AMA1_PLAFR
ID AMA1_PLAFR Reviewed; 562 AA.
AC P22622;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Apical membrane antigen 1;
DE AltName: Full=Merozoite surface antigen;
DE Flags: Precursor;
GN Name=AMA-1; Synonyms=AG352;
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2181309; DOI=10.1016/0166-6851(90)90067-v;
RA Peterson M.G., Nguyen-Dinh P., Marshall V.M., Elliott J.F., Collins W.E.,
RA Anders R.F., Kemp D.J.;
RT "Apical membrane antigen of Plasmodium fragile.";
RL Mol. Biochem. Parasitol. 39:279-284(1990).
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; M29898; AAA29474.1; -; Genomic_DNA.
DR PIR; A44944; A44944.
DR AlphaFoldDB; P22622; -.
DR SMR; P22622; -.
DR VEuPathDB; PlasmoDB:AK88_00071; -.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Malaria; Membrane; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..562
FT /note="Apical membrane antigen 1"
FT /id="PRO_0000024615"
FT TOPO_DOM 22..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 519..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..247
FT /evidence="ECO:0000250"
FT DISULFID 162..192
FT /evidence="ECO:0000250"
FT DISULFID 208..220
FT /evidence="ECO:0000250"
FT DISULFID 265..363
FT /evidence="ECO:0000250"
FT DISULFID 282..354
FT /evidence="ECO:0000250"
FT DISULFID 388..444
FT /evidence="ECO:0000250"
FT DISULFID 432..449
FT /evidence="ECO:0000250"
FT DISULFID 434..451
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 64488 MW; 9EAB72D437EA7164 CRC64;
MNKIYCILFL SAQCLVHMGK CEPNQKPSRL TRSAKNVLLE QEPMVERSTR MSNPWKAFME
KYDIEKTHSS GIRVDLGEDA EVGNSSYRIP AGKCPVFGKG IVIQNSEVSF LTPVATGNQK
LKDGGFAFPQ ANDHISPISI KNLRERYKEN PDLMKLNDLA LCKTHAASFV MEMDKNSSYR
HPAVYDEDKK ICYMLYLSAQ ENMGPRYCSK DAENKDAMFC FKPDKNETFD HLAYLSKNVV
NDWQNKCPRK NLGNSKFGLW VDGNCEEIPY VQDVQAKDLR ECNRIVFEAS ASDQPTQYEE
ELTDYQKIQE GFRQNDQGMI KSAFLPVGAF NSDNFKSKGR GYNWANFDTE NKVCYLFNAK
PTCLINDKNF IATTALSHPQ EVDNEFPCSI YKDEMEREMR KESRNMSLYN VDKARIVLPR
IFISNDKDSL KCPCAPEHIT NSTCNFYVCN CVEKRAEIKE NNEVAIKEEF KQDYQYAQGE
SKNQMLLIII GITGGVCVVA LASMFYFRKK AHNDKYDKME QADGYGKPTT RKDEMLDPEA
SFWGEEKRAS HTTPVLMEKP YY
