GBP_PLAFG
ID GBP_PLAFG Reviewed; 774 AA.
AC P02895; Q25858;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Glycophorin-binding protein 130 {ECO:0000305};
DE Short=GBP130 protein {ECO:0000303|PubMed:3512098};
GN Name=GBP130 {ECO:0000303|PubMed:3512098};
GN Synonyms=GBP {ECO:0000303|PubMed:3883491};
OS Plasmodium falciparum (isolate FCR-3 / Gambia).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5838;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH HOST
RP GLYCOPHORIN.
RX PubMed=3512098; DOI=10.1016/0092-8674(86)90834-2;
RA Kochan J., Perkins M., Ravetch J.V.;
RT "A tandemly repeated sequence determines the binding domain for an
RT erythrocyte receptor binding protein of P. falciparum.";
RL Cell 44:689-696(1986).
RN [2] {ECO:0000312|EMBL:AAA29606.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 344-415, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Isolate FC27 {ECO:0000312|EMBL:AAA29606.1};
RX PubMed=3553939; DOI=10.1016/0166-6851(87)90191-5;
RA Bianco A.E., Culvenor J.G., Coppel R.L., Crewther P.E., McIntyre P.,
RA Favaloro J.M., Brown G.V., Kemp D.J., Anders R.F.;
RT "Putative glycophorin-binding protein is secreted from schizonts of
RT Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 23:91-102(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 556-774, AND DEVELOPMENTAL STAGE.
RX PubMed=3883491; DOI=10.1126/science.3883491;
RA Ravetch J.V., Kochan J., Perkins M.;
RT "Isolation of the gene for a glycophorin-binding protein implicated in
RT erythrocyte invasion by a malaria parasite.";
RL Science 227:1593-1597(1985).
RN [4]
RP FUNCTION, INTERACTION WITH HOST GLYCOPHORIN, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=6206188; DOI=10.1084/jem.160.3.788;
RA Perkins M.E.;
RT "Surface proteins of Plasmodium falciparum merozoites binding to the
RT erythrocyte receptor, glycophorin.";
RL J. Exp. Med. 160:788-798(1984).
CC -!- FUNCTION: Involved in merozoite invasion of host erythrocytes.
CC {ECO:0000269|PubMed:3512098, ECO:0000269|PubMed:6206188}.
CC -!- SUBUNIT: Interacts with host glycophorin. {ECO:0000269|PubMed:3512098,
CC ECO:0000269|PubMed:6206188}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3553939}. Cell
CC surface {ECO:0000269|PubMed:6206188}. Host cytoplasm
CC {ECO:0000269|PubMed:3553939}. Note=Secreted at the schizont stage into
CC the host erythrocyte cytoplasm (PubMed:3553939). Localizes to the cell
CC surface of free merozoites to some extent (PubMed:3553939,
CC PubMed:6206188). {ECO:0000269|PubMed:3553939,
CC ECO:0000269|PubMed:6206188}.
CC -!- DEVELOPMENTAL STAGE: During the asexual blood stage, expressed at the
CC trophozoite and schizont stages (at protein level).
CC {ECO:0000269|PubMed:3553939, ECO:0000269|PubMed:3883491,
CC ECO:0000269|PubMed:6206188}.
CC -!- DOMAIN: The PEXEL motif is involved in the protein translocation
CC through the parasitophorous vacuole membrane and into the host
CC erythrocyte cytoplasm. {ECO:0000250|UniProtKB:Q8I6U8}.
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DR EMBL; M12897; AAA29608.1; -; Genomic_DNA.
DR EMBL; M15212; AAA29606.1; -; mRNA.
DR EMBL; M10985; AAA29607.1; -; mRNA.
DR PIR; A03390; ZOZQMF.
DR PIR; A24057; A24057.
DR PIR; A54532; A54532.
DR AlphaFoldDB; P02895; -.
DR VEuPathDB; PlasmoDB:PF3D7_1016300; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000301900; -.
DR VEuPathDB; PlasmoDB:Pf7G8_100020800; -.
DR VEuPathDB; PlasmoDB:PfCD01_100021600; -.
DR VEuPathDB; PlasmoDB:PfDd2_100021700; -.
DR VEuPathDB; PlasmoDB:PfGA01_100021700; -.
DR VEuPathDB; PlasmoDB:PfGB4_100021400; -.
DR VEuPathDB; PlasmoDB:PfGN01_100021900; -.
DR VEuPathDB; PlasmoDB:PfHB3_100020800; -.
DR VEuPathDB; PlasmoDB:PfIT_100020400; -.
DR VEuPathDB; PlasmoDB:PfKE01_100021700; -.
DR VEuPathDB; PlasmoDB:PfKH01_100020900; -.
DR VEuPathDB; PlasmoDB:PfKH02_100021800; -.
DR VEuPathDB; PlasmoDB:PfML01_100020600; -.
DR VEuPathDB; PlasmoDB:PfNF135_100021700; -.
DR VEuPathDB; PlasmoDB:PfNF166_130006400; -.
DR VEuPathDB; PlasmoDB:PfNF54_100021500; -.
DR VEuPathDB; PlasmoDB:PfSD01_100021000; -.
DR VEuPathDB; PlasmoDB:PfSN01_100021800; -.
DR VEuPathDB; PlasmoDB:PfTG01_100021600; -.
DR InterPro; IPR003681; Glycophorin-bd.
DR Pfam; PF02526; GBP_repeat; 11.
DR PROSITE; PS51069; GBP; 11.
PE 1: Evidence at protein level;
KW Host cytoplasm; Malaria; Merozoite; Repeat; Secreted.
FT CHAIN 1..774
FT /note="Glycophorin-binding protein 130"
FT /id="PRO_0000217186"
FT REPEAT 226..275
FT /note="GBP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 276..325
FT /note="GBP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 326..375
FT /note="GBP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 376..425
FT /note="GBP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 426..474
FT /note="GBP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 475..524
FT /note="GBP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 525..574
FT /note="GBP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 575..624
FT /note="GBP 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 625..674
FT /note="GBP 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 675..724
FT /note="GBP 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 725..774
FT /note="GBP 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REGION 97..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..88
FT /note="PEXEL motif"
FT /evidence="ECO:0000250|UniProtKB:Q8I6U8"
FT COMPBIAS 114..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 344
FT /note="E -> A (in Ref. 2; AAA29606)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="T -> A (in Ref. 3; AAA29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="E -> D (in Ref. 3; AAA29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="D -> E (in Ref. 3; AAA29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="A -> V (in Ref. 3; AAA29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="S -> P (in Ref. 3; AAA29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="H -> D (in Ref. 3; AAA29607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 774 AA; 90018 MW; 16B795D08C0C1798 CRC64;
MRLSKVSDIK STGVSNYKNF NSKNSSKYSL MEVSKKNEKK NSLGAFHSKK ILLIFGIIYV
VLLNAYICGD KYEKAVDYGF RESRILAEGE DTCARKEKTT LRKSKQKTST RTVATQTKKD
EENKSVVTEE QKVESDSEKQ KRTKKVVKKQ INIGDTENQK EGKNVKKVIK KEKKKEESGK
PEENKHANEA SKKKEPKASK VSQKPSTSTR SNNEVKIRAA SNQETLTSAD PEGQIMREYA
ADPEYRKHLE IFYKILTNTD PNDEVERRNA DNKEDLTSAD PEGQIMREYA SDPEYRKHLE
IFYKILTNTD PNDDVERRNA DNKEDLTSAD PEGQIMREYA ADPEYRKHLE VFHKILTNTD
PNDEVERRNA DNKEDLTSAD PEGQIMREYA ADPEYRKHLE IFHKILTNTD PNDEVERRNA
DNKEDLTSAD PEGQIMREYA ADPEYRKHLE VFHKILTNTD PNDEVERRNA DNKELTSSDP
EGQIMREYAA DPEYRKHLEI FHKILTNTDP NDEVERRNAD NKEDLTSADP EGQIMREYAA
DPEYRKHLEI FYKILTNTDP NDEVERRNAD NKEELTSSDP EGQIMREYAA DPEYRKHLEI
FHKILTNTDP NDEVERRNAD NKEDLTSADP EGQIMREYAA DPEYRKHLEI FYKILTNTDP
NDEVERRNAD NKEDLTSADP EGQIMREYAS DPEYRKHLEI FYKILTNTDP NDDVERRNAD
NKEDLTSADP EGQIMREYAA DPEYRKHLEI FHKILTNTDP NDEVERQNAD NNEA
