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Database: UniProt
Entry: M1VF11_PLAFA
LinkDB: M1VF11_PLAFA
Original site: M1VF11_PLAFA 
ID   M1VF11_PLAFA            Unreviewed;      1702 AA.
AC   M1VF11;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:BAM84484.1};
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:BAM84484.1};
RN   [1] {ECO:0000313|EMBL:BAM84484.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Gha1109-038 {ECO:0000313|EMBL:BAM84484.1};
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; AB502532; BAM84484.1; -; Genomic_DNA.
DR   VEuPathDB; PlasmoDB:PfML01_090034800; -.
DR   VEuPathDB; PlasmoDB:PfSD01_090035300; -.
DR   VEuPathDB; PlasmoDB:PfTG01_090034700; -.
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:BAM84484.1};
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..1702
FT                   /note="Merozoite surface protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004017986"
FT   TRANSMEM        1683..1701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          963..1518
FT                   /note="Merozoite surface 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07462"
FT   DOMAIN          1594..1630
FT                   /note="Merozoite surface protein EGF"
FT                   /evidence="ECO:0000259|Pfam:PF12946"
FT   REGION          63..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1452..1473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          291..318
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          465..510
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          583..610
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        63..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1702 AA;  193935 MW;  6DFD22347E6D86E4 CRC64;
     MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFQKEK MVLNEEEITT
     KGASAQSGAS AQSGASAQSG ASAQSGTSGP SGPSGPSGTS PSSRSNTLPR SNTSSGASPP
     ADASDSDAKS YADLKHRVRN YLFTIKELKY PELFDLTNHM LTLCDNIHGF KYLIDGYEEI
     NELLYKLNFY FDLLRAKLND VCANDYCQIP FNLKIRANEL DVLKKLVFGY RKPLDNIKDN
     VGKMEDYIKK NKTTIANINE LIEGSKKTID QNKNADNEEG KKKLYQAQYD LSIYNKQLEE
     AHNLISVLEK RIDTLKKNEN IKKLLDKINE IKNPPPANSG NTPNTLLDKN KKIEEHEEKI
     KEIAKTIKFN IDSLFTDPLE LEYYLREKNK KVDVTPKSQD PTKSVQIPKV PYPNGIVYPL
     PLTDIHNSLA ADNDKNSYGD LMNPDTKEKI NEKIITDNKE RKIFINNIKK QIDLEEKNIN
     HTKEQNKKLL EDYEKSKKDY EELLEKFYEM KFNNNFDKDV VDKIFSARYT YNVEKQRYNN
     KFSSSNNSVY NVQKLKKALS YLEDYSLRKG ISEKDFNHYY TLKTGLEADI KKLTEEIKSS
     ENKILEKNFK GLTHSANASL EVSDIVKLQV QKVLLIKKIE DLRKIELFLK NAQLKDSIHV
     PNIYKPQNKP EPYYLIVLKK EVDKLKEFIP KVKDMLKKEQ AVLSSITQPL VAASETTEDG
     GHSTHTLSQS GETEVTEETE ETVGHTTTVT ITLPPKEVKV VENSIEHKSN DNSQALTKTV
     YLKKLDEFLT KSYICHKYIL VSNSSMDQKL LEVYNLTPEE KNELKSCDPL DLLFNIQNNI
     PAMYSLYDSM NNDLQHLFFE LYQKEMIYYL HKLKEENHIK KLLEEQKQIT GTSSTSSPGN
     TTVNTAQSAT HSNSQNQQSN ASSTNTQNGV AVSSGPAVVE ESHDPLTVLS ISNDLKGIVS
     LLNLGNKTKV PNPLTISTTE MEKFYENILK NNDTYFNDDI KQFVKSNSKV ITGLTETQKN
     ALNDEIKKLK DTLQLSFDLY NKYKLKLDRL FNKKKELGQD KMQIKKLTLL KEQLESKLNS
     LNNPHNVLQN FSVFFNKKKE AEIAETENTL ENTKILLKHY KGLVKYYNGE SSPLKTLSEV
     SIQTEDNYAN LEKFRVLSKI DGKLNDNLHL GKKKLSFLSS GLHHLITELK EVIKNKNYTG
     NSPSENNKKV NEALKSYENF LPEAKVTTVV TPPQPDVTPS PLSVRVSGSS GSTKEETQIP
     TSGSLLTELQ QVVQLQNYDE EDDSLVVLPI FGESEDNDEY LDQVVTGEAI SVTMDNILSG
     FENEYDVIYL KPLAGVYRSL KKQIEKNIFT FNLNLNDILN SRLKKRKYFL DVLESDLMQF
     KHISSNEYII EDSFKLLNSE QKNTLLKSYK YIKESVENDI KFAQEGISYY EKVLAKYKDD
     LESIKKVIKE EKEKFPSSPP TTPPSPAKTD EQKKESKFLP FLTNIETLYN NLVNKIDDYL
     INLKAKINDC NVEKDEAHVK ITKLSDLKAI DDKIDLFKNH NDFEAIKKLI NDDTKKDMLG
     KLLSTGLVQN FPNTIISKLI EGKFQDMLNI SQHQCVKKQC PENSGCFRHL DEREECKCLL
     NYKQEGDKCV ENPNPTCNEN NGGCDADAKC TEEDSGSNGK KITCECTKPD SYPLFDGIFC
     SSSNFLGISF LLILMLILYS FI
//
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