ID Q8I1L5_PLAVI Unreviewed; 1758 AA.
AC Q8I1L5;
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:AAN86228.1};
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:AAN86228.1};
RN [1] {ECO:0000313|EMBL:AAN86228.1}
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; AF435615; AAN86228.1; -; 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:AAN86228.1};
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..1758
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004307800"
FT TRANSMEM 1729..1754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1013..1583
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1653..1689
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 203..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1102..1168
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1547..1592
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 213..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1758 AA; 196665 MW; C0E736CC7EF88E25 CRC64;
MKALLFLFSF IFFVTKCQCE TESYKQLVAK LDKLEALVVD GYELFHKKKL GENDIKVETN
ASANNNNNNQ VSVLTSKIRN FLSKFLELQI PGHTDLLHLI RELAVEPNGI KYLVESYEEF
NQLMHVINFH YDLLRAKLHD MCAHDYCKIP EHLKITEKEL DMLKKVVLGY RKPLDNIKDD
IGKLEAFITK NKDTIKKISD LITEEHKKRS GHPTTTTNGA GTQPANGSIA AASSETTQIS
GSSNSGSTGH GSSNSGSTVT GSTVTGSTGT GSTGTGSTGN GQSPPATADA SSTNANYEAK
KIIYQAVYNT IFYTNQLQEA QKLIAVLEKR VKVLKEHKDI KVLLEKIATE KGKFPNNNLN
VENPTDEQKT AKSNIADLEK KIEAIAKTVN FDLDGLFTDA EELEYYLREK AKMAGTLIIP
ESTKSAGTPG NTVPTLKETY PHGISYALAE NSIYELIEKI GSDETFGDLQ NPDDGKQPKK
GILINETKRK ELLEKIMNKI KIEEDKLPNL KKEYEEKYKV YEEKVNEFKP AFNHFYEARL
DNTLVENKFD DFKKKREAYM EEKKKLESCS YEQNTNLINK LKKQLTYLED YVLRKDIADN
EIKHFSFMEW KLKSEIYDLA QEIRKNENKL TVENKFDFSG VVELQVQKVL IIKKIEALKN
VQNLLKNAKV KDDLYVPKVY KTGEKPEPYY LMVLKREIDK LKDFIPKIES MIATEKNKPT
VAAADIVAKG QSLRGASETG TTGNTVNAQT AVVQQPQHQV ANAVTVQPGT TGHQAQGGEA
ETQTNSVQAA QVQQTPAGAG GQVASTQTTS QAPAPNQASP EPAPAAPPST PAAAVAPAPT
MSKLEYLEKL LDFLKSAYAC HKHIFVTNST MKKELLDQYK LNADEQNKIK ENKCDELDLL
FNVQNNLPAM YSIYDSMSNE LQNLYIELYQ KEMVYNIYKN KDTDKKIKAF LETSNNKAAA
PAQSAAKPSG QAGTTPVTTT APVTTTTVTP SPQTSVVTST PPTPQAEENQ RVGGNSEEKP
EADTAQVEKF YEKHLSQIDK YNDYFKKFLE SKKEEIIKMD DTKWNALGKE IEELKKKLQV
SLDHYGKYKL KLERFLKKKN KISNSKDQIK KLTSLKNKLE RRQNLLNNPT SVLKNYTAFF
NKKRETEKKE VENTLKNTEI LLKYYKARAK YYIGEPFPLK TLSEESMQKE DNYLNLEKFR
VLSRLEGRLG KNIELEKENI SYLSSGLLHV LTELKEIIND KKYSGKDHAK NIAEVKKALQ
AYQELIPKVT SQESTSVAVT VPGAVVPGVP TAAAAGSGAS GAVPPAGGPS PPATGPGAAA
GSTEENVAAK AQDYAEDYDK VIALPLFGNN DDDGEEDQVT TGEAESEAPE ILVPAGISDY
DVVYLKPLAG MYKTIKKQLE NHVNAFNTNI TDMLDSRLKK RNYFLEVLNS DLNPFKYSSS
GEYIIKDPYK LLDLEKKKKL IGSYKYIGAS IDMDLATAND GVAYYNKMEE LYKTHLTAVN
AQIKKVEDDI KAEDDKIKKI GSDSTKTTEK TQSMAKKAEL EKYLPFLNSL QKEYESLVSK
VNTYTDNLKK VINNCQLEKK EAEITVKKLQ DYNKMDEKLE EYKKSEKKNE VKSSGLLEKL
MKSKLIKENE SKEILSQLLN VQTQLLTMSS EHTCIDTNVP DNAACYRYLD GTEEWRCLLT
FKEEGGKCVP ASNVTCKDNN GGCAPEAECK MTDSNKIVCK CTKEGSEPLF EGVFCSSSSF
LSLSFLLLML LFLLCMEL
//
