PVDR_PLAVS
ID PVDR_PLAVS Reviewed; 1070 AA.
AC P22290;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Duffy receptor;
DE AltName: Full=Erythrocyte-binding protein;
DE Flags: Precursor;
GN Name=PVDR;
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1849231; DOI=10.1016/0166-6851(91)90228-x;
RA Fang X., Kaslow D.C., Adams J.H., Miller L.H.;
RT "Cloning of the Plasmodium vivax Duffy receptor.";
RL Mol. Biochem. Parasitol. 44:125-132(1991).
CC -!- FUNCTION: Binds to the human erythrocytes Duffy blood group
CC determinant.
CC -!- INTERACTION:
CC P22290; P22290: PVDR; NbExp=2; IntAct=EBI-15935953, EBI-15935953;
CC P22290; Q16570-1: ACKR1; Xeno; NbExp=3; IntAct=EBI-15935953, EBI-15935975;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; M61095; AAA63423.1; -; Genomic_DNA.
DR PIR; T30848; T30848.
DR RefSeq; XP_001608387.1; XM_001608337.1.
DR PDB; 3RRC; X-ray; 1.95 A; A/B=211-525.
DR PDB; 4NUU; X-ray; 1.95 A; A/B=211-525.
DR PDB; 4NUV; X-ray; 2.60 A; A/B=211-525.
DR PDB; 4YFS; X-ray; 2.10 A; A=198-521.
DR PDB; 5F3J; X-ray; 4.00 A; A/B=211-525.
DR PDB; 6OAN; X-ray; 2.90 A; A/C=211-525.
DR PDB; 6OAO; X-ray; 3.50 A; A/C/E/G/I/K=211-525.
DR PDB; 6R2S; X-ray; 3.04 A; C=211-508.
DR PDBsum; 3RRC; -.
DR PDBsum; 4NUU; -.
DR PDBsum; 4NUV; -.
DR PDBsum; 4YFS; -.
DR PDBsum; 5F3J; -.
DR PDBsum; 6OAN; -.
DR PDBsum; 6OAO; -.
DR PDBsum; 6R2S; -.
DR AlphaFoldDB; P22290; -.
DR SMR; P22290; -.
DR DIP; DIP-59099N; -.
DR IntAct; P22290; 1.
DR STRING; 5855.PVX_110810; -.
DR ABCD; P22290; 26 sequenced antibodies.
DR GeneID; 5471431; -.
DR KEGG; pvx:PVX_110810; -.
DR VEuPathDB; PlasmoDB:PVX_110810; -.
DR OMA; RICPKEE; -.
DR PhylomeDB; P22290; -.
DR EvolutionaryTrace; P22290; -.
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 GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Malaria; Membrane; Receptor;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1070
FT /note="Duffy receptor"
FT /id="PRO_0000024621"
FT TOPO_DOM 21..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1025
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1026..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 116..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 217..246
FT /evidence="ECO:0000250"
FT DISULFID 230..237
FT /evidence="ECO:0000250"
FT DISULFID 300..377
FT /evidence="ECO:0000250"
FT DISULFID 415..432
FT /evidence="ECO:0000250"
FT DISULFID 427..507
FT /evidence="ECO:0000250"
FT DISULFID 436..505
FT /evidence="ECO:0000250"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3RRC"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3RRC"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6R2S"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:6R2S"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:3RRC"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 297..315
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:3RRC"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4NUV"
FT HELIX 342..361
FT /evidence="ECO:0007829|PDB:3RRC"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 388..415
FT /evidence="ECO:0007829|PDB:3RRC"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 430..464
FT /evidence="ECO:0007829|PDB:3RRC"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:6OAO"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:3RRC"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:4NUU"
FT HELIX 487..494
FT /evidence="ECO:0007829|PDB:3RRC"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:3RRC"
SQ SEQUENCE 1070 AA; 119683 MW; CB051DF13E294603 CRC64;
MKGKNRSLFV LLVLLLLHKV NNVLLERTIE TLLECKNEYV KGENGYKLAK GHHCVEEDNL
ERWLQGTNER RSEENIKYKY GVTELKIKYA QMNGKRSSRI LKESIYGAHN FGGNSYMEGK
DGGDKTGEEK DGEHKTDSKT DNGKGANNLV MLDYETSSNG QPAGTLDNVL EFVTGHEGNS
RKNSSNGGNP YDIDHKKTIS SAIINHAFLQ NTVMKNCNYK RKRRERDWDC NTKKDVCIPD
RRYQLCMKEL TNLVNNTDTN FHRDITFRKL YLKRKLIYDA AVEGDLLLKL NNYRYNKDFC
KDIRWSLGDF GDIIMGTDME GIGYSKVVEN NLRSIFGTDE KAQQRRKQWW NESKAQIWTA
MMYSVKKRLK GNFIWICKLN VAVNIEPQIY RWIREWGRDY VSELPTEVQK LKEKCDGKIN
YTDKKVCKVP PCQNACKSYD QWITRKKNQW DVLSNKFISV KNAEKVQTAG IVTPYDILKQ
ELDEFNEVAF ENEINKRDGA YIELCVCSVE EAKKNTQEVV TNVDNAAKSQ ATNSNPISQP
VDSSKAEKVP GDSTHGNVNS GQDSSTTGKA VTGDGQNGNQ TPAESDVQRS DIAESVSAKN
VDPQKSVSKR SDDTASVTGI AEAGKENLGA SNSRPSESTV EANSPGDDTV NSASIPVVSG
ENPLVTPYNG LRHSKDNSDS DGPAESMANP DSNSKGETGK GQDNDMAKAT KDSSNSSDGT
SSATGDTTDA VDREINKGVP EDRDKTVGSK DGGGEDNSAN KDAATVVGED RIRENSAGGS
TNDRSKNDTE KNGASTPDSK QSEDATALSK TESLESTESG DRTTNDTTNS LENKNGGKEK
DLQKHDFKSN DTPNEEPNSD QTTDAEGHDR DSIKNDKAER RKHMNKDTFT KNTNSHHLNS
NNNLSNGKLD IKEYKYRDVK ATREDIILMS SVRKCNNNIS LEYCNSVEDK ISSNTCSREK
SKNLCCSISD FCLNYFDVYS YEYLSCMKKE FEDPSYKCFT KGGFKDKTYF AAAGALLILL
LLIASRKMIK NDSEEATFNE FEEYCDNIHR IPLMPNNIEH MQPSTPLDYS
