AMA1_PLAFF
ID AMA1_PLAFF Reviewed; 622 AA.
AC P22621;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 FC27 / Papua New Guinea).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5837;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2701947; DOI=10.1128/mcb.9.7.3151-3154.1989;
RA Peterson M.G., Marshall V.M., Smythe J.A., Crewther P.E., Lew A., Silva A.,
RA Anders R.F., Kemp D.J.;
RT "Integral membrane protein located in the apical complex of Plasmodium
RT falciparum.";
RL Mol. Cell. Biol. 9:3151-3154(1989).
RN [2]
RP STRUCTURE BY NMR OF 309-436, AND DISULFIDE BONDS.
RX PubMed=15964019; DOI=10.1016/j.jmb.2005.05.011;
RA Feng Z.-P., Keizer D.W., Stevenson R.A., Yao S., Babon J.J., Murphy V.J.,
RA Anders R.F., Norton R.S.;
RT "Structure and inter-domain interactions of domain II from the blood-stage
RT malarial protein, apical membrane antigen 1.";
RL J. Mol. Biol. 350:641-656(2005).
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; M27133; AAA29475.1; -; Genomic_DNA.
DR EMBL; M27957; AAA29476.1; -; mRNA.
DR PIR; A32499; A32499.
DR PDB; 1YXE; NMR; -; A=309-436.
DR PDB; 2Q8A; X-ray; 2.40 A; A=104-438.
DR PDB; 2Q8B; X-ray; 2.30 A; A=104-438.
DR PDBsum; 1YXE; -.
DR PDBsum; 2Q8A; -.
DR PDBsum; 2Q8B; -.
DR AlphaFoldDB; P22621; -.
DR BMRB; P22621; -.
DR SMR; P22621; -.
DR ABCD; P22621; 4 sequenced antibodies.
DR EvolutionaryTrace; P22621; -.
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 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_0000024611"
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..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..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:0000269|PubMed:15964019"
FT DISULFID 337..409
FT /evidence="ECO:0000269|PubMed:15964019"
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 CONFLICT 308
FT /note="Q -> E (in Ref. 1; AAA29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="I -> N (in Ref. 1; AAA29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="Q -> H (in Ref. 1; AAA29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="H -> N (in Ref. 1; AAA29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="I -> M (in Ref. 1; AAA29476)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="N -> R (in Ref. 1; AAA29476)"
FT /evidence="ECO:0000305"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1YXE"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1YXE"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1YXE"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:1YXE"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1YXE"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1YXE"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:1YXE"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:1YXE"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:1YXE"
SQ SEQUENCE 622 AA; 72010 MW; 7D41335E249FA18F CRC64;
MRKLYCVLLL SAFEFTYMIN FGRGQNYWEH PYQKSDVYHP INEHREHPKE YQYPLHQEHT
YQQEDSGEDE NTLQHAYPID HEGAEPAPQE QNLFSSIEIV ERSNYMGNPW TEYMAKYDIE
EVHGSGIRVD LGEDAEVAGT QYRLPSGKCP VFGKGIIIEN SNTTFLTPVA TGNQYLKDGG
FAFPPTEPLM SPMTLDEMRH FYKDNKYVKN LDELTLCSRH AGNMIPDNDK NSNYKYPAVY
DDKDKKCHIL YIAAQENNGP RYCNKDESKR NSMFCFRPAK DISFQNYTYL SKNVVDNWEK
VCPRKNLQNA KFGLWVDGNC EDIPHVNEFS AIDLFECNKL VFELSASDQP KQYEQHLTDY
EKIKEGFKNK NASMIKSAFL PTGAFKADRY KSHGKGYNWG NYNTETQKCE IFNVKPTCLI
NNSSYIATTA LSHPIEVEHN FPCSLYKNEI MKEIERESKR IKLNDNDDEG NKKIIAPRIF
ISDDKDSLKC PCDPEIVSNS TCNFFVCKCV ERRAEVTSNN EVVVKEEYKD EYADIPEHKP
TYDKMKIIIA SSAAVAVLAT ILMVYLYKRK GNAEKYDKMD EPQHYGKSNS RNDEMLDPEA
SFWGEEKRAS HTTPVLMEKP YY
