PF12_PLAFA
ID PF12_PLAFA Reviewed; 347 AA.
AC P19259;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Merozoite surface protein P12;
DE Flags: Precursor;
GN Name=PF12;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1696728; DOI=10.1073/pnas.87.16.6363;
RA Elliott J.F., Albrecht G.R., Gilladoga A., Handunnetti S.M., Neequaye J.,
RA Lallinger G., Minjas J.N., Howard R.J.;
RT "Genes for Plasmodium falciparum surface antigens cloned by expression in
RT COS cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6363-6367(1990).
RN [2]
RP STRUCTURE BY NMR OF 174-300 AND DISULFIDE BONDS.
RX PubMed=22493233; DOI=10.1073/pnas.1204363109;
RA Arredondo S.A., Cai M., Takayama Y., MacDonald N.J., Anderson D.E.,
RA Aravind L., Clore G.M., Miller L.H.;
RT "Structure of the Plasmodium 6-cysteine s48/45 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6692-6697(2012).
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PF41. May form an
CC antiparallel heterodimer with PF41 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell surface. Cell membrane {ECO:0000250}; Lipid-
CC anchor, GPI-anchor {ECO:0000250}. Note=Present on the surface of
CC merozoite. {ECO:0000250}.
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DR EMBL; M28889; AAA29649.1; -; Genomic_DNA.
DR PIR; B36018; B36018.
DR PDB; 2LOE; NMR; -; A=174-300.
DR PDBsum; 2LOE; -.
DR AlphaFoldDB; P19259; -.
DR BMRB; P19259; -.
DR SMR; P19259; -.
DR VEuPathDB; PlasmoDB:PF3D7_0612700; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000165100; -.
DR VEuPathDB; PlasmoDB:Pf7G8_060017700; -.
DR VEuPathDB; PlasmoDB:PfCD01_060018200; -.
DR VEuPathDB; PlasmoDB:PfDd2_060017600; -.
DR VEuPathDB; PlasmoDB:PfGA01_060017600; -.
DR VEuPathDB; PlasmoDB:PfGB4_060017300; -.
DR VEuPathDB; PlasmoDB:PfGN01_060018500; -.
DR VEuPathDB; PlasmoDB:PfHB3_060017000; -.
DR VEuPathDB; PlasmoDB:PfIT_060016700; -.
DR VEuPathDB; PlasmoDB:PfKE01_060018900; -.
DR VEuPathDB; PlasmoDB:PfKH01_060019900; -.
DR VEuPathDB; PlasmoDB:PfKH02_060019000; -.
DR VEuPathDB; PlasmoDB:PfML01_060016700; -.
DR VEuPathDB; PlasmoDB:PfNF135_060016900; -.
DR VEuPathDB; PlasmoDB:PfNF166_060017300; -.
DR VEuPathDB; PlasmoDB:PfNF54_060017600; -.
DR VEuPathDB; PlasmoDB:PfSD01_060016700; -.
DR VEuPathDB; PlasmoDB:PfSN01_060017700; -.
DR VEuPathDB; PlasmoDB:PfTG01_060018200; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Repeat; Signal.
FT SIGNAL 1..23
FT /note="Or 25"
FT /evidence="ECO:0000255"
FT CHAIN 24..322
FT /note="Merozoite surface protein P12"
FT /id="PRO_0000024606"
FT PROPEP 323..347
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024607"
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:0000250"
FT DISULFID 67..138
FT /evidence="ECO:0000250"
FT DISULFID 81..136
FT /evidence="ECO:0000250"
FT DISULFID 179..211
FT DISULFID 225..286
FT DISULFID 236..284
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:2LOE"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2LOE"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2LOE"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:2LOE"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:2LOE"
SQ SEQUENCE 347 AA; 39468 MW; 5FBA590AEEFC4E39 CRC64;
MIKLSKKYCL GISFVLYILL SVCEGHKNLT CDFNDVYKLE FHPNQQTSVT KLCNVTPNVL
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 SRYNTYQDYI SNSSFLTLSS YCAFITFIIT SFLSFIL
