MSP1_PLAYO
ID MSP1_PLAYO Reviewed; 1772 AA.
AC P13828; Q6LEJ9; Q7RCN0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Merozoite surface protein 1;
DE AltName: Full=230 kDa merozoite surface antigen;
DE Short=Py230;
DE AltName: Full=Merozoite surface antigens;
DE AltName: Full=PMMSA;
DE Flags: Precursor;
GN Name=MSP-1; ORFNames=PY05748;
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YM;
RX PubMed=2797063; DOI=10.1016/0166-6851(89)90175-8;
RA Lewis A.P.;
RT "Cloning and analysis of the gene encoding the 230-kilodalton merozoite
RT surface antigen of Plasmodium yoelii.";
RL Mol. Biochem. Parasitol. 36:271-282(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 454-1094.
RX PubMed=2797064; DOI=10.1016/0166-6851(89)90176-x;
RA Daly T.M., Burns J.M. Jr., Long C.A.;
RT "Precursor to the major merozoite surface antigen of Plasmodium yoelii:
RT cloning and sequencing of the middle 1.9 kb region.";
RL Mol. Biochem. Parasitol. 36:283-285(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1093-1772.
RC STRAIN=17XL;
RX PubMed=2448778; DOI=10.1073/pnas.85.2.602;
RA Burns J.M. Jr., Daly T.M., Vaidya A.B., Long C.A.;
RT "The 3' portion of the gene for a Plasmodium yoelii merozoite surface
RT antigen encodes the epitope recognized by a protective monoclonal
RT antibody.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:602-606(1988).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
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; J04668; AAA29702.1; -; Genomic_DNA.
DR EMBL; AABL01001865; EAA17822.1; -; Genomic_DNA.
DR EMBL; J03975; AAA29486.1; -; Genomic_DNA.
DR EMBL; J03612; AAA29762.1; -; Genomic_DNA.
DR PIR; A28121; A28121.
DR PIR; A45532; A45532.
DR RefSeq; XP_726257.1; XM_721164.1.
DR PDB; 2MGP; NMR; -; A=1656-1754.
DR PDB; 2MGR; NMR; -; A=1656-1754.
DR PDBsum; 2MGP; -.
DR PDBsum; 2MGR; -.
DR AlphaFoldDB; P13828; -.
DR BMRB; P13828; -.
DR SMR; P13828; -.
DR STRING; 73239.P13828; -.
DR EnsemblProtists; EAA17822; EAA17822; EAA17822.
DR GeneID; 3791597; -.
DR KEGG; pyo:PY17X_0834400; -.
DR InParanoid; P13828; -.
DR OMA; TEEWRCL; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
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; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1751
FT /note="Merozoite surface protein 1"
FT /id="PRO_0000024563"
FT PROPEP 1752..1772
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024564"
FT REGION 290..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1751
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1663..1675
FT /evidence="ECO:0000250"
FT DISULFID 1687..1699
FT /evidence="ECO:0000250"
FT DISULFID 1707..1720
FT /evidence="ECO:0000250"
FT DISULFID 1714..1734
FT /evidence="ECO:0000250"
FT DISULFID 1736..1750
FT /evidence="ECO:0000250"
FT CONFLICT 1521
FT /note="L -> V (in Ref. 4; AAA29762)"
FT /evidence="ECO:0000305"
FT STRAND 1673..1677
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1679..1681
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1683..1687
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1691..1693
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1695..1697
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1699..1701
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1707..1709
FT /evidence="ECO:0007829|PDB:2MGR"
FT HELIX 1710..1713
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1718..1722
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1726..1728
FT /evidence="ECO:0007829|PDB:2MGP"
FT TURN 1729..1731
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1732..1736
FT /evidence="ECO:0007829|PDB:2MGP"
FT STRAND 1742..1744
FT /evidence="ECO:0007829|PDB:2MGP"
FT TURN 1745..1748
FT /evidence="ECO:0007829|PDB:2MGP"
SQ SEQUENCE 1772 AA; 197231 MW; 9A6291658EB0F45D CRC64;
MKVIGLLFSF VFFAIKCKSE TIEVYNDLIQ KLEKLESLSV DGLELFQKSQ VIINATQPTE
TIDPFTNHNF AQQVQDFVTK FEGLGFTEQT ELVNLIKALT PNRYGVKYLI ESKEEFNGLM
HAINFYYDVL RDKLNDMCAN NYCEIPEHLK ISEEETEMLK KVILGYRKPI ENIQDDIEKL
EIYIERNKET VAALNALIAE ETKKIQPEGN EDCNDASCDS DKYNKKKPIY QAMYNVIFYK
KQLAEIQKVV EVLEKRVSTL KKNDAIKPLW QQIEVLNAAP VVTAETQIVT GGQSSTEPGS
GGSSASGTSS SGQASAGTGV EQANTVASVT VTPSVGQNGE ASTNPQTAQV QPVPTLTLEE
KQKKIAGLYA QIKEIAKTIK FNLEGIFVDP IELEYFKKEK KKESCNLSTS SCKKNKASET
IIPLTIRYPN GISYPLPEND VYNKIANNAA ETTYGDLTHP DNTPLTGDLA TNEQARKDLI
KAIKKKIKAE EKKLETLKTN YDNKLTEFNQ QKTPFKEAAK EFYESKFRNK LTSEIFEKFK
TKRDEYMTKK TELNTCEYGN TKELINKLNK QLNYLQDYSL RKDIISNEIE YFSNKKKELQ
YNINRLAEAV QAKQNVLVAS KDVPLSTLVE LQIQKSLLTK QIEQLNKTEV SLNKAQLKDK
LYVPKTYGNE GKPEPYYLIA VKKEVDRLAQ FIPKIESMIA KEKERMEQGP AITGESEEVP
SGPSAESSTD RSTQSSTSSS SSSSSTPAAA ESSSATLPEA PAPAEAASPS TEASEETTIP
PTTQETQPSQ AASSTTPAKP VMTKLYYLEK LQKFLVFSYS CHKYVLLQNS TINKDALSKY
ALTSEEDKIR TLKRCSELDV LLAIQNNMPT MYSLYESIVD GLQNIYTELY EKEMMYHIYK
LKDENPSIKS LLVKAGVIEP EPVAAPTPVT PAATEQQQQQ ATPDVQSDAP APSDVSQQPE
TPVTSTTPEV TTSTEASSSA PGEGTPSGEA GASGTEGATA SNAATPAGTS ASGSAASNAS
TTSDVTPPAA AAAVPSTSTP APAQPPAANS QSGNPDSGIR SRAESEEDMP ADDFELDNLY
KSYLQQIDGN NTEFINFIKS KKELIKALTP EKVNQLYLEI AHLKELSEHY YDRYSTYKLK
LERLYNKHEQ IQLTNRQIRD LSILKARLLK RKQTLNGVFY ILNGYVNFFN KRREAEKQYV
DNALKNTDML LKYYKARTKY FTSEAVPLKT LSKASLDRES NYLKIEKFRA YSRLELRLKK
NINLGKERIS YVSGGLHHVF EEFKELIKDK DYTGKKNPDN APEVTNAFEQ YKELLPKGVT
VSTPAVAVTT TLAADAPATP EGAVPGAVPG AVPGAVPGAV PGAVPGSGTD TRVAGSSVDD
NEDDDIYQIA SGQSEDAPEK DILSEFTNES LYVYTKRLGS TYKSLKKHML REFSTIKEDM
TNGLNNKSQK RNDFLEVLSH ELDLFKDLST NKYVIRNPYQ LLDNDKKDKQ IVNLKYATKG
INEDIETTTD GIKFFNKMVE LYNTQLAAVK EQIATIEAET NDTNKEEKKK YIPILEDLKG
LYETVIGQAE EYSEELQNRL DNYKNEKAEF EILTKNLEKY IQIDEKLDEF VEHAENNKHI
ASIALNNLNK SGLVGEGESK KILAKMLNMD GMDLLGVDPK HVCVDTRDIP KNAGCFRDDN
GTEEWRCLLG YKKGEGNTCV ENNNPTCDIN NGGCDPTASC QNAESTENSK KIICTCKEPT
PNAYYEGVFC SSSSFMGLSI LLIITLIVFN IF
