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Database: UniProt
Entry: M1VF28_PLAFA
LinkDB: M1VF28_PLAFA
Original site: M1VF28_PLAFA 
ID   M1VF28_PLAFA            Unreviewed;      1699 AA.
AC   M1VF28;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
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:BAM84509.1};
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:BAM84509.1};
RN   [1] {ECO:0000313|EMBL:BAM84509.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TiMS95-102 {ECO:0000313|EMBL:BAM84509.1};
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).
RN   [2] {ECO:0000313|EMBL:BAN59451.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PFS79 {ECO:0000313|EMBL:BAN59451.1};
RA   Tanabe K., Zollner G.E., Sattabongkt J., Khuntirat B., Honma H., Mita T.,
RA   Tsuboi T., Coleman R.;
RT   "Genetic diversity of Plasmodium falciparum in an isolated village in
RT   western Thailand.";
RL   Submitted (JUN-2013) 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; AB502557; BAM84509.1; -; Genomic_DNA.
DR   EMBL; AB827758; BAN59451.1; -; Genomic_DNA.
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:BAM84509.1};
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..1699
FT                   /note="Merozoite surface protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007688824"
FT   TRANSMEM        1680..1698
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          961..1515
FT                   /note="Merozoite surface 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07462"
FT   DOMAIN          1591..1627
FT                   /note="Merozoite surface protein EGF"
FT                   /evidence="ECO:0000259|Pfam:PF12946"
FT   REGION          58..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1450..1470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          460..505
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          578..605
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        82..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..931
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1699 AA;  193460 MW;  C926C669CA88A04D CRC64;
     MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFQKEK MVLNEGTSGT
     AVTTSTPGSV ASGGSVASGG SGGSVASGGS GGSVASGGSV ASGGSGNSRR TNPSDNSSDS
     DAKSYADLKH RVRNYLFTIK ELKYPELFDL TNHMLTLCDN IHGFKYLIDG YEEINELLYK
     LNFYFDLLRA KLNDVCANDY CQIPFNLKIR ANELDVLKKI VFGYRKPLDN IKDNVGKMED
     YIKKNKTTIA NINELIEGSK KTIDQNKNAD NEEGKKKLYQ AQYDLFIYNK QLQEAHNLIS
     VLEKRIDTLK KNENIKKLLE DIDKIKTDAE KLTTGSKPNT LLDKNKKIEE HEEKIKEIAK
     TIKFNIDSLF TDPLELEYYL REKNKKVDVT PKSQDPTKSV QIPKVPYPNG IVYPLPLTDI
     HNSLAADNDK NSYGDLMNPD TKEKINEKII TDNKERKIFI NNIKKQIDLE EKNINHTKEQ
     NKKLLEDYEK SKKDYEELLE KFYEMKFNNN FDKDVVDKIF RARYTYNVEK QTYNNKFSSS
     NNSVYNVQKL KKALSYLEDY SLRKGISEKD FNHYYTLKTG LEADIKKLTE EIKSSENKIL
     EKNFKGLTHS ANASLEVSDI VKLQVQKVLL IKKIEDLRKI ELFLKNAQLK DSIHVPNIYK
     PQNKPEPYYL IVLKKEVDKL KEFIPKVKDM LKKEQAVLSS ITQPLVAASE TTEDGGHSTH
     TLSQSGETEV TEETEETEET VGHTTTVTIT LPPKEVKVVE NSIEHKSNDN SQALTKTVYL
     KKLDEFLTKS YICHKYILVS NSSMDQKLLE VYNLTPEEEN ELKSCDPLDL LFNIQNNIPA
     MYSLYDSMNN DLQHLFFELY QKEMIYYLHK LKEENHIKKL LEEQKQITGT SSTSSPGNTT
     VNTAQSATHS NSQNQQSNAS STNTQNGVAV SSGPAVVEES HDPLTVLSIS NDLKGIVSLL
     NLGNKTKVPN PLTISTTEME KFYENILKNN DTYFNDDIKQ FVKSNSKVIT GLTETQKNAL
     NDEIKKLKDT LQLSFDLYNK YKLKLDRLFN KKKELGQDKM QIKKLTLLKE QLESKLNSLN
     NPHNVLQNFS VFFNKKKEAE IAETENTLEN TKILLKHYKG LVKYYNGESS PLKTLSEVSI
     QTEDNYANLE KFRTLSKIDG KLNDNLHLGK KKLSFLSSGL HHLITELKEV IKNKNYTGNS
     PSENNKKVNE ALKSYENFLP EAKVTTVVTP PQPDVTPSPL SVRVSGSSGS TKEETQIPTS
     GSLLTELQQV VQLQNYDEED DSLVVLPIFG ESEDNDEYLD QVVTGEAISV TMDNILSGFE
     NEYDVIYLKP LAGVYRSLKK QIEKNIFTFN LNLNDILNSR LKKRKYFLDV LESDLMQFKH
     ISSNEYIIED SFKLLNSEQK NTLLKSYKYI KESVENDIKF AQEGISYYEK VLAKYKDDLE
     SIKKVIKEEK EFPSSPPTTP PSPAKTDEQK KESKFLPFLT NIETLYNNLV NKIDDYLINL
     KAKINDCNVE KDEAHVKITK LSDLKAIDDK IDLFKNTNDF EAIKKLINDD TKKDMLGKLL
     STGLVQNFPN TIISKLIEGK FQDMLNISQH QCVKKQCPEN SGCFRHLDER EECKCLLNYK
     QEGDKCVENP NPTCNENNGG CDADATCTEE DSGSSRKKIT CECTKPDSYP LFDGIFCSSS
     NFLGISFLLI LMLILYSFI
//
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