ID Q9NHX1_PLAFA Unreviewed; 1694 AA.
AC Q9NHX1;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 63.
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};
GN Name=gp195 {ECO:0000313|EMBL:AAF27526.1};
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:AAF27526.1};
RN [1] {ECO:0000313|EMBL:AAF27526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FCC1/HN {ECO:0000313|EMBL:AAF27526.1};
RA Shan Z.X., Yu X.B., Li X.R., Ma C.L., Fang J.M.;
RT "Molecular cloning and sequence analysis of major merozoite surface
RT antigen(gp195)gene of Plasmodium falciparum isolate FCC1/HN.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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; AF218248; AAF27526.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PfKH01_090034600; -.
DR VEuPathDB; PlasmoDB:PfKH02_090035100; -.
DR VEuPathDB; PlasmoDB:PfNF135_090034000; -.
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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Merozoite {ECO:0000313|EMBL:AAF27526.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1694
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004330635"
FT TRANSMEM 1675..1693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 956..1510
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1586..1622
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 58..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 455..500
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 573..600
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1694 AA; 192768 MW; B51634A49E0F6728 CRC64;
MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFQKEK MVLNEGTSGT
AVTTSTPGSG GSVTSGGSGG SVASVASGGS GGSVASGGSG NSRRTNPSDN SSDSDAKSYA
DLKHRVQNYL FTIKELKYPE LFDLTNHMLT LCDNIHGFKY LIDGYEEINE LLYKLNFYYD
LLRAKLNDAC ANSYCQIPFN LKIRANELDV LKKIVFGYRK PLDNIKDNVG KMEDYIKKNK
TTIANINELI EGSKKTIDQN KNADNEEGKK KLYQAQYNLF IYNKQLQEAH NLISVLEKRI
DTLKKNENIK KLLEDIDKIK TDAEKLTTGS KPNPLPENKK KEVEGHEEKI KEIAKTIKFN
IDSLFTDPLE LEYYLREKNK KVDVTPKSQD PTKSVQIPKV PYPNGIVYPL PLTDIHNSLA
ADNDKNSYGD LMNPDTKEKI NEKIITDNKE RKIFINNIKK QIDLEEKNIN HTKEQNKKLL
EDYEKSKKDY EELLEKFYEM KFNNNFDKDV VDKIFSARYT YNVEKQKYNN KFSSSNNSVY
NVQKLKKALS YLEDYSLRKG ISEKDFNHYY TLKTGLEADI KKLTEEIKSS ENKILEKNFK
GLTHSANASL EVSDIVKLQV QKVLLIKKIE DLRKIELFLK NAQLKDSIHV PNIYKPQNKP
EPYYLIVLKK EVDKLKEFIP KVKDMLKKEQ AVLSSITQPL VAASETTEDG GHSTHTLSQS
GETEETEETV GHTTTVTITL PPTQPSPPKE VKVVENSIEH KSNDNSQALT KTVYLKKLDE
FLTKSYICHK YILVSNSSMD QKLLEVYNLT PEEKNELKSC DPLDLLFNIQ NNIPAMYSLY
DSMNNDLQHL FFELYQKEMI YYLHKLKEEN HIKKLLEEQK QITGTSSTSS PGNTTVNTAQ
SATHSNSQNQ QSNASSTNTQ NGVAVSSGPA VVEESHDPLT VLSISNDLKG IVSLLNLGNK
TKVPNPLTIS TTEMEKFYEN ILKNNDTYFN DDIKQFVKSN SKVITGLTET QKNALNDEIK
KLKDTLQLSF DLYNKYKLKL DRLFNKKKEL GQDKMQIKKL TLLKEQLESK LNSLNNPHNV
LQNFSVFFNK KKEAEIAETE NTLENTKILL KHYKGLVKYY NGESSPLKTL SEVSIQTEDN
YANLEKFRVL SKIDGKLNDN LHLGKKKLSF LSSGLHHLIT ELKEVIKNKN YTGNSPSENN
KKVNEALKSY ENFLPEAKVT TVVTPPQPDV TPSPLSVRVS GSSGSTKEET QIPTSGSLLT
ELQQVVQSQN YDEEDDSLVV LPIFGESEDN DEYLDQVVTG EAISVTMDNI LSGFENEYDV
IYLKPLAGVY RSLKKQIEKN IITFNLNLND ILNSRLKKRK YFLDVLESDL MQFKHISSNE
YIIEDSFKLL NSEQKNTLLK SYKYIKESVE NDIKFAQEGI SYYEKVLAKY KDDLESIKKV
IKEEKEFPSS PPTTPPSPAK TDEQKKESKF LPFLTNIETL YNNLVNKIDD YLINLKAKIN
DCNVEKDEAH VKITKLSDLK AIDDKIDLFK NTNDFEAIKK LINDDTKKDM LGKLLSTGLV
QNFPNTIISK LIEGKFQDML NISQHQCVKK QCPENSGCFR HLDEREECKC LLNYKQEGDK
CVENPNPTCN ENNGGCDADA KCTEEDSGSN GKKITCECTK PDSYPLFDGI FCSSSNFLGI
SFLLILMLIL YSFI
//
