ID   MSP1_PLAFF              Reviewed;        1701 AA.
AC   P13819;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Merozoite surface protein 1;
DE   AltName: Full=Merozoite surface antigens;
DE   AltName: Full=PMMSA;
DE   Flags: Precursor;
GN   Name=MSP-1;
OS   Plasmodium falciparum (isolate FC27 / Papua New Guinea).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2449612; DOI=10.1016/0166-6851(88)90049-7;
RA   Peterson M.G., Coppel R.L., McIntyre P., Langford C.J., Woodrow G.,
RA   Brown G.V., Anders R.F., Kemp D.J.;
RT   "Variation in the precursor to the major merozoite surface antigens of
RT   Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 27:291-302(1988).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- PTM: Merozoite surface antigen contain the sequence of 83 kDa, 42 kDa
CC       and 19 kDa antigens which are the major surface antigens of merozoites.
CC       The maturation take place during schizont.
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DR   EMBL; M19143; AAA29653.1; -; mRNA.
DR   PIR; A54498; A54498.
DR   AlphaFoldDB; P13819; -.
DR   BMRB; P13819; -.
DR   SMR; P13819; -.
DR   PRIDE; P13819; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR010901; MSP1_C.
DR   InterPro; IPR024730; MSP1_EGF_1.
DR   Pfam; PF12946; EGF_MSP1_1; 1.
DR   Pfam; PF07462; MSP1_C; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Malaria; Membrane; Merozoite; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1680
FT                   /note="Merozoite surface protein 1"
FT                   /id="PRO_0000024550"
FT   PROPEP          1681..1701
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024551"
FT   REGION          89..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1231..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1451..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1239..1259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1680
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        802
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        899
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        919
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        965
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        991
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1089
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1588
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1594..1605
FT                   /evidence="ECO:0000250"
FT   DISULFID        1599..1615
FT                   /evidence="ECO:0000250"
FT   DISULFID        1617..1628
FT                   /evidence="ECO:0000250"
FT   DISULFID        1636..1649
FT                   /evidence="ECO:0000250"
FT   DISULFID        1643..1663
FT                   /evidence="ECO:0000250"
FT   DISULFID        1665..1679
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1701 AA;  193720 MW;  3920B75E73D38552 CRC64;
     MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFQKEK MVLNEGTSGT
     AVTTSTPGSS GSVTSGGSVA SVASVASGGS GGSVASGGSG NSRRTNPSDN SSDSNTKTYA
     DLKHRVQNYL FTIKELKYPE LFDLTNHMLT LSKNVDGFKY LIDGYEEINE LLYKLNFYYD
     LLRAKLNDAC ANSYCQIPFN LKIRANELDV LKKIVFGYRK PLDNIKDNVG KMEDYIKKNK
     TTIANINELI EGSKKTIDQN KNADNEEGKK KLYQAQYNLF IYNKQLQEAH NLISVLEKRI
     DTLKKNENIK KLLEDIDKIK TDAENPTTGS KPNPLPENKK KEVEGHEEKI 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 VTEETVGHTT TVTITLPPKE ESAPKEVKVV ENSIEHKSND NSQALTKTVY
     LKKLDEFLTK SYICHKYILV SNSSMDQKLL EVYNLTPEEE NELKSCDPLD LLFNIQNNIP
     AMYSLYDSMN IDLQHLFFEL YQKEMIYYLH KLKEENHIKK LLEEQKQITG TSSTSSPGNT
     TVNTAQSATH SNSQNQQSNA SSTNTQNGVA VSSGPAVVEE SHDPLTVLSI SNDLKGIVSL
     LNLGNKTKVP NPLTISTTEM EKFYENILKN NDTYFNDDIK QFVKSNSKVI TGLTETQKNA
     LNDEIKKLKD TLQLSFDLYN KYKLKLDRLF NKKKELGQDK MQIKKLTLLK EQLESKLNSL
     NNPHNVLQNF SVFFNKKKEA EIAETENTLE NTKILLKHYK GLVKYYNGES SPLKTLSEVS
     IQTEDNYANL EKFRALSKID GKLNDNLHLG KKKLSFLSSG LHHLITELKE VIKNKNYTGN
     SPSENNKKVN EALKSYENFL PEAKVTTVVT PPQPDVTPSP LSVRVSGSSG STKEETQIPT
     SGSLLTELQQ VVQLQNYDEE DDSLVVLPIF GESEDNDEYL DQVVTGEAIS VTMDNILSGF
     ENEYDVIYLK PLAGVYRSLK KQIEKNIITF NLNLNDILNS RLKKRKYFLD VLESDLMQFK
     HISSNEYIIE DSFKLLNSEQ KNTLLKSYKY IKESVENDIK FAQEGISYYE KVLAKYKDDL
     ESIKKVIKEE KEKFPSSPPT TPPSPAKTDE QKKESKFLPF LTNIETLYNN LVNKIDDYLI
     NLKAKINDCN VEKDEAHVKI TKLSDLKAID DKIDLFKNTN DFEAIKKLIN DDTKKDMLGK
     LLSTGLVQNF PNTIISKLIE GKFQDMLNIS QHQCVKKQCP ENSGCFRHLD EREECKCLLN
     YKQEGDKCVE NPNPTCNENN GGCDADATCT EEDSGSSRKK ITCECTKPDS YPLFDGIFCS
     SSNFLGISFL LILMLILYSF I