ID Q8I1K8_PLAVI Unreviewed; 1752 AA.
AC Q8I1K8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:AAN86242.1};
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:AAN86242.1};
RN [1] {ECO:0000313|EMBL:AAN86242.1}
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}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AF435632; AAN86242.1; -; 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; PTHR47246; MUCIN-19; 1.
DR PANTHER; PTHR47246:SF1; MUCIN-19; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Merozoite {ECO:0000313|EMBL:AAN86242.1};
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..1752
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004310623"
FT TRANSMEM 1723..1748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1007..1577
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1647..1683
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 207..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1096..1162
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1490..1517
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 762..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..828
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1752 AA; 195850 MW; 41F4162B295C4572 CRC64;
MKALLFLFSF IFFVTKCQCE TESYKQLVAK LDKLEALVVD GYELFHKKKL GENDIKVDAN
ANNNNNNQVS VLTSKIRNFV SKFLELQIPG HTDLLHLIRE LAVEPNGIKY LVESYEEFNQ
LMHVINFHYD LLRAKLHDMC AHDYCKIPEH LKISDKELDM LKKVVLGYRK PLDNIKDDIG
KLETFITKNK ITIKNISDLI IAENKKRSGH PTTTTNGAGT QPANGSFPAA SSETTQISGS
SNSGSTGHGS SGTGSSGTGS SNSGSTGHGS TGNGQSPPAP AAPSSTNANY EAKKIIYQAM
YNGIFYTNQL EEAQKLIAVL EKRVKVLKEH KGIKALLEQV EAEKKKLPKD NTTNTPLTDE
QQKAAQKKIA DLESQIVAIA KTVNFDLDGL FTDAEELEYY LREKAKMAGT LIIPESTKSA
GTPGKTVPTL KETYPHGISY ALAENSIYEL IEKIGSDETF GDLQNPDDGK QPKKGILINE
TKRKELLEKI MNKIKIEEDK LPNLKKEYEE KYKVYEAKVN EFKPAFNHFY EARLDNTLVE
NKFDEFKTKR EAYMEEKKKL ESCSYEQNAN LINKLKKQLT YLEDYVLRKD IADDEIKHFS
FMEWKLKSEI YDLAQEIRKN ENKLTVENKF DFSGVVELQV QKVLIIKKIE ALKNVQNLLK
NAKVKDDLYI PKVYKTGEKP EPYYLMVLKR EIDKLKDFIP KIESMIATEK NKPTVAAADI
VAKGQSLRGA SETGTTGNTV NAQTAVVQQP QHQVANAVTV QPGTTGHQAQ GGEAETQTNS
VQAAQVQQTP AGAGGQVAST QTISQAPAPT QASPEPAPAA PPSTPAAAVA PAPTMSKLEY
LQKLLDFLKS AYACHKHIFV TNSTMKKELL DQYKLNADEQ NKIKENKCDE LDLLFNVQNN
LPAMYSIYDS MSSELQNLYI ELYQKEMVYN IYKNKDTDKK IKAFLETSNN KAAAPAQSAA
KPSGQAGTTP VTTTAPVTTT TVTPSPQTSV VTSTPPTPQA EENQRVGGNS EEKPEADTAQ
VEKFYEKHLS QIDKYNDYFK KFLESKKEEI IKMDDTKWNA LGKEIEELKK KLQVSLDHYG
KYKLKLERFL KKKNKISNSK DQIKKLTSLK NKLERRQNLL NNPTSVLKNY TAFFNKKRET
EKKEVENTLK NTEILLKYYK ARAKYYIGEP FPLKTLSEES MQKEDNYLNL EKFRVLSRLE
GRLGKNIELE KENISYLSSG LLHVLTELKE IINDKKYSGK DHAKNIAEVK KALQAYQELI
PKVTSQESTS VAVTVPGAVV PGVPTAAAAG SGASGAVPPA GGPSPPATGP GAAAGSTEEN
VAAKAQDYAE DYDKVIALPL FGNNDDDGEE DQVTTGEAES EAPEILVPAG ISDYDVVYLK
PLAGMYKTIK KQLENHVNAF NTNITDMLDS RLKKRNYFLE VLNSDLNPFK YSSSGEYIIK
DPYKLLDLEK KKKLIGSYKY IGASIDKDLA TANDGVAYYN KMGELYKTHL DGVKTEIKKV
EDDIKTHDEK LQKLGSEVSQ NSEKTQLNAK KAELEKYLPF LNSLQKEYES LVSKVNTYTD
NLKKVISNCQ LEKKEAEITV KKLQDYNKMD EKLEEYKKSE KKNEVKSSGL LEKLMKSKLI
KENESKEILS QLLNVQTQLL TMSSEHTCID TNVPDNAACY RYLDGTEEWR CLLTFKEEGG
KCVPASNVTC KDNNGGCAPE AECKMTDSNK IVCKCTKEGS EPLFEGVFCS SSSFLSLSFL
LLMLLFLLCM EL
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