ID   AMA1_PLACH              Reviewed;         558 AA.
AC   P16445;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Apical membrane antigen 1;
DE   AltName: Full=Merozoite surface antigen;
DE   Flags: Precursor;
GN   Name=AMA-1;
OS   Plasmodium chabaudi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS;
RX   PubMed=2608101; DOI=10.1016/0166-6851(89)90160-6;
RA   Marshall V.M., Peterson M.G., Lew A.M., Kemp D.J.;
RT   "Structure of the apical membrane antigen I (AMA-1) of Plasmodium
RT   chabaudi.";
RL   Mol. Biochem. Parasitol. 37:281-284(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-377.
RC   STRAIN=DK;
RX   PubMed=8757869; DOI=10.1128/iai.64.8.3310-3317.1996;
RA   Crewther P.E., Matthew M.L., Flegg R.H., Anders R.F.;
RT   "Protective immune responses to apical membrane antigen 1 of Plasmodium
RT   chabaudi involve recognition of strain-specific epitopes.";
RL   Infect. Immun. 64:3310-3317(1996).
RN   [3]
RP   DISULFIDE BONDS.
RX   PubMed=8910611; DOI=10.1074/jbc.271.46.29446;
RA   Hodder A.N., Crewther P.E., Matthew M.L., Reid G.E., Moritz R.L.,
RA   Simpson R.J., Anders R.F.;
RT   "The disulfide bond structure of Plasmodium apical membrane antigen-1.";
RL   J. Biol. Chem. 271:29446-29452(1996).
CC   -!- FUNCTION: Involved in parasite invasion of erythrocytes.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the apicomplexan parasites AMA1 family.
CC       {ECO:0000305}.
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DR   EMBL; M25248; AAA90929.1; -; Genomic_DNA.
DR   EMBL; U49745; AAB36511.1; -; Genomic_DNA.
DR   PIR; A44964; A44964.
DR   AlphaFoldDB; P16445; -.
DR   SMR; P16445; -.
DR   VEuPathDB; PlasmoDB:PCHAS_0931000; -.
DR   eggNOG; ENOG502SRUQ; Eukaryota.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.1010.10; -; 1.
DR   InterPro; IPR003298; Apmem_Ag1.
DR   InterPro; IPR024056; Apmem_Ag1_dom_sf.
DR   Pfam; PF02430; AMA-1; 1.
DR   PRINTS; PR01361; MEROZOITESA.
DR   SMART; SM00815; AMA-1; 1.
DR   SUPFAM; SSF82910; SSF82910; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Malaria; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..558
FT                   /note="Apical membrane antigen 1"
FT                   /id="PRO_0000024609"
FT   TOPO_DOM        22..480
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        504..558
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..247
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        162..192
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        208..220
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        265..363
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        282..354
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        389..443
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        431..448
FT                   /evidence="ECO:0000269|PubMed:8910611"
FT   DISULFID        433..450
FT                   /evidence="ECO:0000269|PubMed:8910611"
SQ   SEQUENCE   558 AA;  63974 MW;  9773F3E6A439A972 CRC64;
     MKEIYYIVIL CSLYLINLGN CSEGTDKIIS ENGDVKFDLI PKENTERSHK LINPWEKFME
     KYDIEKVHGS GIRVDLGEDA RVENQDYRIP SGKCPVMGKG ITIQNSKVSF LTRVATGNQK
     VREGGLAFPQ TDVNISPITI DNLKLMYKDH KEILALNDMS LCAKHASFYV PGTNVNTAYR
     HPAVYDKSNK TCYILYVAAQ ENMGPRYCSN EEDNENQPFC FTPEKKDEYK NLSYLTKNLR
     EDWETSCPNK SIQNAKFGVW VDGYCSEYQK KEVHDNKTLL ECNQIVFNES ASDQPKQYEK
     HLEDTAKIRR GIVDRNGKLI GEALLPIGSY RADQVKSKGK GYNWANYDKK TKKCYIFNKK
     PTCLINDKDF VATTALSSLE EGPQESFPCD IYKKKIAEEI KVMNVNRNNN GNDTIKFPRI
     FISDDKESLN CPCEPTQLTQ STCKFFVCNC VEKRQFISEN NEVEIKDEFK SEYESPINQR
     MLIIIILIAT GAILASLLIF YFFKSNKPGD DYDKMGQADT YGKAQSRKDE MLDPEVSFWG
     EDKRASHTTP VLMEKPYY