PF12_PLAF7
ID PF12_PLAF7 Reviewed; 347 AA.
AC C6KSX0;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Merozoite surface protein P12;
DE Contains:
DE RecName: Full=Merozoite surface protein P12, processed form;
DE Flags: Precursor;
GN Name=PF12; ORFNames=PFF0615c;
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 IDENTIFICATION.
RX PubMed=7477102; DOI=10.1016/0166-6851(94)00054-q;
RA Carter R., Coulson A., Bhatti S., Taylor B.J., Elliott J.F.;
RT "Predicted disulfide-bonded structures for three uniquely related proteins
RT of Plasmodium falciparum, Pfs230, Pfs48/45 and Pf12.";
RL Mol. Biochem. Parasitol. 71:203-210(1995).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, CLEAVAGE, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH PF41.
RX PubMed=22848665; DOI=10.1371/journal.pone.0041937;
RA Taechalertpaisarn T., Crosnier C., Bartholdson S.J., Hodder A.N.,
RA Thompson J., Bustamante L.Y., Wilson D.W., Sanders P.R., Wright G.J.,
RA Rayner J.C., Cowman A.F., Gilson P.R., Crabb B.S.;
RT "Biochemical and functional analysis of two Plasmodium falciparum blood-
RT stage 6-cys proteins: P12 and P41.";
RL PLoS ONE 7:E41937-E41937(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 28-304, DISULFIDE BOND,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PF41.
RX PubMed=23511632; DOI=10.1074/jbc.m113.455667;
RA Tonkin M.L., Arredondo S.A., Loveless B.C., Serpa J.J., Makepeace K.A.,
RA Sundar N., Petrotchenko E.V., Miller L.H., Grigg M.E., Boulanger M.J.;
RT "Structural and biochemical characterization of Plasmodium falciparum 12
RT (Pf12) reveals a unique interdomain organization and the potential for an
RT antiparallel arrangement with Pf41.";
RL J. Biol. Chem. 288:12805-12817(2013).
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PF41. May form an
CC antiparallel heterodimer with PF41.
CC -!- SUBCELLULAR LOCATION: [Merozoite surface protein P12]: Cell surface.
CC Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC Note=Present on the surface of merozoite.
CC {ECO:0000269|PubMed:22848665}.
CC -!- SUBCELLULAR LOCATION: [Merozoite surface protein P12, processed form]:
CC Cell surface. Cell membrane. Note=Shed from the merozoite surface.
CC {ECO:0000269|PubMed:22848665}.
CC -!- DEVELOPMENTAL STAGE: Specifically present in asexual blood stage
CC parasites. First detected in the trophozoite stage, 30-40 hours post-
CC invasion (HPI) and the proteins reaches peak expression in schizont
CC stage, 40-48 HPI. {ECO:0000269|PubMed:16203726,
CC ECO:0000269|PubMed:22848665}.
CC -!- PTM: Processed into a soluble form. {ECO:0000269|PubMed:22848665}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Parasites grow at normal
CC rates in vitro. {ECO:0000269|PubMed:22848665}.
CC -!- MISCELLANEOUS: Does not have erythrocyte-receptor-binding ability.
CC {ECO:0000305|PubMed:22848665}.
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DR EMBL; AL844505; CAG25366.1; -; Genomic_DNA.
DR RefSeq; XP_966114.1; XM_961021.1.
DR PDB; 2YMO; X-ray; 1.90 A; A=28-304.
DR PDB; 7S7Q; X-ray; 2.85 A; B=28-304.
DR PDB; 7S7R; X-ray; 1.77 A; A=28-304.
DR PDBsum; 2YMO; -.
DR PDBsum; 7S7Q; -.
DR PDBsum; 7S7R; -.
DR AlphaFoldDB; C6KSX0; -.
DR BMRB; C6KSX0; -.
DR SMR; C6KSX0; -.
DR STRING; 5833.PFF0615c; -.
DR SwissPalm; C6KSX0; -.
DR PRIDE; C6KSX0; -.
DR EnsemblProtists; CAG25366; CAG25366; PF3D7_0612700.
DR GeneID; 3885775; -.
DR KEGG; pfa:PF3D7_0612700; -.
DR VEuPathDB; PlasmoDB:PF3D7_0612700; -.
DR HOGENOM; CLU_766140_0_0_1; -.
DR InParanoid; C6KSX0; -.
DR OMA; TCDFNDE; -.
DR PhylomeDB; C6KSX0; -.
DR Proteomes; UP000001450; Chromosome 6.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:GeneDB.
DR GO; GO:0045177; C:apical part of cell; IDA:GeneDB.
DR GO; GO:0009986; C:cell surface; IDA:GeneDB.
DR GO; GO:0020004; C:symbiont-containing vacuolar space; IDA:GeneDB.
DR GO; GO:0044409; P:entry into host; IDA:GeneDB.
DR DisProt; DP01574; -.
DR Gene3D; 2.60.40.2860; -; 2.
DR InterPro; IPR010884; 6_CYS_dom.
DR InterPro; IPR038160; 6_CYS_dom_sf.
DR Pfam; PF07422; s48_45; 2.
DR SMART; SM00970; s48_45; 2.
DR PROSITE; PS51701; 6_CYS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Malaria; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..322
FT /note="Merozoite surface protein P12"
FT /id="PRO_0000423557"
FT CHAIN 26..?
FT /note="Merozoite surface protein P12, processed form"
FT /id="PRO_0000423558"
FT PROPEP 323..347
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423559"
FT DOMAIN 27..172
FT /note="6-Cys 1"
FT DOMAIN 175..305
FT /note="6-Cys 2"
FT LIPID 322
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..53
FT /evidence="ECO:0000269|PubMed:23511632"
FT DISULFID 67..138
FT /evidence="ECO:0000269|PubMed:23511632"
FT DISULFID 81..136
FT /evidence="ECO:0000269|PubMed:23511632"
FT DISULFID 179..211
FT /evidence="ECO:0000269|PubMed:23511632"
FT DISULFID 225..286
FT /evidence="ECO:0000269|PubMed:23511632"
FT DISULFID 236..284
FT /evidence="ECO:0000269|PubMed:23511632"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2YMO"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:2YMO"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2YMO"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:2YMO"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2YMO"
SQ SEQUENCE 347 AA; 39434 MW; 0950614A8565DEA5 CRC64;
MIKLSKKYCL GISFVLYILL SVCEGHKNLT CDFNDVYKLE FHPNQQTSVT KLCNLTPNVL
EKVTIKCGSD KLNYNLYPPT CFEEVYASRN MMHLKKIKEF VIGSSMFMRR SLTPNKINEV
SFRIPPNMMP EKPIYCFCEN KKTITINGSN GNPSSKKDII NRGIVEIIIP SLNEKVKGCD
FTTSESTIFS KGYSINEISN KSSNNQQDIV CTVKAHANDL IGFKCPSNYS VEPHDCFVSA
FNLSGKNENL ENKLKLTNII MDHYNNTFYS RLPSLISDNW KFFCVCSKDN EKKLVFTVEA
SISSSNTKLA SRDNTYQDYI SNSSFLTLSS YCAFITFIIT SFLSFIL
