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Database: UniProt
Entry: M1VNZ8_PLAFA
LinkDB: M1VNZ8_PLAFA
Original site: M1VNZ8_PLAFA 
ID   M1VNZ8_PLAFA            Unreviewed;      1724 AA.
AC   M1VNZ8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:BAM84408.1};
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:BAM84408.1};
RN   [1] {ECO:0000313|EMBL:BAM84408.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tz98-009 {ECO:0000313|EMBL:BAM84408.1};
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; AB502456; BAM84408.1; -; Genomic_DNA.
DR   VEuPathDB; PlasmoDB:PfGA01_090034600; -.
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:BAM84408.1};
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..1724
FT                   /note="Merozoite surface protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004019091"
FT   TRANSMEM        1705..1723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          985..1540
FT                   /note="Merozoite surface 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07462"
FT   DOMAIN          1616..1652
FT                   /note="Merozoite surface protein EGF"
FT                   /evidence="ECO:0000259|Pfam:PF12946"
FT   REGION          61..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          727..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          912..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1252..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1474..1495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          303..330
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          478..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          596..623
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        61..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1724 AA;  196038 MW;  08519CCF1C6F795C CRC64;
     MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYGLFHKEK MILNEEEITT
     KGASAQSGTS GTSGTSGTSG TSGTSGTSGT SGTSGTSGTS GTSGPSGPSG TSPSSRSNTL
     PRSNTSSGAS PPADASDSDA KSYADLKHRV RNYLFTIKEL KYPELFDLTN HMLTLCDNIH
     GFKYLIDGYE EINELLYKLN FYFDLLRAKL NDVCANDYCQ IPFNLKIRAN ELDVLKKLVF
     GYRKPLDNIK DNVGKMEDYI KKNKTTIANI NELIEGSKKT IDQNKNADNE EGKKKLYQAQ
     YDLSIYNKQL EEAHNLISVL EKRIDTLKKN ENIKKLLEDI DKIKTDAEKL TTGSKPNTLL
     DKNKKIEEHE EKIKEIAKTI KFNIDSLFTD PLELEYYLRE KNKKVDVTPK SQDPTKSVQI
     PKVPYPNGIV YPLPLTDIHN SLAADNDKNS YGDLMNPGTK EKINEKIITD NKERKIFINN
     IKKQIDLEEK NINHTKEQNK KLLEDYEKSK KDYEELLEKF YEMKFNNNFD KDVVDKMFSA
     RYTYNVEKQR YNNKFSSSNN SVYNVQKLKK ALSYLEDYSL RKGISEKDFN HYYTLKTGLE
     ADIKKLTEEI KSSENKILEK NFKGLTHSAN ASLEVYDIVK LQVQKVLLIK KIEDLRKIEL
     FLKNAQLKDS IHVPNIYKPQ NKPEPYYLIV LKKEVDKLKE FIPKVKDMLK KEQAVLSSIT
     QPLVAASETT EDGGHSTHTL SQSGETEVTE ETEETEETVG HTTTVTITLP PTQPSPPKEV
     KVVENSIEHK SNDNSQALTK TVYLKKLDEF LTKSYICHKY ILVSNSSMDQ KLLEVYNLTP
     EEKNELKSCD PLDLLFNIQN NIPAMYSLYD SMNNDLQHLF FELYQKEMIY YLHKLKEENH
     IKKLLEEQKQ ITGTSSTSSP GNTTVNTAQS ATHSNSQNQQ SNASSTNTQN GVAVSSGPAV
     VEESHDPLTV LSISNDLKGI VSLLNLGNKT KVPNPLTIST TEMEKFYENI LKNNDTYFND
     DIKQFVKSNS KVITGLTETQ KNALNDEIKK LKDTLQLSFD LYNKYKLKLD RLFNKKKELG
     QDKMQIKKLT LLKEQLESKL NSLNNPHNVL QNFSVFFNKK KEAEIAETEN TLENTKILLK
     HYKGLVKYYN GESSPLKTLS EVSIQTEDNY ANLEKFRVLS KIDGKLNDNL HLGKKKLSFL
     SSGLHHLITE LKEVIKNKNY TGNSPSENNK KVNEALKSYE NFLPEAKVTT VVTPPQPDVT
     PSPLSVRVSG SSGSTKEETQ IPTSGSLLTE LQQVVQSQNY DEEDDSLVVL PIFGESEDND
     EYLDQVVTGE AISVTMDNIL SGFENEYDVI YLKPLAGVYR SLKKQIEKNI FTFNLNLNDI
     LNSRLKKRKY FLDVLESDLM QFKHISSNEY IIEDSFKLLN SEQKNTLLKS YKYIKESVEN
     DIKFAQEGIS YYEKVLAKYK DDLESIKKVI KEEKEKFPSS PPTTPPSPAK TDEQKKESKF
     LPFLTNIETL YNNLVNKIDD YLINLKAKIN DCNVEKNEAH VKITKLSDLK AIDDKIDLFK
     NHNDFEAIKK LINDDTKKDM LGKLLSTGLV QNFPNTIISK LIEGKFQDML NISQHQCVKK
     QCPQNSGCFR HLDEREECKC LLNYKQEGDK CVENPNPTCN ENNGGCDADA KCTEEDSGSN
     GKKITCECTK PDSYPLFDGI FCSSSNFLGI SFLLILMLIL YSFI
//
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