MAFA1_TOXGM
ID MAFA1_TOXGM Reviewed; 435 AA.
AC S8GJB7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Mitochondrial association factor 1 form a1 {ECO:0000303|PubMed:26920761};
DE Short=MAF1ME49a1 allele {ECO:0000303|PubMed:26920761};
DE Flags: Precursor;
GN Name=MAF1a1 {ECO:0000303|PubMed:26920761};
GN Synonyms=MAF1 {ECO:0000303|PubMed:26920761};
GN ORFNames=TGME49_279100 {ECO:0000312|EMBL:EPT31950.1};
OS Toxoplasma gondii (strain ATCC 50611 / Me49).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=508771 {ECO:0000312|Proteomes:UP000001529};
RN [1] {ECO:0000312|Proteomes:UP000001529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50611 / Me49 {ECO:0000312|Proteomes:UP000001529};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NOMENCLATURE, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP POLYMORPHISM.
RC STRAIN=ATCC 50611 / Me49 {ECO:0000269|PubMed:26920761};
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).
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}.
CC -!- SUBUNIT: Interacts with host SAMM50.
CC {ECO:0000250|UniProtKB:A0A193AUK9}.
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 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; KE138816; EPT31950.1; -; Genomic_DNA.
DR RefSeq; XP_018638253.1; XM_018781832.1.
DR SwissPalm; S8GJB7; -.
DR EnsemblProtists; TGME49_279100-t26_1; TGME49_279100-t26_1; TGME49_279100.
DR GeneID; 29769515; -.
DR KEGG; tgo:TGME49_279100; -.
DR VEuPathDB; ToxoDB:TGME49_279100; -.
DR HOGENOM; CLU_051602_0_0_1; -.
DR PhylomeDB; S8GJB7; -.
DR Proteomes; UP000001529; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Membrane; Signal; Tachyzoite; Transmembrane; 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_5004551867"
FT TOPO_DOM 21..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; 47694 MW; D42DA013AA00E95A CRC64;
MWRIWRCRLS FLFATGCLLG ALTAGLGSQM SDSVGRNVQA PAGVADASQE AGDVVEERTE
RTEQQVFALG PPRRHSSESL FPRNASVTAR RRRNRRIALI ATAVGVAVIL AALYVLRRRR
AQPPQEPEPP TRLRTPRPRA PSGQQQPSES EPPAGVPMTP GFLTLPFTCL RDTKVTFFGP
SGRQHGFTAL YDPSPNKRVA TVDAGTNRLF IGGGGMNGEF ANTIIEEARR NRIPLTATEL
SAESQEIQER LLRDAERRPG TLVEIDSGRF SRVFARSFAY VAIVPNTVWD ESETGKNVGA
TFLHILKPEV TPHGNQMNDV MLYTVAPLGN ASDSAYNLAY KATMLGIVGA VSEYNKTPWG
EVKPVEAIRL PLLGAGHFRG RRGLHSIGRA NAVAVEAAIT RFDPRVELQF MYEPSDAALR
GLMESERTYT FPQGD
