ID Q8I1K9_PLAVI Unreviewed; 1699 AA.
AC Q8I1K9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AAN86240.1};
OS Plasmodium vivax (malaria parasite P. vivax).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5855 {ECO:0000313|EMBL:AAN86240.1};
RN [1] {ECO:0000313|EMBL:AAN86240.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12466500; DOI=10.1073/pnas.252348999;
RA Putaporntip C., Jongwutiwes S., Sakihama N., Ferreira M.U., Kho W.G.,
RA Kaneko A., Kanbara H., Hattori T., Tanabe K.;
RT "Mosaic organization and heterogeneity in frequency of allelic
RT recombination of the Plasmodium vivax merozoite surface protein-1 locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16348-16353(2002).
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; AF435630; AAN86240.1; -; Genomic_DNA.
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; PTHR48125; LP07818P1; 1.
DR PANTHER; PTHR48125:SF10; RNA POLYMERASE II-ASSOCIATED FACTOR 1 HOMOLOG; 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:AAN86240.1};
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..1699
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004307921"
FT TRANSMEM 1670..1695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 961..1524
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1594..1630
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 208..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 288..315
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 339..366
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1050..1116
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1437..1533
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 211..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1699 AA; 192023 MW; 3557E4C3F2E519D6 CRC64;
MKALLFLFSF IFFVTKCQCE TESYKQLVAK LDKLEALVVD GYELFHKKKL GENDIKVDAN
ANNNNNNQVS VLTSKIRNFV GKFLELQIPG HTDLLHLIRE LAFEPNGIKY LVESYEEFNQ
LMHVINFHYD LLRAKLHDMC AHDYCKIPEH LKITEKELDM LKKVVLGYRK PLDNIKDDIG
KLEAFITKNK KTIDNINKLI SDENAKRGGQ YTDMINGNGT QADGTQGTTG SSETTQNSGS
SGTGSSDSGS SGTGSTGNIS HPAAPAASSP TDENYTNKKA IFQAVYNIIF YTNLKEEAQK
LIEVLEKRVK VLKEHKDIKV LLEQIAKEKE NLPKDNTTTT TLTAEQKAAQ SKIADLEKKI
VDIAKTVNFD LDGLFTNAEE LEYYLREKAK MAGTLIIPES TKSAGTPGKT VPTLKETYPH
GISYALAENS IYELIEKIGS DETFGDLQNP DDGKQPKKET IANEIKRKEL LEKIMNKIKI
EEDKLPDLKK EYEEKYTVYE QKVKEFQPEF NHFYEARLDN TLVGEKFGEF KKKREEYMKE
KKKLESCSYE QNTNLINKLK KQLTYLEDYV LRKDIADDEI KHFSFMEWKL KSEIYDLAQE
IRKNENKLTV ENKFDFSGVV ELQVQKVLII KKIEALKNVQ NLLKNAKVKD DLYVPKVYKT
GEKPEPYYLM VLKREIDKLK DFIPKIESMI ATEKAKPAAS APVTSGQLLR GSSEAATEVT
TNAVTSEVQQ QQQQQQQQQQ QQQSQVVPAP AGDAQQVIST QPTSQSAAPG VSATPAPTPA
AAAAPAPAMS KLEYLEKLLD FLKSAYACHK HIFVTNSTMD KKLLKEYELN ADEKTKINQN
KCDELDLLFN VQNNLPAMYS IYDSMSNELQ NLYIELYQKE MVYNIYKNKD TDKKIKAFLE
TSNNKAAAPA QSAAKPSGQA GTTPVTTTAP VTTTTVTPSP QTSVVTNTPP TPQAEENQRV
GGNSEEKPEA DTAQVEKFYE KHLSQIDKYN DYFKKFLESK KEEIIKMDDT KWNALGKEIE
ELKKKLQVSL DHYGKYKLKL ERFLKKKNKI SNSKDQIKKL TSLKNKLERR QNLLNNPTSV
LKNYTAFFNK KRETEKKEVE NTLKNTEILL KYYKARAKYY IGEPFPLKTL SEESMQKEDN
YLNLEKFRVL SRLEGRLGKN IELEKENISY LSSGLHHVLT ELKEIIKNKK YSGNDHTKNI
AAVKEALQAY QELIPKVTTQ ESTSVAVTVP GAVVPGVPTA AAAGSGASGA VPPATGPGAA
AGSTEENVAA KAQDYAEDYD KVIALPLFGN NDDDWEEDQV TTGEAESEEP EILVPAGISD
YDVVYLKPLA GMYKTIKKQL ENHVNAFNTN ITDMLDSRLK KRNYFLEVLN SDLNPFKYSS
SGEYIIKDPY KLLDLEKKKK LLGSYKYIGA SIDKDLATAN DGVAYYNKME ELYKTHLTAV
NAQIKKVEDD IKKQDEELKK IENEANKTAE KAKFTAKKAE LEKYLPFLNS LQKEYESLVS
KVNTYTDNLK KVINNCQLEK KEAEITVKKL QDYNKMDEKL EEYKKSEKKN EVKSSGLLER
LMKSKLIKEN ESKEILSQLL NVQTQLLTMS SEHTCIDTNV PDNAACYRYL DGTEEWRCLL
TFKEEGGKCV PASNVTCKDN NGGCAPEAEC KMTDSNKIVC KCTKEGSEPL FEGVFCSSSS
FLSLSFLLLM LLFLLCMEL
//
