MAFB0_TOXGO
ID MAFB0_TOXGO Reviewed; 435 AA.
AC A0A140H545;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Mitochondrial association factor 1 form b0 {ECO:0000303|PubMed:26920761};
DE Short=MAF1RHb0 allele {ECO:0000303|PubMed:26920761};
DE Flags: Precursor;
GN Name=MAF1b0 {ECO:0000303|PubMed:26920761};
GN Synonyms=MAF1 {ECO:0000303|PubMed:26920761};
GN ORFNames=TGRH88_000150 {ECO:0000312|EMBL:KAF4645528.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000312|EMBL:AMN92246.1};
RN [1] {ECO:0000312|EMBL:AMN92246.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NOMENCLATURE, FUNCTION, AND
RP POLYMORPHISM.
RC STRAIN=RH {ECO:0000312|EMBL:AMN92246.1};
RX PubMed=26920761; DOI=10.1534/genetics.115.186270;
RA Adomako-Ankomah Y., English E.D., Danielson J.J., Pernas L.F., Parker M.L.,
RA Boulanger M.J., Dubey J.P., Boyle J.P.;
RT "Host Mitochondrial Association Evolved in the Human Parasite Toxoplasma
RT gondii via Neofunctionalization of a Gene Duplicate.";
RL Genetics 203:283-298(2016).
RN [2] {ECO:0000312|Proteomes:UP000557509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RH-88 {ECO:0000312|Proteomes:UP000557509};
RA Lorenzi H.A., Venepally P., Rozenberg A., Sibley D.;
RT "Genome sequence of Toxoplasma gondii RH-88 strain.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: During host cell infection by tachyzoites, does not play a
CC role in tethering the parasitophorous vacuole to the host mitochondria.
CC {ECO:0000269|PubMed:26920761}.
CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole membrane
CC {ECO:0000250|UniProtKB:A0A140H546}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:A0A140H546}.
CC -!- POLYMORPHISM: The MAF1 locus encodes multiple tandemly duplicated
CC paralogs that vary in expression, sequence and copy number across
CC T.gondii strains (PubMed:26920761). For instance, type I strain GT1 has
CC 6 copies, type I strain RH has 4 copies, type II strains ME49 and PRU
CC have 4 copies, type III strain VEG has 4 copies and type III strain CTG
CC has only 2 copies (PubMed:26920761). The paralogs are classified into
CC two groups, a and b and have probably arisen from the
CC neofunctionalization of an ancestral MAF1 a gene (PubMed:26920761).
CC They are characterized by the presence or absence of a repetitive
CC stretch of 4 to 7 prolines followed by a serine (P(4:7)S), as well as
CC differences in the amino acids surrounding the proline motif
CC (PubMed:26920761). This motif is either completely missing (a and b0
CC paralogs) or repeated up to six times (b paralogs) (PubMed:26920761).
CC cross the strains, transcript levels for the a paralogs are similar,
CC however, in type II strain ME49, transcript levels for the b paralogs
CC are low and no paralog MAF1 b1 protein is produced (PubMed:26920761).
CC Paralogs differ in their ability to mediate host mitochondrial
CC association (HMA), but also in their ability to confer a selective
CC advantage during infection in a mouse model (PubMed:26920761).
CC Tachyzoites from type I and III strains associate with host
CC mitochondria (HMA(+)), while tachyzoites from type II strains, such as
CC ME49, do not associate with host mitochondria (HMA(-)) due to a lack of
CC MAF1 b1 expression (PubMed:26920761). {ECO:0000269|PubMed:26920761}.
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DR EMBL; KU761333; AMN92246.1; -; Genomic_DNA.
DR EMBL; JAAUHK010000187; KAF4645528.1; -; Genomic_DNA.
DR VEuPathDB; ToxoDB:TGARI_220950; -.
DR VEuPathDB; ToxoDB:TGCAST_387150; -.
DR VEuPathDB; ToxoDB:TGCAST_390500; -.
DR VEuPathDB; ToxoDB:TGCOUG_394540; -.
DR VEuPathDB; ToxoDB:TGCOUG_394550; -.
DR VEuPathDB; ToxoDB:TGDOM2_323100; -.
DR VEuPathDB; ToxoDB:TGDOM2_401920; -.
DR VEuPathDB; ToxoDB:TGFOU_407650; -.
DR VEuPathDB; ToxoDB:TGGT1_220950; -.
DR VEuPathDB; ToxoDB:TGGT1_279100; -.
DR VEuPathDB; ToxoDB:TGMAS_361110; -.
DR VEuPathDB; ToxoDB:TGME49_220950; -.
DR VEuPathDB; ToxoDB:TGP89_422200; -.
DR VEuPathDB; ToxoDB:TGPRC2_279100B; -.
DR VEuPathDB; ToxoDB:TGRH88_000150; -.
DR VEuPathDB; ToxoDB:TGRUB_433890; -.
DR VEuPathDB; ToxoDB:TGVAND_437510; -.
DR VEuPathDB; ToxoDB:TGVAND_437520; -.
DR VEuPathDB; ToxoDB:TGVAND_439210; -.
DR VEuPathDB; ToxoDB:TGVEG_279100; -.
DR Proteomes; UP000557509; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Membrane; Signal; Tachyzoite; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..435
FT /note="Mitochondrial association factor 1 form b0"
FT /evidence="ECO:0000255"
FT /id="PRO_5029112464"
FT TOPO_DOM 28..96
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 46978 MW; 261A321B8BD67BB8 CRC64;
MWRIWRCRLS FLFVTGCLLG ALTAGLGSQM SDSVGRNVQA PAGVADASQE AGDVVEERTE
RTEEQVFAPG PPRRHSSESL FPRNPSVTAR RRRNRRITLI ATAVGVAVIL AALYVLRRRR
AQPPQEPEPP TRLRTPRPRA PSGQQQPSES EPPAGVPMKP GSLTLPFTCL GDTKVTFFGP
SGRQHGFTPL YDPSPSKRVA TVDAGANALF IGGGGLNGQF AKTLLEEAEK NGIRLTSVAL
SEHSQRIQQS LLRRAVKSPG KLVELDTGVA SPVFARSFGF VPVVPGLMWK ESKVGANVGV
TFIHILKPEV TPYGNLNNNV MMYTVAPCGA PPDTTYSLAY KTTIAGVIRA AAAYNDTPAG
QQYPVQGLRL PLLRGGIFRR NRSLESIGRA NAEGTSLAIT QYGPNFELQY MYDPSNAALH
GLQEAESTYL ASMLD
