PVDA_PLAKN
ID PVDA_PLAKN Reviewed; 1073 AA.
AC P22545;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Duffy receptor alpha form;
DE AltName: Full=Erythrocyte-binding protein;
DE Flags: Precursor;
OS Plasmodium knowlesi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1496004; DOI=10.1073/pnas.89.15.7085;
RA Adams J.H., Sim B.K., Dolan S.A., Fang X., Kaslow D.C., Miller L.H.;
RT "A family of erythrocyte binding proteins of malaria parasites.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7085-7089(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 296-1073.
RX PubMed=2170017; DOI=10.1016/0092-8674(90)90295-p;
RA Adams J.H., Hudson D.E., Torii M., Ward G.E., Wellems T.E., Aikawa M.,
RA Miller L.H.;
RT "The Duffy receptor family of Plasmodium knowlesi is located within the
RT micronemes of invasive malaria merozoites.";
RL Cell 63:141-153(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 200-536, AND DISULFIDE BONDS.
RX PubMed=16372020; DOI=10.1038/nature04443;
RA Singh S.K., Hora R., Belrhali H., Chitnis C.E., Sharma A.;
RT "Structural basis for Duffy recognition by the malaria parasite Duffy-
RT binding-like domain.";
RL Nature 439:741-744(2006).
CC -!- FUNCTION: Binds to the human erythrocytes Duffy blood group
CC determinant.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; M90466; AAA29602.1; -; Genomic_DNA.
DR EMBL; M68517; AAA29590.1; -; mRNA.
DR EMBL; M68518; AAA29591.1; -; Genomic_DNA.
DR PIR; A35970; A35970.
DR PDB; 5X6N; X-ray; 3.00 A; A=200-536.
DR PDBsum; 5X6N; -.
DR AlphaFoldDB; P22545; -.
DR SMR; P22545; -.
DR VEuPathDB; PlasmoDB:PKA1H_060029200; -.
DR VEuPathDB; PlasmoDB:PKNH_0623500; -.
DR VEuPathDB; PlasmoDB:PKNOH_S03338900; -.
DR eggNOG; ENOG502SZ6Z; Eukaryota.
DR EvolutionaryTrace; P22545; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR Gene3D; 1.10.1740.170; -; 1.
DR Gene3D; 1.20.1310.20; -; 1.
DR InterPro; IPR004258; DBL.
DR InterPro; IPR042202; Duffy-ag-bd_sf.
DR InterPro; IPR008602; Duffy-antigen-binding.
DR InterPro; IPR021032; Duffy-antigen-binding_N.
DR InterPro; IPR021620; EBA-175_C.
DR InterPro; IPR043057; EBA-175_C_sf.
DR Pfam; PF05424; Duffy_binding; 1.
DR Pfam; PF12377; DuffyBP_N; 1.
DR Pfam; PF11556; EBA-175_VI; 1.
DR Pfam; PF03011; PFEMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Malaria; Membrane; Receptor;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1073
FT /note="Duffy receptor alpha form"
FT /id="PRO_0000024618"
FT TOPO_DOM 22..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1029
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1030..1073
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 517..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..243
FT /evidence="ECO:0000269|PubMed:16372020"
FT DISULFID 227..234
FT /evidence="ECO:0000269|PubMed:16372020"
FT DISULFID 297..374
FT /evidence="ECO:0000269|PubMed:16372020"
FT DISULFID 412..429
FT /evidence="ECO:0000269|PubMed:16372020"
FT DISULFID 424..504
FT /evidence="ECO:0000269|PubMed:16372020"
FT DISULFID 433..502
FT /evidence="ECO:0000269|PubMed:16372020"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 263..287
FT /evidence="ECO:0007829|PDB:5X6N"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 294..312
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:5X6N"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:5X6N"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 385..410
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 420..425
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 427..460
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:5X6N"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 484..491
FT /evidence="ECO:0007829|PDB:5X6N"
FT HELIX 496..501
FT /evidence="ECO:0007829|PDB:5X6N"
SQ SEQUENCE 1073 AA; 120683 MW; 3965FC9F46B71808 CRC64;
MEGKKKRPLF FLLVLLLSHK ANNVLFERMN GILLLECENE YVKNENGYKL ATGHHYMDND
QIEQWLQGTD RSRRVKIEEN VKYKYNVEEL NTKYEQMKAP RINRILKEST YEAQNVADNN
YIDDKANGEH KTDNKTNKGE GARNMVMLDY DISGSGQPDG IIDNVVELGT EDEGNFLENS
SKGGDHPYRM NRKERMSNGV INQTFLQNNV MDKCNDKRKR GERDWDCPAE KDICISVRRY
QLCMKGLTNL VNNTRTHSHN DITFLKLNLK RKLMYDAAVE GDLLLKKNNY QYNKEFCKDI
RWGLGDFGDI IMGTNMEGIG YSQVVENNLR QVFGTDEKAK QDRKQWWNES KEHIWRAMMF
SIRSRLKEKF VWICKKDVTL KVEPQIYRWI REWGRDYMSK LPKEQGKLNE KCASKLYYNN
MAICMLPLCH DACKSYDQWI TRKKKQWDVL STKFSSVKKT QKIGTENIAT AYDILKQELN
GFKEATFENE INKRDNLYNH LCPCVVEEAR KNTQENVKNV GSGVESKAAS SNPITEAVKS
SSGEGKVQED SAHKSVNKGE GKSSTNEADP GSQSGAPASR SVDEKAGVPA LSAGQGHDKV
PPAEAAATES AVLHSADKTP NTVTEENKEG TQMDGAAGGD GKAPGPTVSS DVPSVGGKDS
GPSTSASHAL AGENGEVHNG TDTEPKEDGE KADPQKDIEV KGKQDTDDRS QGSLGPHTDE
RATLGETHME KDTETAGGST LTPEQNVSVA SDNGNVPGSG NKQNEGATAL SGAESLKSNE
SVHKTIDNTT HGLENKNGGN EKDFQKHDFM NNDMLNDQAS SDHTSSDQTS SDHTSSDQTS
SDHTSSDHTS SDQTSSDQTS SDQTIDTEGH HRDNVRNPEI KSSEDMSKGD FMRNSNSNEL
YSHNNLNNRK LNRDQYEHRD VKATREKIIL MSEVNKCNNR ASVKYCNTIE DRMLSSTCSR
ERRKNLCCSI SDFCLNYFEL YSYEFYNCMK KEFEDPSYEC FTKGSSTGIV YFATGGAFLI
ILLLFASWNA ASNDYEEEAT FDEFVEYSDD IHRTPLMPND IEHMQQFTPL DYS
