MSP1_PLAFW
ID MSP1_PLAFW Reviewed; 1639 AA.
AC P04933;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Merozoite surface protein 1;
DE AltName: Full=Merozoite surface antigens;
DE AltName: Full=PMMSA;
DE AltName: Full=p195;
DE Flags: Precursor;
GN Name=MSP-1;
OS Plasmodium falciparum (isolate Wellcome).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5848;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2995820; DOI=10.1038/317270a0;
RA Holder A.A., Lockyer M.J., Odink K.G., Sandhu J.S., Riveros-Moreno V.,
RA Nicholls S.C., Hillman Y., Davey L.S., Tizard M.L.V., Schwarz R.T.,
RA Freeman R.R.;
RT "Primary structure of the precursor to the three major surface antigens of
RT Plasmodium falciparum merozoites.";
RL Nature 317:270-273(1985).
RN [2]
RP SEQUENCE REVISION.
RA Holder A.A.;
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR OF 1526-1621, AND DISULFIDE BONDS.
RX PubMed=10339410; DOI=10.1006/jmbi.1999.2753;
RA Morgan W.D., Birdsall B., Frenkiel T.A., Gradwell M.G., Burghaus P.A.,
RA Syed S.E., Uthaipibull C., Holder A.A., Feeney J.;
RT "Solution structure of an EGF module pair from the Plasmodium falciparum
RT merozoite surface protein 1.";
RL J. Mol. Biol. 289:113-122(1999).
RN [4]
RP STRUCTURE BY NMR OF 1526-1573, AND DISULFIDE BONDS.
RX PubMed=17068840; DOI=10.1002/cbic.200600357;
RA James S., Moehle K., Renard A., Mueller M.S., Vogel D., Zurbriggen R.,
RA Pluschke G., Robinson J.A.;
RT "Synthesis, solution structure and immune recognition of an epidermal
RT growth factor-like domain from Plasmodium falciparum merozoite surface
RT protein-1.";
RL ChemBioChem 7:1943-1950(2006).
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; X02919; CAA26676.1; -; mRNA.
DR PIR; A24594; A24594.
DR PIR; S05603; S05603.
DR PDB; 1CEJ; NMR; -; A=1526-1621.
DR PDB; 2FLG; NMR; -; A=1526-1573.
DR PDB; 2MU7; NMR; -; A=42-61.
DR PDB; 2MUE; NMR; -; A=1282-1301.
DR PDBsum; 1CEJ; -.
DR PDBsum; 2FLG; -.
DR PDBsum; 2MU7; -.
DR PDBsum; 2MUE; -.
DR AlphaFoldDB; P04933; -.
DR BMRB; P04933; -.
DR SMR; P04933; -.
DR ABCD; P04933; 14 sequenced antibodies.
DR EvolutionaryTrace; P04933; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Malaria; Membrane; Merozoite; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1618
FT /note="Merozoite surface protein 1"
FT /id="PRO_0000024561"
FT PROPEP 1619..1639
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024562"
FT REGION 58..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1618
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1058
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1532..1543
FT DISULFID 1537..1553
FT DISULFID 1555..1566
FT DISULFID 1574..1587
FT DISULFID 1581..1601
FT DISULFID 1603..1617
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2MU7"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2MU7"
FT TURN 1283..1285
FT /evidence="ECO:0007829|PDB:2MUE"
FT HELIX 1286..1296
FT /evidence="ECO:0007829|PDB:2MUE"
FT TURN 1297..1300
FT /evidence="ECO:0007829|PDB:2MUE"
FT STRAND 1541..1546
FT /evidence="ECO:0007829|PDB:1CEJ"
FT TURN 1547..1549
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1550..1555
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1559..1562
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1565..1568
FT /evidence="ECO:0007829|PDB:1CEJ"
FT TURN 1575..1577
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1578..1581
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1585..1588
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1594..1596
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1600..1602
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1605..1607
FT /evidence="ECO:0007829|PDB:1CEJ"
FT STRAND 1611..1616
FT /evidence="ECO:0007829|PDB:1CEJ"
SQ SEQUENCE 1639 AA; 187619 MW; 2C255B6616C87F6E CRC64;
MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFQKEK MVLNEGTSGT
AVTTSTPGSK GSVASGGSGG SVASGGSVAS GGSVASGGSV ASGGSGNSRR TNPSDNSSDS
DAKSYADLKH RVRNYLLTIK ELKYPQLFDL TNHMLTLCDN IHGFKYLIDG YEEINELLYK
LNFYFDLLRA KLNDVCANDY CQIPFNLKIR ANELDVLKKL VFGYRKPLDN IKDNVGKMED
YIKKNKKTIE NINELIEESK KTIDKNKNAT KEEEKKKLYQ AQYDLSIYNK QLEEAHNLIS
VLEKRIDTLK KNENIKELLD KINEIKNPPP ANSGNTPNTL LDKNKKIEEH EKEIKEIAKT
IKFNIDSLFT DPLELEYYLR EKNKNIDISA KVETKESTEP NEYPNGVTYP LSYNDINNAL
NELNSFGDLI NPFDYTKEPS KNIYTDNERK KFINEIKEKI KIEKKKIESD KKSYEDRSKS
LNDITKEYEK LLNEIYDSKF NNNIDLTNFE KMMGKRYSYK VEKLTHHNTF ASYENSKHNL
EKLTKALKYM EDYSLRNIVV EKELKYYKNL ISKIENEIET LVENIKKDEE QLFEKKITKD
ENKPDEKILE VSDIVKVQVQ KVLLMNKIDE LKKTQLILKN VELKHNIHVP NSYKQENKQE
PYYLIVLKKE IDKLKVFMPK VESLINEEKK NIKTEGQSDN SEPSTEGEIT GQATTKPGQQ
AGSALEGDSV QAQAQEQKQA QPPVPVPVPE AKAQVPTPPA PVNNKTENVS KLDYLEKLYE
FLNTSYICHK YILVSHSTMN EKILKQYKIT KEEESKLSSC DPLDLLFNIQ NNIPVMYSMF
DSLNNSLSQL FMEIYEKEMV CNLYKLKDND KIKNLLEEAK KVSTSVKTLS SSSMQPLSLT
PQDKPEVSAN DDTSHSTNLN NSLKLFENIL SLGKNKNIYQ ELIGQKSSEN FYEKILKDSD
TFYNESFTNF VKSKADDINS LNDESKRKKL EEDINKLKKT LQLSFDLYNK YKLKLERLFD
KKKTVGKYKM QIKKLTLLKE QLESKLNSLN NPKHVLQNFS VFFNKKKEAE IAETENTLEN
TKILLKHYKG LVKYYNGESS PLKTLSEESI QTEDNYASLE NFKVLSKLEG KLKDNLNLEK
KKLSYLSSGL HHLIAELKEV IKNKNYTGNS PSENNTDVNN ALESYKKFLP EGTDVATVVS
ESGSDTLEQS QPKKPASTHV GAESNTITTS QNVDDEVDDV IIVPIFGESE EDYDDLGQVV
TGEAVTPSVI DNILSKIENE YEVLYLKPLA GVYRSLKKQL ENNVMTFNVN VKDILNSRFN
KRENFKNVLE SDLIPYKDLT SSNYVVKDPY KFLNKEKRDK FLSSYNYIKD SIDTDINFAN
DVLGYYKILS EKYKSDLDSI KKYINDKQGE NEKYLPFLNN IETLYKTVND KIDLFVIHLE
AKVLNYTYEK SNVEVKIKEL NYLKTIQDKL ADFKKNNNFV GIADLSTDYN HNNLLTKFLS
TGMVFENLAK TVLSNLLDGN LQGMLNISQH QCVKKQCPQN SGCFRHLDER EECKCLLNYK
QEGDKCVENP NPTCNENNGG CDADAKCTEE DSGSNGKKIT CECTKPDSYP LFDGIFCSSS
NFLGISFLLI LMLILYSFI
