AMA1L_TOXGV
ID AMA1L_TOXGV Reviewed; 651 AA.
AC B6K9M7; B9QA70; V4ZJL7;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Apical membrane antigen 1-like protein;
DE Short=SporoAMA1;
DE Contains:
DE RecName: Full=Apical membrane antigen 1-like protein, soluble form;
DE Flags: Precursor;
GN ORFNames=TGVEG_315730;
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG;
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=22279555; DOI=10.1371/journal.pone.0029955;
RA Fritz H.M., Bowyer P.W., Bogyo M., Conrad P.A., Boothroyd J.C.;
RT "Proteomic analysis of fractionated Toxoplasma oocysts reveals clues to
RT their environmental resistance.";
RL PLoS ONE 7:E29955-E29955(2012).
RN [3]
RP INDUCTION.
RX PubMed=22347997; DOI=10.1371/journal.pone.0029998;
RA Fritz H.M., Buchholz K.R., Chen X., Durbin-Johnson B., Rocke D.M.,
RA Conrad P.A., Boothroyd J.C.;
RT "Transcriptomic analysis of toxoplasma development reveals many novel
RT functions and structures specific to sporozoites and oocysts.";
RL PLoS ONE 7:E29998-E29998(2012).
CC -!- FUNCTION: May play a role in host cell invasion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted {ECO:0000250}. Note=Initially
CC localizes to micronemes, specialized secretory organelles of
CC apicomplexan parasites important for host cell invasion. Relocalizes to
CC the surface membrane upon host invasion. {ECO:0000250}.
CC -!- INDUCTION: Readily detected in oocysts (at protein level). Specifically
CC up-regulated in sporozoites, but not in tachyzoites and bradyzoites.
CC {ECO:0000269|PubMed:22279555, ECO:0000269|PubMed:22347997}.
CC -!- PTM: Proteolytically cleaved within its transmembrane domain, releasing
CC a soluble form from the cell surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the apicomplexan parasites AMA1 family.
CC {ECO:0000305}.
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DR EMBL; AAYL02000034; ESS35318.1; -; Genomic_DNA.
DR PDB; 3ZLD; X-ray; 3.10 A; A=97-480.
DR PDB; 3ZLE; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L=97-480.
DR PDBsum; 3ZLD; -.
DR PDBsum; 3ZLE; -.
DR AlphaFoldDB; B6K9M7; -.
DR SMR; B6K9M7; -.
DR STRING; 5811.TGME49_115730; -.
DR EnsemblProtists; ESS35318; ESS35318; TGVEG_315730.
DR EnsemblProtists; TGME49_315730-t26_1; TGME49_315730-t26_1; TGME49_315730.
DR VEuPathDB; ToxoDB:TGVEG_315730; -.
DR eggNOG; ENOG502QYHG; Eukaryota.
DR HOGENOM; CLU_712722_0_0_1; -.
DR InParanoid; B6K9M7; -.
DR OMA; GANWANF; -.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR003298; Apmem_Ag1.
DR Pfam; PF02430; AMA-1; 1.
DR PRINTS; PR01361; MEROZOITESA.
DR SMART; SM00815; AMA-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT PROPEP 42..81
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421956"
FT CHAIN 82..651
FT /note="Apical membrane antigen 1-like protein"
FT /id="PRO_0000421957"
FT CHAIN 82..574
FT /note="Apical membrane antigen 1-like protein, soluble
FT form"
FT /id="PRO_0000421958"
FT TOPO_DOM 42..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 483..486
FT /note="1; approximate"
FT REPEAT 487..490
FT /note="2"
FT REPEAT 491..494
FT /note="3"
FT REPEAT 495..498
FT /note="4"
FT REPEAT 499..502
FT /note="5"
FT REPEAT 503..506
FT /note="6"
FT REPEAT 507..510
FT /note="7"
FT REPEAT 511..514
FT /note="8"
FT REPEAT 515..518
FT /note="9"
FT REPEAT 519..522
FT /note="10"
FT REPEAT 523..527
FT /note="11; approximate"
FT REPEAT 528..531
FT /note="12; approximate"
FT REGION 483..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..531
FT /note="12 x 4 AA approximate tandem-repeats of P-P-V-E"
FT REGION 598..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 574..575
FT /note="Cleavage; by rhomboid-like protease"
FT /evidence="ECO:0000250"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..309
FT /evidence="ECO:0000250"
FT DISULFID 215..248
FT /evidence="ECO:0000250"
FT DISULFID 264..277
FT /evidence="ECO:0000250"
FT DISULFID 327..417
FT /evidence="ECO:0000250"
FT DISULFID 347..408
FT /evidence="ECO:0000250"
FT DISULFID 441..463
FT /evidence="ECO:0000250"
FT DISULFID 453..475
FT /evidence="ECO:0000250"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3ZLD"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3ZLD"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3ZLD"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3ZLE"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:3ZLE"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:3ZLE"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 312..323
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:3ZLE"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:3ZLE"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 417..431
FT /evidence="ECO:0007829|PDB:3ZLE"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 457..464
FT /evidence="ECO:0007829|PDB:3ZLE"
FT STRAND 467..474
FT /evidence="ECO:0007829|PDB:3ZLE"
SQ SEQUENCE 651 AA; 69944 MW; AC1175273C5AD676 CRC64;
MPTESRSILA RAEETRCRHL SRLLRAGLVF LLCDVLTSCL ATPELQNTVI RSSKAHHLQL
LFSSRSTPAV KFPLDATLSA PNSFGEQEAR SVEAVKQNPW ATTTAFADFM KRFNIPQVHG
SGIFVDLGRD TEGYREVGGK CPVFGKAIQM HQPAEYSNNF LDDAPTSNDA SKKPLPGGFN
NPQVYTSGQK FSPIDDSLLQ ERLGTAGPKT AIGRCALYAY STIAVNPSTN YTSTYKYPFV
YDAVSRKCYV LSVSAQLLKG EKYCSVNGTP SGLTWACFEP VKEKSSARAL VYGSAFVAEG
NPDAWQSACP NDAVKDALFG KWEDGQCVPF DTKTSVQSDQ ATNKEECWKR VFANPLVASD
APTTYPEAAQ KNWNDFWPVH EQSSPKSGGF GANWANFYLE KESGETICAI FDQVPDCFAP
ITGAVAYTAL GSSTEVNLPQ CDSASFIPIE GPCNNCVQVV TECVGNQFDQ TSKACCTEPE
IIPPVKPPVE PPVEPPVEPP VEPPVEPPVE PPVEPPVEPP VEPPVVEPPT EPSVPEPEPP
VVLPPTPGEG GGGGTSGDET VEKEGSGGNT ALIAGSVLGM LIILALVGTC VGFYYRKRPL
PPTERPTVEA SGGREVEGPS DVAVPPDHSW WGEGEHETES LLGSRAVDAE F
