AMA1_PLAFG
ID AMA1_PLAFG Reviewed; 622 AA.
AC P50490;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, 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=PF83;
OS Plasmodium falciparum (isolate FCR-3 / Gambia).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5838;
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; M58546; AAA29719.1; -; Genomic_DNA.
DR PDB; 4R1A; X-ray; 2.00 A; A=104-438.
DR PDBsum; 4R1A; -.
DR AlphaFoldDB; P50490; -.
DR BMRB; P50490; -.
DR SMR; P50490; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR DisProt; DP02941; -.
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 3D-structure; Disulfide bond; Glycoprotein; Malaria; Membrane; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..622
FT /note="Apical membrane antigen 1"
FT /id="PRO_0000024612"
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 578..603
FT /note="Disordered"
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"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:4R1A"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:4R1A"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4R1A"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 305..316
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:4R1A"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:4R1A"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:4R1A"
FT STRAND 418..429
FT /evidence="ECO:0007829|PDB:4R1A"
SQ SEQUENCE 622 AA; 71968 MW; 089336BE0464695C CRC64;
MRKLYCVLLL SAFEFTYMIN FGRGQNYWEH PYQKSGVYHP INEHREHPKE YEYPLHQEHT
YQQEDSGEDE NTLQHAYPID HEGAEPAPQE QNLFSSIEIV ERSNYMGNPW TEYMAKYDIE
EVHGSGIRVD LGEDAEVAGT QYRLPSGKCP VFGKGIIIEN SNTTFLKPVA TGNQDLKDGG
FAFPPTNPLI SPMTLNGMRD FYKNNEYVKN LDELTLCSRH AGNMNPDNDK NSNYKYPAVY
DYNDKKCHIL YIAAQENNGP RYCNKDQSKR NSMFCFRPAK DKLFENYTYL SKNVVDNWEE
VCPRKNLENA KFGLWVDGNC EDIPHVNEFS ANDLFECNKL VFELSASDQP KQYEQHLTDY
EKIKEGFKNK NASMIKSAFL PTGAFKADRY KSHGKGYNWG NYNRETQKCE IFNVKPTCLI
NNSSYIATTA LSHPIEVEHN FPCSLYKDEI KKEIERESKR IKLNDNDDEG NKKIIAPRIF
ISDDKDSLKC PCDPEMVSNS TCRFFVCKCV ERRAEVTSNN EVVVKEEYKD EYADIPEHKP
TYDNMKIIIA SSAAVAVLAT ILMVYLYKRK GNAEKYDKMD QPQHYGKSTS RNDEMLDPEA
SFWGEEKRAS HTTPVLMEKP YY
