AMA1_PLAF8
ID AMA1_PLAF8 Reviewed; 622 AA.
AC P50492;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Apical membrane antigen 1;
DE AltName: Full=Merozoite surface antigen;
DE Flags: Precursor;
GN Name=AMA-1; Synonyms=PF83;
OS Plasmodium falciparum (isolate 7G8).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2270110; DOI=10.1016/0166-6851(90)90172-i;
RA Thomas A.W., Waters A.P., Carr D.;
RT "Analysis of variation in PF83, an erythrocytic merozoite vaccine candidate
RT antigen of Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 42:285-287(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; M58548; AAA29721.1; -; Genomic_DNA.
DR AlphaFoldDB; P50492; -.
DR BMRB; P50492; -.
DR SMR; P50492; -.
DR PRIDE; P50492; -.
DR ABCD; P50492; 12 sequenced antibodies.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..622
FT /note="Apical membrane antigen 1"
FT /id="PRO_0000024614"
FT TOPO_DOM 25..546
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 577..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 149..302
FT /evidence="ECO:0000250"
FT DISULFID 217..247
FT /evidence="ECO:0000250"
FT DISULFID 263..275
FT /evidence="ECO:0000250"
FT DISULFID 320..418
FT /evidence="ECO:0000250"
FT DISULFID 337..409
FT /evidence="ECO:0000250"
FT DISULFID 443..502
FT /evidence="ECO:0000250"
FT DISULFID 490..507
FT /evidence="ECO:0000250"
FT DISULFID 492..509
FT /evidence="ECO:0000250"
SQ SEQUENCE 622 AA; 71991 MW; 1C9C8715D8E2915F CRC64;
MRKLYCVLLL SAFEFTYMIN FGRGQNYWEH PYQKSDVYHP INEHREHSKE YEYPLHQEHT
YQQEDSGEDE NTLQHAYPID HEGAEPAPQE QNLFSSIEIV ERSNYMGNPW TEYMAKYDIK
EVHGSGIRVD LGEDAEVAGT QYRLPSGKCP VFGKGIIIEN SNTTFLKPVA TGNQDLKDGG
FAFPPTNPLI SPMTLDHMRD FYKNNEYVKN LDELTLCSRH AGNMNPDNDK NSNYKYPAVY
DYNDKKCHIL YIAAQENNGP RYCNKDESKR NSMFCFRPAK DKSFQNYTYL SKNVVDNWEK
VCPRKNLENA KFGLWVDGNC EDIPHVNEFS ANDLFECNKL VFELSASDQP KQYEQHLTDY
EKIKEGFKNK NASMIKSAFL PTGAFKADRY KSRGKGYNWG NYNRKTQKCE IFNVKPTCLI
NNSSYIATTA LSHPNEVEHN FPCSLYKDEI KKEIERESKR IKLNDNDDEG NKKIIAPRIF
ISDDIDSLKC PCDPEIVSNS TCNFFVCKCV EKRAEVTSNN EVVVKEEYKD EYADIPEHKP
TYDKMKIIIA SSAAVAVLAT ILMVYLYKRK GNAEKYDKMD EPQDYGKSNS RNDEMLDPEA
SFWGEEKRAS HTTPVLMEKP YY