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Database: UniProt
Entry: M1VEW4_PLAFA
LinkDB: M1VEW4_PLAFA
Original site: M1VEW4_PLAFA 
ID   M1VEW4_PLAFA            Unreviewed;      1688 AA.
AC   M1VEW4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=msp1 {ECO:0000313|EMBL:BAM84404.1};
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:BAM84404.1};
RN   [1] {ECO:0000313|EMBL:BAM84404.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tz03-086 {ECO:0000313|EMBL:BAM84404.1};
RA   Tanabe K., Mita T., Palacpac N.M.Q., Arisue N., Tougan T., Kawai S.,
RA   Jombart T., Kobayashi F., Horii T.;
RT   "Within-population genetic diversity of Plasmodium falciparum vaccine
RT   candidate antigens reveals geographic distance from a Central sub-Saharan
RT   African origin.";
RL   Vaccine 31:1134-1139(2013).
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; AB502452; BAM84404.1; -; Genomic_DNA.
DR   VEuPathDB; PlasmoDB:PfKE01_090034700; -.
DR   VEuPathDB; PlasmoDB:PfSN01_090034900; -.
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:BAM84404.1};
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..1688
FT                   /note="Merozoite surface protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004018915"
FT   TRANSMEM        1669..1687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          949..1504
FT                   /note="Merozoite surface 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07462"
FT   DOMAIN          1580..1616
FT                   /note="Merozoite surface protein EGF"
FT                   /evidence="ECO:0000259|Pfam:PF12946"
FT   REGION          68..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1216..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          273..300
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          448..493
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          566..593
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        68..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1226..1246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1688 AA;  193030 MW;  F3BB418344AE781D CRC64;
     MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYGLFHKEK MVLKDGANTQ
     VVAKPADAVS TQSAKNPPGA TVPSGTASTK GAIRSPGAAN PSDDSSDSDA KSYADLKHRV
     QNYLFTIKEL KYPELFDLTN HMLTLCDNIH GFKYLIDGYE EINELLYKLN FYFDLLRAKL
     NDVCANDYCQ IPFNLKIRAN ELDVLKKLVF GYRKPLDNIK DNVGKMEDYI KKNKTTIANI
     NELIEGSKKT IDQNKNADNE EGKKKLYQAQ YDLSIYNKQL EEAHNLISVL EKRIDTLKKN
     ENIKKLLEDI DKIKTDAEKP TTGSKPNTLL DKNKKIEEHE EKIKEIAKTI KFNIDSLFTD
     PLELEYYLRE KNKKVDVTPK SQDPTKSVQI PKVPYPNGIV YPLPLTDIHN SLAADNDKNS
     YGDLMNPNTK EKINEKIITD NKERKIFINN IKKQIDLEEK NINHTKEQNK KLLEDYEKSK
     KDYEELLEKF YEMKFNNNFN KDVVDKMFSA RYTYNVEKQR YNNKFSSSNN SVYNVQKLKK
     ALSYLEDYSL RKGISEKDFN HYYTLKTGLE ADIKKLTEEI KSSENKILEK NFKGLTHSAN
     ASLEVYDIVK LQVQKVLLIK KIEDLRKIEL FLKNAQLKDS IHVPNIYKPQ NKPEPYYLIV
     LKKEVDKLKE FIPKVKDMLK KEQAVLSSIT QPLVAASETT EDGGHSTHTL SQSGETEVTE
     ETEETEETVG HTTTVTITLP PKEVKVVENS IEHKSNDNSQ ALTKTVYLKK LDEFLTKSYI
     CHKYILVSNS SMDQKLLEVY NLTPEEKNEL KSCDPLDLLF NIQNNIPAMY SLYDSMNNDL
     QHLFFELYQK EMIYYLHKLK EENHIKKLLE EQKQITGTSS TSSPGNTTVN TAQSATHSNS
     QNQQSNASST NTQNGVAVSS GPAVVEESHD PLTVLSISND LKGIVSLLNL GNKTKVPNPL
     TISTTEMEKF YENILKNNDT YFNDDIKQFV KSNSKVITGL TETQKNALND EIKKLKDTLQ
     LSFDLYNKYK LKLDRLFNKK KELGQDKMQI KKLTLLKEQL ESKLNSLNNP HNVLQNFSVF
     FNKKKEAEIA ETENTLENTK ILLKHYKGLV KYYNGESSPL KTLSEVSIQT EDNYANLEKF
     RVLSKIDGKL NDNLHLGKKK LSFLSSGLHH LITELKEVIK NKNYTGNSPS ENNKKVNEAL
     KSYENFLPEA KVTTVVTPPQ PDVTPSPLSV RVSGSSGSTK EETQIPTSGS LLTELQQVVQ
     LQNYDEEDDS LVVLPIFGES EDNDEYLDQV VTGEAISVTM DNILSGFENE YDVIYLKPLA
     GVYRSLKKQI EKNIFTFNLN LNDILNSRLK KRKYFLDVLE SDLMQFKHIS SNEYIIEDSF
     KLLNSEQKNT LLKSYKYIKE SVENDIKFAQ EGISYYEKVL AKYKDDLESI KKVIKEEKEK
     FPSSPPTTPP SPAKTDEQKK ESKFLPFLTN IETLYNNLVN KIDDYLINLK AKINDCNVEK
     DEAHVKITKL SDLKAIDDKI DLFKNTDDFE AIKKLINDDT KKDMLGKLLS TGLVQNFPNT
     IISKLIEGKF QDMLNISQHQ CVKKQCPQNS GCFRHLDERE ECKCLLNYKQ EGDKCVENPN
     PTCNENNGGC DADAKCTEED SGSNGKKITC ECTKPDSYPF FDGIFCSSSN FLGISFLLIL
     MLILYSFI
//
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