GBP_PLAF7
ID GBP_PLAF7 Reviewed; 824 AA.
AC Q8I6U8; A0A143ZWU2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Glycophorin-binding protein 130 {ECO:0000305};
DE Short=GBP130 protein {ECO:0000303|PubMed:15591202};
GN Name=GBP130 {ECO:0000303|PubMed:15591202};
GN Synonyms=GBP {ECO:0000250|UniProtKB:P02895};
GN ORFNames=PF10_0159, PF3D7_1016300;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP SUBCELLULAR LOCATION, AND PEXEL MOTIF.
RX PubMed=15591202; DOI=10.1126/science.1102452;
RA Marti M., Good R.T., Rug M., Knuepfer E., Cowman A.F.;
RT "Targeting malaria virulence and remodeling proteins to the host
RT erythrocyte.";
RL Science 306:1930-1933(2004).
CC -!- FUNCTION: Involved in merozoite invasion of host erythrocytes.
CC {ECO:0000250|UniProtKB:P02895}.
CC -!- SUBUNIT: Interacts with host glycophorin.
CC {ECO:0000250|UniProtKB:P02895}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02895}. Cell
CC surface {ECO:0000250|UniProtKB:P02895}. Host cytoplasm
CC {ECO:0000269|PubMed:15591202}. Note=Secreted at the schizont stage into
CC the host erythrocyte cytoplasm. Localizes to the cell surface of free
CC merozoites to some extent. {ECO:0000250|UniProtKB:P02895}.
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:0000269|PubMed:15591202}.
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DR EMBL; LN999944; CZT98416.1; -; Genomic_DNA.
DR RefSeq; XP_001347444.1; XM_001347408.1.
DR AlphaFoldDB; Q8I6U8; -.
DR STRING; 5833.PF10_0159; -.
DR DrugBank; DB11638; Artenimol.
DR SwissPalm; Q8I6U8; -.
DR PRIDE; Q8I6U8; -.
DR EnsemblProtists; CZT98416; CZT98416; PF3D7_1016300.
DR GeneID; 810317; -.
DR KEGG; pfa:PF3D7_1016300; -.
DR VEuPathDB; PlasmoDB:PF3D7_1016300; -.
DR HOGENOM; CLU_343722_0_0_1; -.
DR InParanoid; Q8I6U8; -.
DR OMA; EHDREMR; -.
DR PhylomeDB; Q8I6U8; -.
DR Proteomes; UP000001450; Chromosome 10.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:GeneDB.
DR InterPro; IPR003681; Glycophorin-bd.
DR Pfam; PF02526; GBP_repeat; 12.
DR PROSITE; PS51069; GBP; 12.
PE 3: Inferred from homology;
KW Host cytoplasm; Malaria; Merozoite; Reference proteome; Repeat; Secreted.
FT CHAIN 1..824
FT /note="Glycophorin-binding protein 130"
FT /id="PRO_0000217185"
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..424
FT /note="GBP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REPEAT 425..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 REPEAT 775..824
FT /note="GBP 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00402"
FT REGION 97..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..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..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..88
FT /note="PEXEL motif"
FT /evidence="ECO:0000269|PubMed:15591202"
FT COMPBIAS 114..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..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 408..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 95844 MW; 5A8FBE83C94B8D33 CRC64;
MRLSKVSDIK STGVSNYKNF NSKNSSKYSL MEVSKKNEKK NSLGAFHSKK ILLIFGIIYV
VLLNAYICGD KYEKAVDYGF RESRILAEGE DTCARKEKTT LRKSKQKTST RTVATQTKKD
EENKSVVTEE QKVESDSEKQ KRTKKVVKKQ INIGDTENQK EGKNVKKVIK KEKKKEESGK
PEENKHANEA SKKQEPKASK VSQKPSTSTR SNNEVKIRAA SNQETLTSAD PEGQIMREYA
ADPEYRKHLE IFYKILTNTD PNDEVERRNA DNKEDLTSAD PEGQIMREYA SDPEYRKHLE
IFYKILTNTD PNDDVERRNA DNKEDLTSAD PEGQIMREYA ADPEYRKHLE VFHKILTNTD
PNDEVERRNA DNKEDLTSAD PEGQIMREYA ADPEYRKHLE VFHKILTNTD PNDEVERRNA
DNKELTSSDP EGQIMREYAA DPEYRKHLEV FHKILTNTDP NDEVERRNAD NKEDLTSADP
EGQIMREYAA DPEYRKHLEV FHKILTNTDP NDEVERRNAD NKEDLTSADP 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 DPEYRKHLEV FHKILTNTDP NDEVERQNAD NNEA
