PF92_PLAF7
ID PF92_PLAF7 Reviewed; 796 AA.
AC Q8ID66; A0A5K1K931;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Merozoite surface protein P92 {ECO:0000305|PubMed:16203726};
DE Flags: Precursor;
GN Name=PF92 {ECO:0000303|PubMed:16203726}; ORFNames=PF13_0338, PF3D7_1364100;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16203726; DOI=10.1074/jbc.m509631200;
RA Sanders P.R., Gilson P.R., Cantin G.T., Greenbaum D.C., Nebl T.,
RA Carucci D.J., McConville M.J., Schofield L., Hodder A.N., Yates J.R. III,
RA Crabb B.S.;
RT "Distinct protein classes including novel merozoite surface antigens in
RT Raft-like membranes of Plasmodium falciparum.";
RL J. Biol. Chem. 280:40169-40176(2005).
RN [4]
RP GPI-ANCHOR.
RX PubMed=16603573; DOI=10.1074/mcp.m600035-mcp200;
RA Gilson P.R., Nebl T., Vukcevic D., Moritz R.L., Sargeant T., Speed T.P.,
RA Schofield L., Crabb B.S.;
RT "Identification and stoichiometry of glycosylphosphatidylinositol-anchored
RT membrane proteins of the human malaria parasite Plasmodium falciparum.";
RL Mol. Cell. Proteomics 5:1286-1299(2006).
RN [5]
RP FUNCTION, INTERACTION WITH HUMAN CFH, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=D10 {ECO:0000269|PubMed:26700768};
RX PubMed=26700768; DOI=10.4049/jimmunol.1501581;
RA Kennedy A.T., Schmidt C.Q., Thompson J.K., Weiss G.E.,
RA Taechalertpaisarn T., Gilson P.R., Barlow P.N., Crabb B.S., Cowman A.F.,
RA Tham W.H.;
RT "Recruitment of Factor H as a Novel Complement Evasion Strategy for Blood-
RT Stage Plasmodium falciparum Infection.";
RL J. Immunol. 196:1239-1248(2016).
CC -!- FUNCTION: During the asexual blood stage, recruits host complement
CC factor H CFH to the surface of merozoites resulting in the down-
CC regulation of the host complement alternative pathway and thus,
CC protecting merozoites from complement-mediated lysis.
CC {ECO:0000269|PubMed:26700768}.
CC -!- SUBUNIT: Interacts with host complement factor CFH isoform 1 (via sushi
CC 4-6 domains) and CFH isoform FHL-1 (via sushi 4-6 domains); this
CC interaction recruits CFH onto the merozoite surface preventing
CC complement-mediated cell lysis (PubMed:26700768). The interaction does
CC not affect CFH activity (PubMed:26700768).
CC {ECO:0000269|PubMed:26700768}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16203726}. Cell
CC membrane {ECO:0000269|PubMed:16203726}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:16203726}. Note=Present on the surface of
CC merozoite. {ECO:0000269|PubMed:16203726}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC specifically in schizonts (at protein level).
CC {ECO:0000269|PubMed:16203726, ECO:0000269|PubMed:26700768}.
CC -!- DISRUPTION PHENOTYPE: In strain D10, causes a loss of binding of human
CC CFH to the merozoite surface resulting in a 7-fold increase in host
CC complement-mediated merozoite lysis. {ECO:0000269|PubMed:26700768}.
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DR EMBL; AL844509; VWP77958.1; -; Genomic_DNA.
DR RefSeq; XP_001350352.1; XM_001350316.1.
DR AlphaFoldDB; Q8ID66; -.
DR STRING; 5833.PF13_0338; -.
DR SwissPalm; Q8ID66; -.
DR PRIDE; Q8ID66; -.
DR EnsemblProtists; CAD52761; CAD52761; PF3D7_1364100.
DR GeneID; 814297; -.
DR KEGG; pfa:PF3D7_1364100; -.
DR VEuPathDB; PlasmoDB:PF3D7_1364100; -.
DR HOGENOM; CLU_324285_0_0_1; -.
DR InParanoid; Q8ID66; -.
DR OMA; YGHREFK; -.
DR PhylomeDB; Q8ID66; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:GeneDB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.2860; -; 1.
DR InterPro; IPR010884; 6_CYS_dom.
DR InterPro; IPR038160; 6_CYS_dom_sf.
DR Pfam; PF07422; s48_45; 1.
DR SMART; SM00970; s48_45; 1.
DR PROSITE; PS51701; 6_CYS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Malaria; Membrane; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..796
FT /note="Merozoite surface protein P92"
FT /id="PRO_0000423565"
FT DOMAIN 571..720
FT /note="6-Cys"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 614..691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 625..689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
SQ SEQUENCE 796 AA; 92728 MW; 20BADAD565C705DA CRC64;
MFAVNLKICI FLSLVSFLLQ CKNTLANVTF EQKVQTNLSH DKNGDIVYGH REFKGGIYAF
LGYDNCTIEV NKTVNGIDWN EKKDVKVSGN NNIAVVYSIF TSEEKMILIF KCDNKFYITK
YGKEFKWSDP KVIDVSNVIG TNTTPAVYSG SLLSMNNDFE KYILVCENHS QNYINVVDQE
YMREIRLLGK CMLSFDEGNN WKNEVMNLYS DEGYTKINTL RLSDYGGKIL VKGTNAQNLN
QTIRSIILLC SNLHDWKLFC GLPTIRFRKD ISVENLTYLN TYHLAIVKNE DKLQLAFTYD
LFETFDPQYL NTEFNGVSHY FVLAPDEMVY LFYHGNEKKN YVIKIKTVPR KIGCELNTND
TVNKIYTYTY KYIYNNKLSA KTCKVPSSHL KYSSDGLYKL FEVRLPKDIK VTENCFRYSF
LSDLNNKYHT TIIKTRVINK LEDYVEVQFH FPIYYTKFLY NYKSTYCVLS NNYRIVVEFD
YIRNHIDLDF PFDTDTVKLY SNESVTHAFR NNTEKTHVHK FPKGTYMTSY FSYEKEYVIS
NYIEEPFSTT FTILTQTQMN VHFMAGGQKY KYEGIDLTDS SPNYELSLNS LSDSQNVDIF
VSKFDNNKTI GFVCPVKSSY DGLNCFDNVY IKNKTLVKIE YLFGENDIFV VPQRRIYKTE
GTAMESLLYL NNNNVKKLID DKSIIHFYCE CNVNNNVIKV NYYISPFYDE NSIKQEINKK
DQEITMINKT IPQDEKDILF NNEKVVPLSN EPQEIIQPPI QEKLNTTDPS KAYIYGANII
FIAIISIISL SISSFI
