PVDG_PLAKN
ID PVDG_PLAKN Reviewed; 1070 AA.
AC P50494;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Duffy receptor gamma 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).
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; M90695; AAA29604.1; -; Genomic_DNA.
DR AlphaFoldDB; P50494; -.
DR SMR; P50494; -.
DR PRIDE; P50494; -.
DR VEuPathDB; PlasmoDB:PKA1H_130061400; -.
DR VEuPathDB; PlasmoDB:PKNH_1356900; -.
DR VEuPathDB; PlasmoDB:PKNOH_S05400700; -.
DR eggNOG; ENOG502SZ6Z; Eukaryota.
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; IPR021015; Duffy-antigen-binding_C.
DR InterPro; IPR021032; Duffy-antigen-binding_N.
DR InterPro; IPR021620; EBA-175_C.
DR InterPro; IPR043057; EBA-175_C_sf.
DR Pfam; PF12361; DBP; 1.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Malaria; Membrane; Receptor; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1070
FT /note="Duffy receptor gamma form"
FT /id="PRO_0000024620"
FT TOPO_DOM 22..1003
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1004..1025
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1026..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 518..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 279..281
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 518..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..906
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 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..243
FT /evidence="ECO:0000250"
FT DISULFID 227..234
FT /evidence="ECO:0000250"
FT DISULFID 296..372
FT /evidence="ECO:0000250"
FT DISULFID 410..427
FT /evidence="ECO:0000250"
FT DISULFID 422..502
FT /evidence="ECO:0000250"
FT DISULFID 431..500
FT /evidence="ECO:0000250"
SQ SEQUENCE 1070 AA; 120931 MW; 703D68811BC11B50 CRC64;
MEGKKKRPLF FLLVLLLSHK ANNVLFERMN GILLLECENE YVKNENGYKL ATGHHYMDND
QIERWLQGTD RSRRVKIEEN VKYKYNVEEL NTKYEQMKGK RINRILKEST YEAQNVADNN
YIDDKANGEY KTDNKTNKGE GARNMVMLDY DISGSGQPDG IIDNVVELLT EDEGNFLKNS
SKGDDHPYRM KRKEKMSSGA INQIFLQNNV MDKCNDKRKR GERDWDCPTE KDVCIPDRRY
QLCMMEITNL VDTDTHFHSD IIFRKSYSRR RLIYDVGGRG DLLLKKYNNV YSEDLCKDIK
WSLQDFGDII MGTDMEGIGY SLVVQNNLRS IFGTGTSAEL DRKKWWNDHK KDIWKAMILS
VKEKNRYSAW NCKEDVQIKV EPQIYRWIRE WGRDYMSEFR EQRRKLNEKC EDKLYYSTML
ICTLPPCNNA CKSYDEWITG KKKQWDVLST KFSSVKKAQK IETENIARAY DILKQELNGF
NEVTFENEIN KRDKLYNYFC VCIVQEARKN TQENVKNVGS GVESKAPSSN PINEAVKSSS
GEGKVQEDSA HRSVNEGEGK SSTNEADPGS QPGGPASRSV DEKAGVPALS AGQGHDKVPP
AEAAATESAV PHSADKTPIT ATEENKQRTQ VDGVAGGDGK APGPTVSSDV PSVGGKDSGP
STPASHLAGE NGEVHNGTDT EPKEDGEKAD PQKNIEVKGK QDTDDRSQGS LGPHTDERAS
LGETHMEKDT ETTGGSTLTP EQNVSVASDN GNVPGSGNKQ NEGATALSGA ESLESSESVH
KTIDNTTHGL ENKNGGNEKD FQKHDFMNND MLNDQTSSDH TSSDQTSSDQ TSSDQTSSDQ
TSSDQTSSDQ TSSDQTSSDQ TIDTEGHHRD NVRNPEIKSS EDMSKGDFMR NSNSNELYSH
NNLNNRKLNR DQYEHRDVKA TREKIILMSE VNKCNNRTSL KYCNTIEDRM LSSTCSRERS
KNLCCSISDF CLNYFELYSY EFYNCMKKEF EDPSYECFTK GSSTGIVYFA TGGAFLIILL
LFASWNAASN DYEEEATFDE FEEYCYNIHR TPQMPNDIEH MQQFTPLDYS
