TRAP_PLAFA
ID TRAP_PLAFA Reviewed; 559 AA.
AC P16893;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Thrombospondin-related anonymous protein;
DE Flags: Precursor;
GN Name=TRAP;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3045563; DOI=10.1038/335079a0;
RA Robson K.J.H., Hall J.R.S., Jennings M.W., Harris T.J.R., Marsh K.,
RA Newbold C.I., Tate V.E., Weatherall D.J.;
RT "A highly conserved amino-acid sequence in thrombospondin, properdin and in
RT proteins from sporozoites and blood stages of a human malaria parasite.";
RL Nature 335:79-82(1988).
RN [2]
RP STRUCTURE BY NMR OF 241-288, SUBCELLULAR LOCATION, HEPARIN-BINDING, AND
RP DISULFIDE BONDS.
RX PubMed=16815922; DOI=10.1110/ps.052068506;
RA Tossavainen H., Pihlajamaa T., Huttunen T.K., Raulo E., Rauvala H.,
RA Permi P., Kilpelainen I.;
RT "The layered fold of the TSR domain of P. falciparum TRAP contains a
RT heparin binding site.";
RL Protein Sci. 15:1760-1768(2006).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16815922};
CC Single-pass membrane protein {ECO:0000305|PubMed:16815922}.
CC -!- DEVELOPMENTAL STAGE: Expressed during erythrocytic stage of life cycle.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X13022; CAA31440.1; -; Genomic_DNA.
DR PIR; S04531; S04531.
DR PDB; 2BBX; NMR; -; A=242-288.
DR PDBsum; 2BBX; -.
DR AlphaFoldDB; P16893; -.
DR BMRB; P16893; -.
DR SMR; P16893; -.
DR PRIDE; P16893; -.
DR VEuPathDB; PlasmoDB:PF3D7_1335900; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000438600; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130040300; -.
DR VEuPathDB; PlasmoDB:PfCD01_130041500; -.
DR VEuPathDB; PlasmoDB:PfDd2_130041700; -.
DR VEuPathDB; PlasmoDB:PfGA01_130042000; -.
DR VEuPathDB; PlasmoDB:PfGB4_130041800; -.
DR VEuPathDB; PlasmoDB:PfGN01_130042600; -.
DR VEuPathDB; PlasmoDB:PfHB3_130042200; -.
DR VEuPathDB; PlasmoDB:PfIT_130041200; -.
DR VEuPathDB; PlasmoDB:PfKE01_130041500; -.
DR VEuPathDB; PlasmoDB:PfKH01_130039900; -.
DR VEuPathDB; PlasmoDB:PfKH02_130038800; -.
DR VEuPathDB; PlasmoDB:PfML01_130039800; -.
DR VEuPathDB; PlasmoDB:PfNF135_130040500; -.
DR VEuPathDB; PlasmoDB:PfNF166_130041100; -.
DR VEuPathDB; PlasmoDB:PfNF54_130040800; -.
DR VEuPathDB; PlasmoDB:PfSD01_130042600; -.
DR VEuPathDB; PlasmoDB:PfSN01_130038900; -.
DR VEuPathDB; PlasmoDB:PfTG01_130041600; -.
DR EvolutionaryTrace; P16893; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF00090; TSP_1; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Heparin-binding; Isopeptide bond; Malaria; Membrane; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..559
FT /note="Thrombospondin-related anonymous protein"
FT /id="PRO_0000024629"
FT TOPO_DOM 26..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..234
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 241..287
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 280..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..309
FT /note="Cell attachment site"
FT COMPBIAS 280..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 244..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16815922"
FT DISULFID 253..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16815922"
FT DISULFID 257..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16815922"
FT CROSSLNK 77
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in Factor 3(A))"
FT /evidence="ECO:0000255"
FT CROSSLNK 78
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in Factor 3(A))"
FT /evidence="ECO:0000255"
FT STRAND 254..265
FT /evidence="ECO:0007829|PDB:2BBX"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:2BBX"
SQ SEQUENCE 559 AA; 63300 MW; 02A20164D198C37A CRC64;
MNHLGNVKYL VIVFLIFFDL FLVNGRDVQN NIVDEIKYSE EVCNDQVDLY LLMDCSGSIR
RHNWVNHAVP LAMKLIQQLN LNDNAIHLYV NVFSNNAKEI IRLHSDASKN KEKALIIIRS
LLSTNLPYGR TNLTDALLQV RKHLNDRINR ENANQLVVIL TDGIPDSIQD SLKESRKLSD
RGVKIAVFGI GQGINVAFNR FLVGCHPSDG KCNLYADSAW ENVKNVIGPF MKAVCVEVEK
TASCGVWDEW SPCSVTCGKG TRSRKREILH EGCTSEIQEQ CEEERCPPKW EPLDVPDEPE
DDQPRPRGDN SSVQKPEENI IDNNPQEPSP NPEEGKDENP NGFDLDENPE NPPNPDIPEQ
KPNIPEDSEK EVPSDVPKNP EDDREENFDI PKKPENKHDN QNNLPNDKSD RNIPYSPLPP
KVLDNERKQS DPQSQDNNGN RHVPNSEDRE TRPHGRNNEN RSYNRKYNDT PKHPEREEHE
KPDNNKKKGE SDNKYKIAGG IAGGLALLAC AGLAYKFVVP GAATPYAGEP APFDETLGEE
DKDLDEPEQF RLPEENEWN
