P16893 (TRAP_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thrombospondin-related anonymous protein

Gene names

Name:

TRAP

Organism

Plasmodium falciparum

Taxonomic identifier

5833 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	559 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)

Subcellular location	Cell membrane; Single-pass membrane protein Probable Ref.2.
Developmental stage	Expressed during erythrocytic stage of life cycle.
Sequence similarities	Contains 1 TSP type-1 domain. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Disease	Malaria
Domain	Signal Transmembrane Transmembrane helix
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein Isopeptide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heparin binding 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 – 25

25

Potential

Chain

26 – 559

534

Thrombospondin-related anonymous protein

PRO_0000024629

Regions

Topological domain

26 – 496

471

Extracellular Potential

Transmembrane

497 – 515

19

Helical; Potential

Topological domain

516 – 559

44

Cytoplasmic Potential

Domain

48 – 234

187

VWFA

Domain

241 – 287

47

TSP type-1

Motif

307 – 309

3

Cell attachment site

Amino acid modifications

Glycosylation

132

1

N-linked (GlcNAc...) Potential

Glycosylation

310

1

N-linked (GlcNAc...) Potential

Glycosylation

460

1

N-linked (GlcNAc...) Potential

Glycosylation

468

1

N-linked (GlcNAc...) Potential

Disulfide bond

244 ↔ 273

Ref.2

Disulfide bond

253 ↔ 281

Ref.2

Disulfide bond

257 ↔ 286

Ref.2

Cross-link

77

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in Factor 3(A)) Potential

Cross-link

78

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in Factor 3(A)) Potential

Secondary structure

1

.

.

.

.

.

559

Helix Strand Turn

Details...

Beta strand

254 – 265

12

Beta strand

276 – 280

5

Sequences

	Sequence		Length	Mass (Da)
	P16893 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 02A20164D198C37A	FASTA	559	63,300
	10 20 30 40 50 60 MNHLGNVKYL VIVFLIFFDL FLVNGRDVQN NIVDEIKYSE EVCNDQVDLY LLMDCSGSIR 70 80 90 100 110 120 RHNWVNHAVP LAMKLIQQLN LNDNAIHLYV NVFSNNAKEI IRLHSDASKN KEKALIIIRS 130 140 150 160 170 180 LLSTNLPYGR TNLTDALLQV RKHLNDRINR ENANQLVVIL TDGIPDSIQD SLKESRKLSD 190 200 210 220 230 240 RGVKIAVFGI GQGINVAFNR FLVGCHPSDG KCNLYADSAW ENVKNVIGPF MKAVCVEVEK 250 260 270 280 290 300 TASCGVWDEW SPCSVTCGKG TRSRKREILH EGCTSEIQEQ CEEERCPPKW EPLDVPDEPE 310 320 330 340 350 360 DDQPRPRGDN SSVQKPEENI IDNNPQEPSP NPEEGKDENP NGFDLDENPE NPPNPDIPEQ 370 380 390 400 410 420 KPNIPEDSEK EVPSDVPKNP EDDREENFDI PKKPENKHDN QNNLPNDKSD RNIPYSPLPP 430 440 450 460 470 480 KVLDNERKQS DPQSQDNNGN RHVPNSEDRE TRPHGRNNEN RSYNRKYNDT PKHPEREEHE 490 500 510 520 530 540 KPDNNKKKGE SDNKYKIAGG IAGGLALLAC AGLAYKFVVP GAATPYAGEP APFDETLGEE 550 DKDLDEPEQF RLPEENEWN

References

[1]	"A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite." Robson K.J.H., Hall J.R.S., Jennings M.W., Harris T.J.R., Marsh K., Newbold C.I., Tate V.E., Weatherall D.J. Nature 335:79-82(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site." Tossavainen H., Pihlajamaa T., Huttunen T.K., Raulo E., Rauvala H., Permi P., Kilpelainen I. Protein Sci. 15:1760-1768(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 241-288, SUBCELLULAR LOCATION, HEPARIN-BINDING, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13022 Genomic DNA. Translation: CAA31440.1.

PIR

S04531.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BBX	NMR	-	A	242-288	[»]

ProteinModelPortal

P16893.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

NOG12793.

Family and domain databases

Gene3D

3.40.50.410. 1 hit.

InterPro

IPR000884. Thrombospondin_1_rpt.
IPR002035. VWF_A.
[Graphical view]

Pfam

PF00090. TSP_1. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]

SMART

SM00209. TSP1. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF82895. TSP1. 1 hit.

PROSITE

PS50092. TSP1. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P16893.

Entry information

Entry name

TRAP_PLAFA

Accession

Primary (citable) accession number: P16893

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)