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Protein

Apical membrane antigen 1

Gene

AMA1

Organism
Toxoplasma gondii (strain ATCC 50861 / VEG)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential microneme protein that plays an important role in host cell invasion. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of the parasite, leading to internalization of the parasite into a parasitophorous vacuole (PV).9 Publications

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Apical membrane antigen 1
Short name:
TgAMA-1
Short name:
TgAMA1
Cleaved into the following chain:
Gene namesi
Name:AMA1
ORF Names:TGVEG_255260
OrganismiToxoplasma gondii (strain ATCC 50861 / VEG)
Taxonomic identifieri432359 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma
Proteomesi
  • UP000002226 Componenti: Partially assembled WGS sequence

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini49 – 483ExtracellularSequence analysisAdd BLAST435
Transmembranei484 – 504HelicalSequence analysisAdd BLAST21
Topological domaini505 – 569CytoplasmicSequence analysisAdd BLAST65

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Severely compromises the parasite in its ability to invade host cells. Inhibits secretion of the rhoptries, organelles whose discharge is coupled to active host cell penetration.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi51L → K: Mislocalizes to the endosomal system. 1 Publication1
Mutagenesisi213Y → A: Abolishes interaction with RON2. 1 Publication1
Mutagenesisi487 – 488AG → FF: Reduces cleavage 30-fold. Uncleavable; when associated with 492-FF-493. 1 Publication2
Mutagenesisi489L → G: Enhances cleavage 13-fold. 1 Publication1
Mutagenesisi492 – 493GG → FF: Minor effect on proteolysis. Uncleavable; when associated with 487-FF-488. 1 Publication2
Mutagenesisi547 – 548FW → AA: Does not impair function. 1 Publication2
Mutagenesisi568 – 569DY → AA: Does not impair function. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 48Sequence analysisAdd BLAST48
PropeptideiPRO_000042195949 – 66Removed in mature form; required for microneme targeting of the proprotein1 PublicationAdd BLAST18
ChainiPRO_000042196067 – 569Apical membrane antigen 1Add BLAST503
ChainiPRO_000042196167 – 487Apical membrane antigen 1, soluble formAdd BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi86N-linked (GlcNAc...)1 Publication1
Disulfide bondi117 ↔ 286
Disulfide bondi194 ↔ 226
Disulfide bondi242 ↔ 255
Disulfide bondi304 ↔ 393
Disulfide bondi324 ↔ 384
Disulfide bondi435 ↔ 459
Disulfide bondi447 ↔ 471
Disulfide bondi452 ↔ 479

Post-translational modificationi

Proteolytically cleaved during invasion within its transmembrane domain, releasing a soluble form from the tachyzoite surface. The cytosolic tail generated by ROM4 cleavage during invasion may trigger parasite replication within the parasitophorous vacuole.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei487 – 488Cleavage; by rhomboid protease ROM42

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

SwissPalmiB6KAM0.

Expressioni

Keywords - Developmental stagei

Tachyzoite

Interactioni

Subunit structurei

Component of the moving junction (MJ) complex, composed of AMA1, a transmembrane protein on the parasite surface, and a complex of the rhoptry neck proteins RON2, RON4, RON5 and RON8 localized to the cytoplasmic face of the host plasma membrane. Interacts (via ectodomain) with RON2 (via C-terminus); RON2 serves as the receptor for AMA1 on the host plasma membrane. AMA1 and the RON proteins are initially in distinct compartments within the parasite, namely the micronemes and the rhoptries, and interaction happens only upon initiation of invasion when the micronemes and rhoptries discharge.4 Publications

Protein-protein interaction databases

STRINGi5811.TGME49_055260.

Structurei

Secondary structure

1569
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi71 – 73Combined sources3
Helixi76 – 83Combined sources8
Turni87 – 91Combined sources5
Beta strandi95 – 97Combined sources3
Beta strandi101 – 105Combined sources5
Beta strandi108 – 112Combined sources5
Beta strandi119 – 121Combined sources3
Beta strandi123 – 126Combined sources4
Helixi145 – 151Combined sources7
Beta strandi170 – 175Combined sources6
Helixi176 – 180Combined sources5
Helixi190 – 199Combined sources10
Beta strandi201 – 204Combined sources4
Beta strandi206 – 208Combined sources3
Beta strandi210 – 214Combined sources5
Beta strandi217 – 220Combined sources4
Turni221 – 224Combined sources4
Beta strandi225 – 230Combined sources6
Turni239 – 241Combined sources3
Beta strandi242 – 244Combined sources3
Beta strandi247 – 250Combined sources4
Beta strandi252 – 254Combined sources3
Beta strandi256 – 259Combined sources4
Beta strandi262 – 264Combined sources3
Beta strandi268 – 271Combined sources4
Helixi273 – 276Combined sources4
Turni279 – 281Combined sources3
Helixi282 – 285Combined sources4
Beta strandi291 – 300Combined sources10
Beta strandi303 – 306Combined sources4
Helixi307 – 309Combined sources3
Beta strandi314 – 317Combined sources4
Helixi321 – 330Combined sources10
Beta strandi346 – 349Combined sources4
Turni353 – 357Combined sources5
Beta strandi371 – 376Combined sources6
Beta strandi382 – 389Combined sources8
Beta strandi392 – 407Combined sources16
Helixi415 – 417Combined sources3
Helixi429 – 432Combined sources4
Helixi437 – 439Combined sources3
Turni449 – 452Combined sources4
Beta strandi453 – 460Combined sources8
Beta strandi463 – 470Combined sources8
Helixi473 – 478Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X2ZX-ray2.00A/B/D/E64-519[»]
2Y8RX-ray2.45A/B/D/E64-484[»]
2Y8SX-ray2.55A/D64-484[»]
2Y8TX-ray1.95A/D64-484[»]
SMRiB6KAM0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB6KAM0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 287DIAdd BLAST221
Regioni288 – 415DIIAdd BLAST128
Regioni416 – 487DIIIAdd BLAST72

Sequence similaritiesi

Belongs to the apicomplexan parasites AMA1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiB6KAM0.

Family and domain databases

InterProiIPR003298. Apmem_Ag1.
[Graphical view]
PfamiPF02430. AMA-1. 1 hit.
[Graphical view]
PRINTSiPR01361. MEROZOITESA.
SMARTiSM00815. AMA-1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B6KAM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MICSIMGGLR SLRAARPYSH QSNTETKHMG LVGVASLLVL VADCTIFASG
60 70 80 90 100
LSSSTRSRES QTLSASTSGN PFQANVEMKT FMERFNLTHH HQSGIYVDLG
110 120 130 140 150
QDKEVDGTLY REPAGLCPIW GKHIELQQPD RPPYRNNFLE DVPTEKEYKQ
160 170 180 190 200
SGNPLPGGFN LNFVTPSGQR ISPFPMELLE KNSNIKASTD LGRCAEFAFK
210 220 230 240 250
TVAMDKNNKA TKYRYPFVYD SKKRLCHILY VSMQLMEGKK YCSVKGEPPD
260 270 280 290 300
LTWYCFKPRK SVTENHHLIY GSAYVGENPD AFISKCPNQA LRGYRFGVWK
310 320 330 340 350
KGRCLDYTEL TDTVIERVES KAQCWVKTFE NDGVASDQPH TYPLTSQASW
360 370 380 390 400
NDWWPLHQSD QPHSGGVGRN YGFYYVDTTG EGKCALSDQV PDCLVSDSAA
410 420 430 440 450
VSYTAAGSLS EETPNFIIPS NPSVTPPTPE TALQCTADKF PDSFGACDVQ
460 470 480 490 500
ACKRQKTSCV GGQIQSTSVD CTADEQNECG SNTALIAGLA VGGVLLLALL
510 520 530 540 550
GGGCYFAKRL DRNKGVQAAH HEHEFQSDRG ARKKRPSDLM QEAEPSFWDE
560
AEENIEQDGE THVMVEGDY
Length:569
Mass (Da):63,021
Last modified:December 16, 2008 - v1
Checksum:i44EDB7C933D75193
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35 – 36AS → QV in AAB65410 (PubMed:11083833).Curated2
Sequence conflicti132P → L in AAB65410 (PubMed:11083833).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAYL02000028 Genomic DNA. Translation: ESS35482.1.
AF010264 mRNA. Translation: AAB65410.1.

Genome annotation databases

EnsemblProtistsiESS35482; ESS35482; TGVEG_255260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAYL02000028 Genomic DNA. Translation: ESS35482.1.
AF010264 mRNA. Translation: AAB65410.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X2ZX-ray2.00A/B/D/E64-519[»]
2Y8RX-ray2.45A/B/D/E64-484[»]
2Y8SX-ray2.55A/D64-484[»]
2Y8TX-ray1.95A/D64-484[»]
SMRiB6KAM0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5811.TGME49_055260.

PTM databases

SwissPalmiB6KAM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiESS35482; ESS35482; TGVEG_255260.

Phylogenomic databases

InParanoidiB6KAM0.

Miscellaneous databases

EvolutionaryTraceiB6KAM0.

Family and domain databases

InterProiIPR003298. Apmem_Ag1.
[Graphical view]
PfamiPF02430. AMA-1. 1 hit.
[Graphical view]
PRINTSiPR01361. MEROZOITESA.
SMARTiSM00815. AMA-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMA1_TOXGV
AccessioniPrimary (citable) accession number: B6KAM0
Secondary accession number(s): B9QC59, O15681, V4ZTW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: December 16, 2008
Last modified: November 30, 2016
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Caution

PubMed:21205639 reported that AMA1 may also be involved in a signaling pathway leading to replication. However, PubMed:22523242 refutes this model.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.