ID A3E7D3_PLAFA Unreviewed; 383 AA.
AC A3E7D3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=mspI {ECO:0000313|EMBL:ABM53990.1};
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:ABM53990.1};
RN [1] {ECO:0000313|EMBL:ABM53990.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S493 {ECO:0000313|EMBL:ABM53990.1};
RX PubMed=17010678; DOI=10.1016/j.meegid.2006.08.002;
RA Pacheco M.A., Poe A.C., Collins W.E., Lal A.A., Tanabe K., Kariuki S.K.,
RA Udhayakumar V., Escalante A.A.;
RT "A comparative study of the genetic diversity of the 42kDa fragment of the
RT merozoite surface protein 1 in Plasmodium falciparum and P. vivax.";
RL Infect. Genet. Evol. 7:180-187(2007).
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; DQ907618; ABM53990.1; -; Genomic_DNA.
DR AlphaFoldDB; A3E7D3; -.
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 Merozoite {ECO:0000313|EMBL:ABM53990.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
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:ABM53990.1"
FT NON_TER 383
FT /evidence="ECO:0000313|EMBL:ABM53990.1"
SQ SEQUENCE 383 AA; 43960 MW; 796E21147825DD3C CRC64;
AISVTMDNIL SGFENEYDVI YLKPLAGVYR SLKKQIEKNI FTFNLNLNDI LNSRLKKRKY
FLDVLESDLM QFKHISSNEY IIEDSFKLLN SEQKNTLLKS YKYIKESVEN DIKFAQEGIS
YYEKVLAKYK DDLESIKKVI KEEKEKFPSS PPTTPPSPAK TDEQKKESKF LPFLTNIETL
YNNLVNKIDD YLINLKAKIN DCNVEKNEAH VKITKLSDLK AIDDKIDLFK NPYDFEAIKK
LINDDTKKDM LGKLLSTGLV QNFPNTIISK LIEGKFQDML NISQHQCVKK QCPENSGCFR
HLDEREECKC LLNYKQEGDK CVENPNPTCN ENNGGCDADA TCTEEDSGSS RKKITCECTK
PDSYPLFDGI FCSSSNFLGI SFL
//
