ID D7P392_PLAVI Unreviewed; 1744 AA.
AC D7P392;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ADF48816.1};
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:ADF48816.1};
RN [1] {ECO:0000313|EMBL:ADF48816.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BSN9 {ECO:0000313|EMBL:ADF48816.1};
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; GQ890949; ADF48816.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PVP01_0728900; -.
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:ADF48816.1};
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..1744
FT /note="Merozoite surface protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003104931"
FT TRANSMEM 1715..1740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 997..1569
FT /note="Merozoite surface 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07462"
FT DOMAIN 1639..1675
FT /note="Merozoite surface protein EGF"
FT /evidence="ECO:0000259|Pfam:PF12946"
FT REGION 206..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..379
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1086..1152
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1482..1578
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 758..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1744
FT /evidence="ECO:0000313|EMBL:ADF48816.1"
SQ SEQUENCE 1744 AA; 195568 MW; 5893E59E774E9EBC CRC64;
MKALLFLFSF IFFVTKCQCE TESYKQLVAK LDKLEALVVD GYELFHKKKL GESDIQVETN
ASANNNNNNQ VSVLTSKIRN FVGKFLELQI PGHTDLLHLI RELAFEPNGI KYLVESYEEF
NQLMHVINFH YDLLRAKLHD MCAHDYCKIP EHLKISDKEL DMLKKVVLGY RKPLDNIKDD
IGKLEAFITK NKETISNINK LISDENAKRG GQSTNTTNGT GAQTDGHQPT TASSETSSGS
SVSSVSGSSG LGSSGTGSTG TGSTGTGSTG NISPSQARAD SPSTGTDYNA KKIIFQAVYN
TIFYTNQLQE AQKLIAVLEK RVKVLKEHKD IKVLLEQVAK EKEKLPKDYP NTTNLTNVHK
EAESKIAELE KKIEAIAKTV NFDLDGLFTD AEELEYYLRE KAKMAGTLII PESTKSAGTP
GKTVPTLKET YPHGISYALA ENSIYELIEK IGSDETFGDL QNPDDGKQPK KGILINETKR
KELLEKIMNK IKIEEDKLPN LKKEYDEKFK VYEEKVKDFQ PAFNHFYEAR LDNTLVENKF
DEFKTKREAY MEEKKKLESC SYEQNTNLIN KLKKQLTYLE DYVLRKDIAD DEIKHFSFME
WKLKSEIYDL AQEIRKNENK LTVENKFDFS GVVELQVQKV LIIKKIEALK NVQNLLKNAK
VKDDLYVPKV YKTGEKPEPY YLMVLKREID KLKDFIPKIE SMIATEKNKP TVAAADIVAK
GQSLRGASET GTTGNTVNAQ TAVVQPQHQV ANAVTVQPGT TGHQAQGGEA ETQTNSVQAA
QVQQTPAGDA QQVISTQPTS QSAAPGVSAT PAPTPAAAAA PAPAMSKLEY LEKLLDFLKS
AYACHKHIFV TNSTMKKELL DQYKLNADEQ NKINETKCDE LDLLFNVQNN LPAMYSIYDS
MSNELQNLYI 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 LQKEDNYLNL EKFRVLSRLE GRLGKNIELE
KENISYLSSG LLHVLTELKE IINDKKYSGK DHAKNIAEVK KALQAYQELI PKVTSQESTS
VAVTVPGAVV PGVPTAAAAG SGASGAVPPA GGPSPPATGG VVPGVVESAE AQTQTQAQDY
AEDYDKVIAL PLFGNNDDDG EEDQVTTGEA ESEAPEILVP AGISDYDVVY LKPLAGMYKT
IKKQLENHVN AFNTNITDML DSRLKKRNYF LEVLNSDLNP FKYSSSGEYI IKDPYKLLDL
EKKKKLIGSY KYIGASIDMD LATANDGVAY YNKMEELYKT HLTAVNAQIK KVEDDINTQN
EELKKIENDS TKTTEKAKFT AKKAELEKYL PFLNSLQKEY ESLVSKVNTY TDNLKKVINN
CQLEKKEAEI TVKKLQDYNK MDEKLEEYKK SEKKNEVKSS GLLEKLMKSK LIKENESKEI
LSQLLNVQTQ LLTMSSEHTC IDTNVPDNAA CYRYLDGTEE WRCLLTFKEE GGKCVPASNV
TCKDNNGGCA PEAECKMTDS NKIVCKCTKE GSEPLFEGVF CSSSSFLSLS FLLLMLLFLL
CMEL
//
