ID A3E7E1_PLAFA Unreviewed; 381 AA.
AC A3E7E1;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:ABM53998.1};
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:ABM53998.1};
RN [1] {ECO:0000313|EMBL:ABM53998.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=787AVen {ECO:0000313|EMBL:ABM53998.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ907626; ABM53998.1; -; Genomic_DNA.
DR AlphaFoldDB; A3E7E1; -.
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:ABM53998.1};
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..209
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 285..321
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABM53998.1"
FT NON_TER 381
FT /evidence="ECO:0000313|EMBL:ABM53998.1"
SQ SEQUENCE 381 AA; 43698 MW; 19BFB5BED7972DBD CRC64;
AISVTMDNIL SGFENEYDVI YLKPLAGVYR SLKKQIEKNI FTFNLNLNDI LNSRLKKRKY
FLDVLESDLM QFKHISSNEY IIEDSFKLLN SEQKNTLLKS YKYIKESVEN DIKFAQEGIS
YYEKVLAKYK DDLESIKKVI KEEKEFPSSP PTTPPSPAKT DEQKKESKFL PFLTNIETLY
NNLVNKIDDY LINLKAKIND CNVEKNEAHV KITKLSDLKA IDDKIDLFKN HNDFEAIKKL
INDDTKKDML GKLLSTGLVQ NFPNTIISKL IEGKFQDMLN ISQHQCVKKQ CPQNSGCFRH
LDEREECKCL LNYKQEGDKC VENPNPTCNE NNGGCDADAK CTEEDSGSNG KKITCECTKP
DSYPFFDGIF CSSSNFLGIS F
//
