYFTVFDYD NHSVGIALAK KNL

References

[1]	"Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum." Dame J.B., Reddy G.R., Yowell C.A., Dunn B.M., Kay J., Berry C. Mol. Biochem. Parasitol. 64:177-190(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, 3D-STRUCTURE MODELING. Strain: HB3.
[2]	"Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum." Silva A.M., Lee A.Y., Gulnik S.V., Maier P., Collins J., Bhat T.N., Collins P.J., Cachau R.E., Luker K.E., Gluzman I.Y., Francis S.E., Oksman A., Goldberg D.E., Erickson J.W. Proc. Natl. Acad. Sci. U.S.A. 93:10034-10039(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[3]	"Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum." Bernstein N.K., Cherney M.M., Loetscher H., Ridley R.G., James M.N. Nat. Struct. Biol. 6:32-37(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF ZYMOGEN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L10740 Genomic DNA. Translation: AAA68217.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J8J	model	-	A	125-453	[»]
1LEE	X-ray	1.90	A	123-453	[»]
1LF2	X-ray	1.80	A	123-453	[»]
1LF3	X-ray	2.70	A	123-453	[»]
1LF4	X-ray	1.90	A	123-453	[»]
1M43	X-ray	2.40	A/B	123-453	[»]
1ME6	X-ray	2.70	A/B	125-453	[»]
1PFZ	X-ray	1.85	A/B/C/D	77-453	[»]
1SME	X-ray	2.70	A/B	125-453	[»]
1W6H	X-ray	2.24	A/B	123-453	[»]
1W6I	X-ray	2.70	A/C	123-453	[»]
1XDH	X-ray	1.70	A/B	123-453	[»]
1XE5	X-ray	2.40	A/B	125-453	[»]
1XE6	X-ray	2.80	A/B	125-453	[»]
2BJU	X-ray	1.56	A	1-453	[»]
2BL3	model	-	A	125-453	[»]
2IGX	X-ray	1.70	A	125-453	[»]
2IGY	X-ray	2.60	A/B	125-453	[»]
2R9B	X-ray	2.80	A/B	125-453	[»]
3F9Q	X-ray	1.90	A	125-453	[»]

ProteinModelPortal

P46925.

ModBase

Search...

Protein family/group databases

MEROPS

A01.023.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

NOG248684.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15374.

Family and domain databases

Gene3D

2.40.70.10. 2 hits.

InterPro

IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
[Graphical view]

PANTHER

PTHR13683. PTHR13683. 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...

Other

BindingDB

P46925.

ChEMBL

CHEMBL4414.

EvolutionaryTrace

P46925.

Entry information

Entry name

PLM2_PLAFA

Accession

Primary (citable) accession number: P46925

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)