ID Q25645_PLABE Unreviewed; 1787 AA.
AC Q25645; O00883;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 2.
DT 27-MAR-2024, entry version 74.
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};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821 {ECO:0000313|EMBL:AAC28871.1};
RN [1] {ECO:0000313|EMBL:AAC28871.1}
RP NUCLEOTIDE SEQUENCE OF 219-373.
RC STRAIN=K173 {ECO:0000313|EMBL:AAC28871.1};
RX PubMed=9080880;
RA Toebe C.S., Clements J.D., Cardenas L., Jennings G.J., Wiser M.F.;
RT "Evaluation of immunogenicity of an oral Salmonella vaccine expressing
RT recombinant Plasmodium berghei merozoite surface protein-1.";
RL Am. J. Trop. Med. Hyg. 56:192-199(1997).
RN [2] {ECO:0000313|EMBL:AAC28871.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K173 {ECO:0000313|EMBL:AAC28871.1};
RX PubMed=9662027; DOI=10.1016/S0166-6851(98)00016-4;
RA Jennings G.J., Toebe C.S., van Belkum A., Wiser M.F.;
RT "The complete sequence of Plasmodium berghei merozoite surface protein-1
RT and its inter- and intra-species variability.";
RL Mol. Biochem. Parasitol. 93:43-55(1998).
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}.
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DR EMBL; U43521; AAC28871.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PBANKA_0831000; -.
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 PANTHER; PTHR48148; KERATINOCYTE PROLINE-RICH PROTEIN; 1.
DR PANTHER; PTHR48148:SF2; KERATINOCYTE PROLINE-RICH PROTEIN; 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:AAC28871.1};
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}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1787
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004203435"
FT TRANSMEM 1758..1784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1079..1607
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1679..1715
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 282..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 236..263
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 491..526
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1582..1647
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..982
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1787 AA; 198157 MW; A585D64F5148E4EA CRC64;
MKVIGLLFSF VFFAIKCKSE TIEVYNDIIQ KLEKLESLSV EGLELFQKSQ VIINASPPSE
TINPFSDNTF APKLQGFITK FEELGFTEQT ELVNLIKTLV PNKYGLKYLI ESKEEFNGLM
HAINFYYDVF RDKLNDMCAN NYCEIPEHLK ISEEETEMLK KVILGYRKPI ENIQDDIEKL
EIYITKNKET VTALNTLIAE ETKKITPENE ADCNDNTCDE SKYSKKKIIY QAMYNVIFYK
KQLAEIQKVI ETLEKRVSAL KKNDVIKPLL QQIEDIKAAP VTTEGQITTS GQSSTEPAST
GTPSSGEVST GTSTGGASAG VTNTGAATTG TTGTGAATTG TTGAEAVTTG NTGAEAATTG
NTNTEVTQVQ TVPTLTPEEK KKKMDGLYAQ IKEIAKTIKF NLDGIFVNPI ELEYLKKEKK
KESCNLSTSS CKKNKTSETI IPLNVRYPNG IGYPLPENDV YNKIANNAAE TTYGDLTNPD
NTPITEDLAT NEQARKNLIK AIKKKIEAEE KNLESLKTNY DNKLASFNQQ KAPFKEAAKL
FYESKFGNKL TSDIFEKFKT QRTEYMNKKT ELENGLYGNT KQLISKLNKQ LNYLQDYSLR
KDIISDEIEY FSNKKKGLQY NINRLAEAVQ AKQNILVASK DVPLSTLVEL QIQKSLLTKQ
IEQLNKTELS LRKAQLKDKV YVPKSYGNGG KPEPYYLIAV KREVDRLAQF IPKIENMIAK
EKEKTEQVPV VTGESEETSS VSTEVSVQAS SQSGTSSTVP AAGATSPTVT PVTEEAQSSQ
NAPPTTAATP ATTPEAATTA ATPATTPEAA TTSTTTSTTT STTTSTTTST TTPVMTKLYY
LEKLQKFLVF SYSCHKYLLL QNSTINKDAL SKYALTTEED KIRTLKRCSE LDILLAIQNN
MPTMYSLYES IVDGLQNIYA ELYEKEMMYH IYKLKDENPS IKSILVKAGV IDPEPVASPP
TPPTPPTPPT PPTLPTTPTP VTPAAPSEQT TTPEAATAAS NPGASASETP ASNPGASASS
TPAAASNPGA SASSTPSTAS NPSAPASSTV QPTQVQPAAP AAPAAVPAQP ANSNGSITTR
AESEEDIPAD DFELDNLYKS YLQRIDGNNT EFINFIKSKK ELIKALTPEK VNQLYLEIAH
LKELSEHYYD RYYKYKLKLE RLYEKHEQIQ VSNRQIRELS ILKARLLKRK QNINGIFYIL
SGYVNFFNKR READKQYVDN ALKNNDMLLK YYKARIKYFT SEAVPLKTLT KASLDRETNY
LKIEKFRAYS RLELRFKKNI NLGKEKISYV SGGLYHVFEE FKELLKNKNY TGKTNPDTVP
EVTNAFEQYK ELLPKGVTAS ASPAAATTPT SADAATQRAT PESGSGSGSG SVVSSTPEEV
ARSGSGENAV VSGSSVDDND DDDIDQIASG QSENAQEKNI LEAFKNESEY LYARSLGITY
KSLKKHMIRE FSTIKEDMTT GLNNKLQKRN DFLEVLNHEL DLFKDLSTNK YVIRNPYQLL
DNDKKDKQIV NLKYAAKGVN EDIETTADGI KFFNKMIELY KIQLAAVKEQ IDAIEAATTD
KDEKKKYVPI FEDLKGLYET ILGQSEEYIE VLQNRLDSYK NEKTEFEILT KNLETYIKID
EKLENFVENA ENNKHIASIA LNNLNKSGLV GEGESKKILA KMLNMDSMDL LGIDPKHVCI
NTRDIPANAG CFRYDNGNEE WRCLLGYKKN NNTCIEDSNP TCGNNNGGCD PTAGCQTAEN
RENSKKIICT CKEPTPNAYY DGVFCSSSSF MGLSILLIIT LIVFNIF
//
