ID A0SJG6_PLAFA Unreviewed; 394 AA.
AC A0SJG6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Merozoite surface protein 1 {ECO:0000256|ARBA:ARBA00022062};
DE AltName: Full=Merozoite surface antigen {ECO:0000256|ARBA:ARBA00031689};
DE AltName: Full=PMMSA {ECO:0000256|ARBA:ARBA00032276};
DE Flags: Fragment;
GN Name=MSP-1 {ECO:0000313|EMBL:ABF18732.1};
OS Plasmodium falciparum (malaria parasite P. falciparum).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833 {ECO:0000313|EMBL:ABF18732.1};
RN [1] {ECO:0000313|EMBL:ABF18732.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MADCH-7 {ECO:0000313|EMBL:ABF18732.1};
RX PubMed=18053992; DOI=10.1016/j.exppara.2007.10.001;
RA Mehrizi A.A., Zakeri S., Salmanian A.H., Sanati M.H., Djadid N.D.;
RT "Plasmodium falciparum: sequence analysis of the gene encoding the C-
RT terminus region of the merozoite surface protein-1, a potential malaria
RT vaccine antigen, in Iranian clinical isolates.";
RL Exp. Parasitol. 118:378-385(2008).
CC -!- FUNCTION: By binding to host proinflammatory cytokine S100P may
CC interfere with host immune responses. {ECO:0000256|ARBA:ARBA00043850}.
CC -!- SUBUNIT: Interacts with host SLC4A1/Band 3 (via 5ABC region) on the
CC host erythrocyte surface in a sialic acid-independent manner.
CC {ECO:0000256|ARBA:ARBA00044022}.
CC -!- SUBUNIT: Interacts with host glycophorin GYPA in a sialic acid-
CC independent manner. {ECO:0000256|ARBA:ARBA00044006}.
CC -!- SUBUNIT: Interacts with host proinflammatory cytokine S100P; the
CC interaction blocks S100P inflammatory and chemotactic activities.
CC {ECO:0000256|ARBA:ARBA00044008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00043950}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00043950}.
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DR EMBL; DQ489604; ABF18732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0SJG6; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR010901; MSP1_C.
DR InterPro; IPR024730; MSP1_EGF_1.
DR Pfam; PF12946; EGF_MSP1_1; 1.
DR Pfam; PF07462; MSP1_C; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Merozoite {ECO:0000313|EMBL:ABF18732.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..210
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 286..322
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 144..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABF18732.1"
SQ SEQUENCE 394 AA; 45233 MW; 5D000BC814DD0450 CRC64;
AISVTMDNIL SGFENEYDVI YLKPLAGVYR SLKKQIEKNI FTFNLNLNDI LNSRLKKRKY
FLDVLESDLM QFKHISSNEY IIEDSFKLLN SEQKNTLLKS YKYIKESVEN DIKFAQEGIS
YYEKVLAKYK DDLESIKKVI KEEKEKFPSS PPTTPPSPAK TDEQKKESKF LPFLTNIETL
YNNLVNKIDD YLINLKAKIN DCNVEKDEAH VKITKLSDLK AIDDKIDLFK NPNDFEAIKK
LINDDTKKDM LGKLLSTGLV QNFPNTIISK LIEGKFQDML NISQHQCVKK QCPENSGCFR
HLDEREECKC LLNYKQEGDK CVENPNPTCN ENNGGCDADA TCTEEDSGSS RKKITCECTK
PDSYPLFDGI FCSSSNFLGI SFLLILMLIL YSFI
//
