ID D5I777_PLAVI Unreviewed; 1743 AA.
AC D5I777;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
DE Flags: Fragment;
GN Name=msp-1 {ECO:0000313|EMBL:ADF48572.1};
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:ADF48572.1};
RN [1] {ECO:0000313|EMBL:ADF48572.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSY535 {ECO:0000313|EMBL:ADF48572.1};
RX PubMed=20199765; DOI=10.1016/j.vaccine.2010.02.062;
RA Jongwutiwes S., Putaporntip C., Hughes A.L.;
RT "Bottleneck effects on vaccine-candidate antigen diversity of malaria
RT parasites in Thailand.";
RL Vaccine 28:3112-3117(2010).
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; GQ890903; ADF48572.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PVP01_0728900; -.
DR VEuPathDB; PlasmoDB:PVW1_070035600; -.
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:ADF48572.1};
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..1743
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003073256"
FT TRANSMEM 1714..1739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 996..1568
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1638..1674
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 209..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 342..369
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1075..1151
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1481..1552
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 212..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..814
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1743
FT /evidence="ECO:0000313|EMBL:ADF48572.1"
SQ SEQUENCE 1743 AA; 195541 MW; CCC519FBC3E6D67D CRC64;
MKALLFLFSF IFFVTKCQCE TESYKQLVAK LDKLEALVVD GYELFHKKKL GESDIQVETN
ASANNNNNNQ VSVLASKIRN FLSKFLELQI PGHTDLLHLI RELAVEPNGI KYLVESYEEF
NQLMHVINFH YDLLRAKLHD MCAHDYCKIP EHLKISDKEL DMLKKVVLGY RKPLDNIKDD
IGKLEAFITK NKDTIKKISD LITEEHKKRG GQYTSTISGN GAQTDGHQTT TASSETSSGS
SVSSVSGSSN SGSSATGSTG NRSSSQARAD SRSTDTDYNA KKIIFQAVYN TIFYTNQLQE
AQKLIAVLEK RVKVLKEHKD IKVLLEQVAK EKEKLPKDNT TTTTLTAEQK AAQSKIAELE
KKIEAIAKTV NFDLDGLFTD AEELEYYLRE KAKMAGTLII PESTKSAGTP GKTVPTLKET
YPHGISYALA ENSIYELIEK IGSDETFGDL QNPDDGKQPK KGILINETKR KELLEKIMNK
IKIEEDKLPN LKKEYEEKYK VYEEKVNEFK PAFNHFYEAR LDNTLVENKF DDFKKKREAY
MEEKKKLESC SYEQNTNLIN KLKKQLTYLE DYVLRKDIAD DEIKHFSFME WKLKSEIYDL
AQEIRKNENK LTIENKFDFS GVVELQVQKV LIIKKIEALK NVQNLLKNAK VKDDLYVPKV
YKTGEKPEPY YLMVLKREID KLKDFIPKIE SMIATEKNKP TVAAADIVAK GQSLRGASET
GTTGNTVNAQ TAVVQPQHQV ANAVTVQPGT TGHQAQGGEA ETQTNSVQAA QVQQTPAGAG
GQVASTQTTS QAPAPNQASP EPAPAAPPST PAAAVAPAPT MSKLEYLEKL LDFLKSAYAC
HKHIFVTNST MKKELLDQYK LNADEQNKIK ENKCDELDLL FNVQNNLPAM YSIYDSMSSE
LQNLYIELYQ KEMVYNIYKN KDTDMKLKAF LETLKSKAAA AGPAKPAAKP IGQAVVPQVA
PPTPVVAPNS GNTATPVTTN TTVSPGTQAE ENQRVGGNSE EKPEADTAQV EKFYEKHLSQ
IDKYNDYFKK FLESKKEEII KMDDTKWNAL GKEIEELKKK LQVSLDHYGK YKLKLERLLK
KKNKISNSKD QIKKLTSLKN KLERRQNLLN NPTSVLKNYT AFFNKKRETE KKEVENTLKN
TEILLKYYKA RAKYYIGEPF PLKTLSEESM QKEDNYLNLE KFRVLSRLEG RLGKNIELEK
ENISYLSSGL LHVLTELKEI INDKKYSGKD HAKNIAEVKK ALQAYQELIP KVTSQESTSV
AVTVPGAVVP GVPTAAAAGS GASGAVPPAG GPSPPATGGV VPGVVESAEA QTKAQAQDYA
EDYDKVIALP LFGNNDDDGE EDQVTTGEAE SEAPEILVPA GISDYDVVYL KPLAGMYKTI
KKQLENHVNA FNTNITDMLD SRLKKRNYFL EVLNSDLNPF KYSSSGEYII KDPYKLLDLE
KKKKLIGSYK YIGASIDMDV ATANDGVAYY NKMEELYKTH LTAVNAQIKK VEADIKAEDD
KIKKIENEAN KAAEKTQSMA KKAELEKYLP FLNSLQKEYE SLVSKVNTYT DNLKKVISNC
QLEKKEAEIT VKKLQDYNKM DEKLEEYKKS EKKNEVKSSG LLEKLMKSKL IKENESKEIL
SQLLNVQTQL LTMSSEHTCI DTNVPDNAAC YRYLDGTEEW RCLLTFKEEG GKCVPASNVT
CKDNNGGCAP EAECKMTDSN KIVCKCTKEG SEPLFEGVFC SSSSFLSLSF LLLMLLFLLC
MEL
//
