AMA1_PLAFH
ID AMA1_PLAFH Reviewed; 622 AA.
AC P50491;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 80.
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 thtn / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=70151;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M58547; AAA29720.1; -; Genomic_DNA.
DR AlphaFoldDB; P50491; -.
DR BMRB; P50491; -.
DR SMR; P50491; -.
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_0000024613"
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 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; 71989 MW; 1FDFA53593C94CC5 CRC64;
MRKLYCVLLL SAFEFTYMIN FGRGQNYWEH PYQNSDVYRP INEHREHPKE YEYPLLQEHT
YQQEDSGEDE NTLQHAYPID HEGAEPAPQE QNLFSSIEIV ERSNYMGNPW TEYMAKYDIE
KVHGSGIRVD LGEDAEVAGT QYRLPSGKCP VFGKGIIIEN SKTTFLTPVA TENQDLKDGG
FAFPPTEPLI SPMTLDQMRH LYKDNEYVKN LDELTLCSRH AGNMNPDNDK NSNYKYPAVY
DYEDKKCHIL YIAAQENNGP RYCNKDESKR NSMFCFRPAK DKLFENYTYL SKNVVDNWEE
VCPRKNLENA KFGLWVDGNC EDIPHVNEFS ANDLFECNKL VFELSASDQP KQYEQHLTDY
EKIKEGFKNK NASMIKSAFL PTGAFKADRY KSRGKGYNWG NYNTETQKCE IFNVKPTCLI
NNSSYIATTA LSHPNEVENN FPCSLYKDEI KKEIERESKR IKLNDNDDEG NKKIIAPRIF
ISDDKDSLKC PCDPEIVSNS TCNFFVCKCV EKRAEVTSNN EVVVKEEYKD EYADIPEHKP
TYDNMKIIIA SSAAVAVLAT ILMVYLYKRK GNAEKYDKMD EPQDYGKSTS RNDEMLDPEA
SFWGEEKRAS HTTPVLMEKP YY
