MFTC_CRIGR
ID MFTC_CRIGR Reviewed; 316 AA.
AC Q6IZB5;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Mitochondrial folate transporter/carrier;
DE AltName: Full=Solute carrier family 25 member 32;
GN Name=SLC25A32; Synonyms=MFTC;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-192, AND FUNCTION.
RX PubMed=15140890; DOI=10.1074/jbc.m403677200;
RA McCarthy E.A., Titus S.A., Taylor S.M., Jackson-Cook C., Moran R.G.;
RT "A mutation inactivating the mitochondrial inner membrane folate
RT transporter creates a glycine requirement for survival of chinese hamster
RT cells.";
RL J. Biol. Chem. 279:33829-33836(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, VARIANT GLU-192, AND MUTAGENESIS OF ARG-19;
RP HIS-41; SER-95; ARG-114; GLU-129; LYS-184; GLU-209; GLU-219; ARG-249 AND
RP HIS-256.
RX PubMed=17279620; DOI=10.1021/bi062191+;
RA Perchiniak E., Lawrence S.A., Kasten S., Woodard B.A., Taylor S.M.,
RA Moran R.G.;
RT "Probing the mechanism of the hamster mitochondrial folate transporter by
RT mutagenesis and homology modeling.";
RL Biochemistry 46:1557-1567(2007).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-91; TRP-96; TRP-142;
RP PHE-200; LYS-235; ARG-249; ARG-288 AND TYR-300.
RX PubMed=21768094; DOI=10.1074/jbc.m111.272187;
RA Lawrence S.A., Hackett J.C., Moran R.G.;
RT "Tetrahydrofolate recognition by the mitochondrial folate transporter.";
RL J. Biol. Chem. 286:31480-31489(2011).
CC -!- FUNCTION: Transports folate across the inner membranes of mitochondria
CC (PubMed:15140890, PubMed:17279620, PubMed:21768094). Can also transport
CC FAD across the mitochondrial inner membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q9H2D1, ECO:0000269|PubMed:15140890,
CC ECO:0000269|PubMed:17279620, ECO:0000269|PubMed:21768094}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17279620, ECO:0000269|PubMed:21768094}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AY611603; AAT42021.1; -; mRNA.
DR RefSeq; NP_001233717.1; NM_001246788.1.
DR AlphaFoldDB; Q6IZB5; -.
DR SMR; Q6IZB5; -.
DR STRING; 10029.NP_001233717.1; -.
DR Ensembl; ENSCGRT00001007555; ENSCGRP00001004967; ENSCGRG00001006441.
DR Ensembl; ENSCGRT00015044283; ENSCGRP00015036324; ENSCGRG00015027224.
DR GeneID; 100689360; -.
DR KEGG; cge:100689360; -.
DR CTD; 81034; -.
DR GeneTree; ENSGT00920000149145; -.
DR OrthoDB; 1080385at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008517; F:folic acid transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:1904947; P:folate import into mitochondrion; IMP:UniProtKB.
DR GO; GO:1990548; P:mitochondrial FAD transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR044712; SLC25A32-like.
DR PANTHER; PTHR45683; PTHR45683; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..316
FT /note="Mitochondrial folate transporter/carrier"
FT /id="PRO_0000448880"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 20..109
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 118..209
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 222..306
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT SITE 91
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000269|PubMed:21768094"
FT SITE 142
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000269|PubMed:21768094"
FT SITE 249
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000269|PubMed:21768094"
FT VARIANT 192
FT /note="G -> E (in cell line CHO-glyB; loss of folate
FT transport into mitochondria; no effect on its mitochondrial
FT localization)"
FT /evidence="ECO:0000269|PubMed:15140890"
FT MUTAGEN 19
FT /note="R->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 41
FT /note="H->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 91
FT /note="G->L,R: Significant decrease in folate transport
FT into mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 95
FT /note="S->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 96
FT /note="W->A: Significant decrease in folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 114
FT /note="R->A: No significant effect on transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 129
FT /note="E->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 142
FT /note="W->A,R,D: Significant decrease in folate transport
FT into mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 142
FT /note="W->F: Significant increase in folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 184
FT /note="K->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 200
FT /note="F->A: Significant decrease in folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 209
FT /note="E->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 219
FT /note="E->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 235
FT /note="K->A: Significant decrease in folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 249
FT /note="R->A: Significant decrease in folate transport into
FT mitochondria. No effect on its mitochondrial localization."
FT /evidence="ECO:0000269|PubMed:17279620,
FT ECO:0000269|PubMed:21768094"
FT MUTAGEN 256
FT /note="H->A: No significant effect on folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17279620"
FT MUTAGEN 288
FT /note="R->A: Significant decrease in folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
FT MUTAGEN 300
FT /note="Y->A: Significant decrease in folate transport into
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:21768094"
SQ SEQUENCE 316 AA; 35125 MW; 7011CCEB6C4C25AA CRC64;
MTGQGQPAAG SAAWSTVFRH VRYENLVAGV SGGVLSNLAL HPLDLVKIRF AVSDGLEVRP
KYKGILHCLT TIWKVEGLRG LYQGVTPNVW GAGLSWGLYF FFYNAIKSYK TEGRAEQLEP
LEYLVSAAEA GAMTLCITNP LWVTKTRLML QYGGVVNPSQ RQYKGMFDAL VKIYKYEGVR
GLYKGFVPGL FGTSHGALQF MAYELLKLEY NKHINRLPEA QLSTPEYISV AALSKIFAVA
ATYPYQVVRA RLQDQHVSYG GVMDVIVKTW RKEGIGGFYK GIAPNLIRVT PACCITFVVY
ENVSHFLCGL REKKVS