ID A0A0Y9WA72_PLABE Unreviewed; 1789 AA.
AC A0A0Y9WA72;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:CXI36173.1};
GN ORFNames=PBK173_000174200 {ECO:0000313|EMBL:CXI36173.1};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821 {ECO:0000313|EMBL:CXI36173.1, ECO:0000313|Proteomes:UP000069549};
RN [1] {ECO:0000313|EMBL:CXI36173.1, ECO:0000313|Proteomes:UP000069549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K173 {ECO:0000313|EMBL:CXI36173.1,
RC ECO:0000313|Proteomes:UP000069549};
RG Pathogen Informatics;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; LT160028; CXI36173.1; -; Genomic_DNA.
DR SMR; A0A0Y9WA72; -.
DR VEuPathDB; PlasmoDB:PBANKA_0831000; -.
DR Proteomes; UP000069549; Chromosome 8.
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; PTHR47246; MUCIN-19; 1.
DR PANTHER; PTHR47246:SF1; MUCIN-19; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Merozoite {ECO:0000313|EMBL:CXI36173.1};
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..1789
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007079097"
FT TRANSMEM 1760..1786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1081..1609
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1681..1717
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..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1415
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 1584..1649
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1789 AA; 198427 MW; 7576D125FD86A3FE 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 ELEYFKKEKK
KESCNLSTSS CKKNKTSETI IPLNVRYPNG IGYPLPENDV YNKIANNAAE TTYGDLTNPD
NTPITEDLAT NEQARKNLIK AIKKKIEAEE KNLESLKTNY DNKLASFNQQ KAPFKEAAKL
FYESKFGNKL TSDIFEKFKT QRTEYMNKKT ELENCLYGNT KQLISKLNKQ LNYLQDYSLR
KDIISDEIEY FSNKKKGLQY NINRLAEAVQ AKQNILVASK DVPLSTLVEL QIQKSLLTKQ
IEQLNKTELS LRKAQLKDKV YVPKSYGNGG KPEPYYLIAV KREVDRLAQF IPKIENMIAK
EKEKTEQVPV VTGESEETSS VSTEVSVQAS SQSGTSSTVP AAGATSPTVT PVTEEAQSSQ
NAPPTTAATP ATTPEAATTA ATPATTPEAA TTSTTTSTTT STTTSTTTPV MTKLYYLEKL
QKFLVFSYSC HKYLLLQNST INKDALSKYA LTTEEDKIRT LKRCSELDIL LAIQNNMPTM
YSLYESIVDG LQNIYAELYE KEMMYHIYKL KDENPSIKSI LVKAGVIDPE PVASPPTPPT
PPTPPTPPTP PTLPTTPTPV TPAAPSEQTT TPEAATAASN PGASASETPA SNPGASASST
PSTPAAASNP GASASSTPST ASNPSAPASS TVQPTQVQPA APAAPAAVPA QPANSNGSIT
TRAESEEDIP ADDFELDNLY KSYLQRIDGN NTEFINFIKS KKELIKALTP EKVNQLYLEI
AHLKELSEHY YDRYYKYKLK LERLYEKHEQ IQVSNRQIRE LSILKARLLK RKQNINGIFY
ILSGYVNFFN KRREADKQYV DNALKNNDML LKYYKARIKY FTSEAVPLKT LTKASLDRET
NYLKIEKFRA YSRLELRFKK NINLGKEKIS YVSGGLYHVF EEFKELLKNK NYTGKTNPDT
VPEVTNAFEQ YKELLPKGVT ASASPAAATT PTSADAATQR ATPESGSGSG SGSVVSSTPE
EVARSGSGEN AVVSGSSVDD NDDDDIDQIA SGQSENAQEK NILEAFKNES EYLYARSLGI
TYKSLKKHMI REFSTIKEDM TTGLNNKLQK RNDFLEVLNH ELDLFKDLST NKYVIRNPYQ
LLDNDKKDKQ IVNLKYAAKG VNEDIETTAD GIKFFNKMIE LYKIQLAAVK EQIDAIEAAT
TDKDEKKKYV PIFEDLKGLY ETILGQSEEY IEVLQNRLDS YKNEKTEFEI LTKNLETYIK
IDEKLENFVE NAENNKHIAS IALNNLNKSG LVGEGESKKI LAKMLNMDSM DLLGIDPKHV
CINTRDIPAN AGCFRYDNGN EEWRCLLGYK KNNNTCIEDS NPTCGNNNGG CDPTAGCQTA
ENRENSKKII CTCKEPTPNA YYDGVFCSSS SFMGLSILLI ITLIVFNIF
//
