MFTC_MOUSE
ID MFTC_MOUSE Reviewed; 316 AA.
AC Q8BMG8; Q3TCM5;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mitochondrial folate transporter/carrier;
DE AltName: Full=Solute carrier family 25 member 32;
GN Name=Slc25a32; Synonyms=Mftc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Forelimb, Placenta, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=29666258; DOI=10.1073/pnas.1800138115;
RA Kim J., Lei Y., Guo J., Kim S.E., Wlodarczyk B.J., Cabrera R.M., Lin Y.L.,
RA Nilsson T.K., Zhang T., Ren A., Wang L., Yuan Z., Zheng Y.F., Wang H.Y.,
RA Finnell R.H.;
RT "Formate rescues neural tube defects caused by mutations in Slc25a32.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:4690-4695(2018).
CC -!- FUNCTION: Transports folate across the inner membranes of mitochondria
CC (PubMed:15140890, PubMed:29666258). Can also transport FAD across the
CC mitochondrial inner membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q9H2D1, ECO:0000269|PubMed:15140890,
CC ECO:0000269|PubMed:29666258}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:29666258}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:29666258). Induces
CC morphological abnormalities of neural tube defects in the entire head
CC region of developing mouse embryos (PubMed:29666258).
CC {ECO:0000269|PubMed:29666258}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK031187; BAC27295.1; -; mRNA.
DR EMBL; AK167501; BAE39577.1; -; mRNA.
DR EMBL; AK170643; BAE41931.1; -; mRNA.
DR EMBL; AK172029; BAE42785.1; -; mRNA.
DR CCDS; CCDS27443.1; -.
DR RefSeq; NP_765990.2; NM_172402.3.
DR AlphaFoldDB; Q8BMG8; -.
DR SMR; Q8BMG8; -.
DR STRING; 10090.ENSMUSP00000022908; -.
DR iPTMnet; Q8BMG8; -.
DR PhosphoSitePlus; Q8BMG8; -.
DR EPD; Q8BMG8; -.
DR MaxQB; Q8BMG8; -.
DR PaxDb; Q8BMG8; -.
DR PeptideAtlas; Q8BMG8; -.
DR PRIDE; Q8BMG8; -.
DR ProteomicsDB; 295895; -.
DR DNASU; 69906; -.
DR Ensembl; ENSMUST00000022908; ENSMUSP00000022908; ENSMUSG00000022299.
DR GeneID; 69906; -.
DR KEGG; mmu:69906; -.
DR UCSC; uc007vob.2; mouse.
DR CTD; 81034; -.
DR MGI; MGI:1917156; Slc25a32.
DR VEuPathDB; HostDB:ENSMUSG00000022299; -.
DR eggNOG; KOG0764; Eukaryota.
DR GeneTree; ENSGT00920000149145; -.
DR HOGENOM; CLU_015166_6_4_1; -.
DR InParanoid; Q8BMG8; -.
DR OMA; GLYFLWY; -.
DR OrthoDB; 1080385at2759; -.
DR PhylomeDB; Q8BMG8; -.
DR TreeFam; TF314217; -.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR BioGRID-ORCS; 69906; 13 hits in 70 CRISPR screens.
DR ChiTaRS; Slc25a32; mouse.
DR PRO; PR:Q8BMG8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BMG8; protein.
DR Bgee; ENSMUSG00000022299; Expressed in secondary oocyte and 62 other tissues.
DR ExpressionAtlas; Q8BMG8; baseline and differential.
DR Genevisible; Q8BMG8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015230; F:FAD transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008517; F:folic acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904947; P:folate import into mitochondrion; IMP:UniProtKB.
DR GO; GO:1990548; P:mitochondrial FAD transmembrane transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..316
FT /note="Mitochondrial folate transporter/carrier"
FT /id="PRO_0000090643"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 20..109
FT /note="Solcar 1"
FT REPEAT 118..209
FT /note="Solcar 2"
FT REPEAT 222..306
FT /note="Solcar 3"
FT SITE 91
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:Q6IZB5"
FT SITE 142
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:Q6IZB5"
FT SITE 249
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:Q6IZB5"
SQ SEQUENCE 316 AA; 35049 MW; 58D18DFBAC6B169E CRC64;
MTGQGQSAAG SAAWSAVFRH VRYENLVAGV SGGVLSNLAL HPLDLVKIRF AVSDGLEVRP
KYKGILHCLA TIWKVDGLRG LYQGVTPNVW GAGLSWGLYF FFYNAIKSYK TEGRAEQLEP
LEYLVSAAEA GAMTLCITNP LWVTKTRLML QYGGVASPSQ RQYKGMFDAL VKIYKYEGVR
GLYKGFVPGL FGTSHGALQF MAYELLKLKY NKHINRLPEA QLSTAEYISV AALSKIFAVA
ATYPYQVVRA RLQDQHVSYG GVTDVITKTW RKEGIGGFYK GIAPNLIRVT PACCITFVVY
ENVSHFLYDL REKKVS
