MAFA1_TOXGO
ID MAFA1_TOXGO Reviewed; 435 AA.
AC A0A193AUK9; A0A7J6KFX2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Mitochondrial association factor 1 form a1 {ECO:0000303|PubMed:26920761};
DE Short=MAF1RHa1 allele {ECO:0000303|PubMed:26920761};
DE AltName: Full=MAF1a {ECO:0000303|PubMed:26920761};
DE Flags: Precursor;
GN Name=MAF1a1 {ECO:0000303|PubMed:26920761};
GN Synonyms=MAF1 {ECO:0000303|PubMed:26920761};
GN ORFNames=TGRH88_000160 {ECO:0000312|EMBL:KAF4645529.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000312|Proteomes:UP000557509};
RN [1] {ECO:0000312|EMBL:ANN02899.1}
RP NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND POLYMORPHISM.
RC STRAIN=RH {ECO:0000312|EMBL:SCA78655.1};
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.
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=33723040; DOI=10.1073/pnas.2013336118;
RA Blank M.L., Xia J., Morcos M.M., Sun M., Cantrell P.S., Liu Y., Zeng X.,
RA Powell C.J., Yates N., Boulanger M.J., Boyle J.P.;
RT "Toxoplasma gondii association with host mitochondria requires key
RT mitochondrial protein import machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [4] {ECO:0007744|PDB:6BXS, ECO:0007744|PDB:6BXT}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 159-435, FUNCTION, INTERACTION
RP WITH HOST SAMM50, POLYMORPHISM, AND MUTAGENESIS OF 420-ARG--ASP-435.
RX PubMed=29505111; DOI=10.1111/mmi.13947;
RA Blank M.L., Parker M.L., Ramaswamy R., Powell C.J., English E.D.,
RA Adomako-Ankomah Y., Pernas L.F., Workman S.D., Boothroyd J.C.,
RA Boulanger M.J., Boyle J.P.;
RT "A Toxoplasma gondii locus required for the direct manipulation of host
RT mitochondria has maintained multiple ancestral functions.";
RL Mol. Microbiol. 108:519-535(2018).
CC -!- FUNCTION: During host cell infection by tachyzoites, does not play a
CC role in tethering the parasitophorous vacuole to the host mitochondria,
CC probably because it does not bind host mitochondrial import protein
CC TOMM70. {ECO:0000269|PubMed:26920761, ECO:0000269|PubMed:29505111,
CC ECO:0000269|PubMed:33723040}.
CC -!- SUBUNIT: Interacts with host SAMM50. {ECO:0000269|PubMed:29505111}.
CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole membrane
CC {ECO:0000269|PubMed:26920761}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in tachyzoites (at protein level).
CC {ECO:0000269|PubMed:26920761}.
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 Across 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 PubMed:29505111). Tachyzoites from type I and III strains associate
CC with host mitochondria (HMA(+)), while tachyzoites from type II
CC strains, such as ME49, do not associate with host mitochondria (HMA(-))
CC due to a lack of MAF1 b1 expression (PubMed:26920761).
CC {ECO:0000269|PubMed:26920761, ECO:0000269|PubMed:29505111}.
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DR EMBL; KX255416; ANN02899.1; -; mRNA.
DR EMBL; LT601556; SCA78655.1; -; mRNA.
DR EMBL; JAAUHK010000187; KAF4645529.1; -; Genomic_DNA.
DR PDB; 6BXS; X-ray; 2.10 A; A/B/C=159-435.
DR PDB; 6BXT; X-ray; 2.70 A; A/B/C=159-435.
DR PDBsum; 6BXS; -.
DR PDBsum; 6BXT; -.
DR SMR; A0A193AUK9; -.
DR VEuPathDB; ToxoDB:TGARI_323100; -.
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_410370; -.
DR VEuPathDB; ToxoDB:TGMAS_279100; -.
DR VEuPathDB; ToxoDB:TGME49_279100; -.
DR VEuPathDB; ToxoDB:TGP89_422200; -.
DR VEuPathDB; ToxoDB:TGP89_422480; -.
DR VEuPathDB; ToxoDB:TGPRC2_279100B; -.
DR VEuPathDB; ToxoDB:TGRH88_000180; -.
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 OMA; HGFTALY; -.
DR Proteomes; UP000557509; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Signal; Tachyzoite; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..435
FT /note="Mitochondrial association factor 1 form a1"
FT /evidence="ECO:0000255"
FT /id="PRO_5014534606"
FT TOPO_DOM 21..95
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 420..435
FT /note="RGLMESERKYKFPQGD->HGLQEAESTYLASMLD: Does not confer
FT host membrane association (HMA)."
FT /evidence="ECO:0000269|PubMed:29505111"
FT CONFLICT 14
FT /note="A -> V (in Ref. 2; KAF4645529)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="P -> L (in Ref. 2; KAF4645529)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="K -> T (in Ref. 2; KAF4645529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47888 MW; 9E3C78CF81886BA1 CRC64;
MWRIWRCRLS FLFATGCLLG ALTAGLGSQM SDSVGRNVQA PAGVADASQE AGDVVEERTE
RTEEQVFAPG PPRRHSSESL FPRNASVTAR RRRNRRIAPI ATAVGVAVIL AALYVLRRRR
AQPPQEPEPP TRLRTPRPRA PSEQQQPSES EPPAEVPMTP DPLTLRFTCL GDRNVIFFGP
SGRQDGFTPL YDPSPSKRVA TVDAGTYGLF IGGVGMNGEF ADTIIEEARR NRIPLTATEL
SAESQEIQER LLHDAERQPG TLVEIDSGRF SRVFARSFAY VAIVPNTVWD ESETGKNVGA
TFLHILKPEV TPHGNEMNDV MLYTVAPFGN ASDSAYNMAY KATMLGIVGA VSEYNKTPWG
EVKPVEAIRL PLLGAGHFRG RRGLHSIGRA NAVAVEAAIT RFDPRVELQF MYEPSDTALR
GLMESERKYK FPQGD
