MSP1_PLAFK
ID MSP1_PLAFK Reviewed; 1630 AA.
AC P04932;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Merozoite surface protein 1;
DE AltName: Full=Merozoite surface antigens;
DE AltName: Full=PMMSA;
DE AltName: Full=p190;
DE Flags: Precursor;
GN Name=MSP-1;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3004972; DOI=10.1002/j.1460-2075.1985.tb04154.x;
RA Mackay M., Goman M., Bone N., Hyde J.E., Scaife J., Certa U.,
RA Stunnenberg H., Bujard H.;
RT "Polymorphism of the precursor for the major surface antigens of Plasmodium
RT falciparum merozoites: studies at the genetic level.";
RL EMBO J. 4:3823-3829(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA Pan W., Tolle R., Bujard H.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- PTM: Merozoite surface antigen contain the sequence of 83 kDa, 42 kDa
CC and 19 kDa antigens which are the major surface antigens of merozoites.
CC The maturation take place during schizont.
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DR EMBL; X03371; CAA27070.1; -; Genomic_DNA.
DR AlphaFoldDB; P04932; -.
DR BMRB; P04932; -.
DR SMR; P04932; -.
DR PRIDE; P04932; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR010901; MSP1_C.
DR InterPro; IPR024730; MSP1_EGF_1.
DR Pfam; PF12946; EGF_MSP1_1; 1.
DR Pfam; PF07462; MSP1_C; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Malaria; Membrane; Merozoite; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1609
FT /note="Merozoite surface protein 1"
FT /id="PRO_0000024554"
FT PROPEP 1610..1630
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024555"
FT REGION 60..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..84
FT /note="Tripeptide SG(TP) repeat"
FT REGION 680..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1609
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1523..1534
FT /evidence="ECO:0000250"
FT DISULFID 1528..1544
FT /evidence="ECO:0000250"
FT DISULFID 1546..1557
FT /evidence="ECO:0000250"
FT DISULFID 1565..1578
FT /evidence="ECO:0000250"
FT DISULFID 1572..1592
FT /evidence="ECO:0000250"
FT DISULFID 1594..1608
FT /evidence="ECO:0000250"
SQ SEQUENCE 1630 AA; 187291 MW; ADBDEC3CE0A46322 CRC64;
MKIIFFLCSF LFFIINTQCV THESYQELVK KLEALEDAVL TGYSLFHKEK MILNEEEITT
KGASAQSGTS GTSGTSGPSG PSGTSPSSRS NTLPRSNTSS GASPPADASD SDAKSYADLK
HRVRNYLLTI KELKYPQLFD LTNHMLTLCD NIHGFKYLID GYEEINELLY KLNFYFDLLR
AKLNDVCAND YCQIPFNLKI RANELDVLKK LVFGYRKPLD NIKDNVGKME DYIKKNKKTI
ENINELIEES KKTIDKNKNA TKEEEKKKLY QAQYDLSIYN KQLEEAHNLI SVLEKRIDTL
KKNENIKELL DKINEIKNPP PANSGNTPNT LLDKNKKIEE HEKEIKEIAK TIKFNIDSLF
TDPLELEYYL REKNKNIDIS AKVETKESTE PNEYPNGVTY PLSYNDINNA LNELNSFGDL
INPFDYTKEP SKNIYTDNER KKFINEIKEK IKIEKKKIES DKKSYEDRSK SLNDITKEYE
KLLNEIYDSK FNNNIDLTNF EKMMGKRYSY KVEKLTHHNT FASYENSKHN LEKLTKALKY
MEDYSLRNIV VEKELKYYKN LISKIENEIE TLVENIKKDE EQLFEKKITK DENKPDEKIL
EVSDIVKVQV QKVLLMNKID ELKKTQLILK NVELKHNIHV PNSYKQENKQ EPYYLIVLKK
EIDKLKVFMP KVESLINEEK KNIKTEGQSD NSEPSTEGEI TGQATTKPGQ QAGSALEGDS
VQAQAQEQKQ AQPPVPVPVP EAKAQVPTPP APVNNKTENV SKLDYLEKLY EFLNTSYICH
KYILVSHSTM NEKILKQYKI TKEEESKLSS CDPLDLLFNI QNNIPVMYSM FDSLNNSLSQ
LFMEIYEKEM VCNLYKLKDN DKIKNLLEEA KKVSTSVKTL SSSSMQPLSL TPQDKPEVSA
NDDTSHSTNL NNSLKLFENI LSLGKNKNIY QELIGQKSSE NFYEKILKDS DTFYNESFTN
FVKSKADDIN SLNDESKRKK LEEDINKLKK TLQLSFDLYN KYKLKLERLF DKKKTVGKYK
MQIKKLTLLK EQLESKLNSL NNPKHVLQNF SVFFNKKKEA EIAETENTLE NTKILLKHYK
GLVKYYNGES SPLKTLSEES IQTEDNYASL ENFKVLSKLE GKLKDNLNLE KKKLSYLSSG
LHHLIAELKE VIKNKNYTGN SPSENNTDVN NALESYKKFL PEGTDVATVV SESGSDTLEQ
SQPKKPASTH VGAESNTITT SQNVDDEVDD VIIVPIFGES EEDYDDLGQV VTGEAVTPSV
IDNILSKIEN EYEVLYLKPL AGVYRSLKKQ LENNVMTFNV NVKDILNSRF NKRENFKNVL
ESDLIPYKDL TSSNYVVKDP YKFLNKEKRD KFLSSYNYIK DSIDTDINFA NDVLGYYKIL
SEKYKSDLDS IKKYINDKQG ENEKYLPFLN NIETLYKTVN DKIDLFVIHL EAKVLNYTYE
KSNVEVKIKE LNYLKTIQDK LADFKKNNNF VGIADLSTDY NHNNLLTKFL STGMVFENLA
KTVLSNLLDG NLQGMLNISQ HQCVKKQCPQ NSGCFRHLDE REECKCLLNY KQEGDKCVEN
PNPTCNENNG GCDADAKCTE EDSGSNGKKI TCECTKPDSY PLFDGIFCSS SNFLGISFLL
ILMLILYSFI
