S2539_MOUSE
ID S2539_MOUSE Reviewed; 359 AA.
AC Q9D8K8; Q3TTM8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable mitochondrial glutathione transporter SLC25A39 {ECO:0000305};
DE AltName: Full=Solute carrier family 25 member 39 {ECO:0000305};
GN Name=Slc25a39 {ECO:0000312|MGI:MGI:1196386};
GN Synonyms=D11Ertd333e {ECO:0000312|MGI:MGI:1196386};
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; TISSUE=Pancreas, Testis, and Wolffian duct;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19656490; DOI=10.1016/j.cmet.2009.06.012;
RA Nilsson R., Schultz I.J., Pierce E.L., Soltis K.A., Naranuntarat A.,
RA Ward D.M., Baughman J.M., Paradkar P.N., Kingsley P.D., Culotta V.C.,
RA Kaplan J., Palis J., Paw B.H., Mootha V.K.;
RT "Discovery of genes essential for heme biosynthesis through large-scale
RT gene expression analysis.";
RL Cell Metab. 10:119-130(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=34707288; DOI=10.1038/s41586-021-04025-w;
RA Wang Y., Yen F.S., Zhu X.G., Timson R.C., Weber R., Xing C., Liu Y.,
RA Allwein B., Luo H., Yeh H.W., Heissel S., Unlu G., Gamazon E.R.,
RA Kharas M.G., Hite R., Birsoy K.;
RT "SLC25A39 is necessary for mitochondrial glutathione import in mammalian
RT cells.";
RL Nature 599:136-140(2021).
CC -!- FUNCTION: Mitochondrial transporter required for glutathione import
CC into mitochondria (By similarity). Glutathione, which plays key roles
CC in oxidative metabolism, is produced exclusively in the cytosol and is
CC imported in many organelles (By similarity). Mitochondrial glutathione
CC is required for the activity and stability of proteins containing iron-
CC sulfur clusters, as well as erythropoiesis (PubMed:34707288).
CC {ECO:0000250|UniProtKB:Q9BZJ4, ECO:0000269|PubMed:34707288}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9BZJ4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Abundant expression in bone marrow, spleen, testis
CC and kidney. {ECO:0000269|PubMed:19656490}.
CC -!- DEVELOPMENTAL STAGE: Highly express in primitive erythroblast that fill
CC yorlk sac blood islands at early somite pair stages, and in fetal liver
CC at 12.5 dpc. {ECO:0000269|PubMed:19656490}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at dpc 13.5
CC (PubMed:34707288). Embryos are pale due to a severely anemic phenotype
CC (PubMed:34707288). Conditional deletion in the erythroid lineage also
CC leads to severe anemia, characterized by a complete absence of
CC Ter119(+) cells, iron overload and increased apoptosis in fetal liver
CC cells (PubMed:34707288). Cells lacking both Slc25a39 and Slc25a40 show
CC defects in the activity and stability of proteins containing iron-
CC sulfur clusters (PubMed:34707288). {ECO:0000269|PubMed:34707288}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AK007934; BAB25360.1; -; mRNA.
DR EMBL; AK078417; BAC37264.1; -; mRNA.
DR EMBL; AK161289; BAE36297.1; -; mRNA.
DR CCDS; CCDS25498.1; -.
DR RefSeq; NP_080818.1; NM_026542.3.
DR RefSeq; XP_006534097.1; XM_006534034.1.
DR RefSeq; XP_006534098.1; XM_006534035.1.
DR AlphaFoldDB; Q9D8K8; -.
DR SMR; Q9D8K8; -.
DR STRING; 10090.ENSMUSP00000018821; -.
DR iPTMnet; Q9D8K8; -.
DR PhosphoSitePlus; Q9D8K8; -.
DR MaxQB; Q9D8K8; -.
DR PaxDb; Q9D8K8; -.
DR PRIDE; Q9D8K8; -.
DR ProteomicsDB; 256668; -.
DR Antibodypedia; 17434; 42 antibodies from 16 providers.
DR DNASU; 68066; -.
DR Ensembl; ENSMUST00000018821; ENSMUSP00000018821; ENSMUSG00000018677.
DR GeneID; 68066; -.
DR KEGG; mmu:68066; -.
DR UCSC; uc007lrt.3; mouse.
DR CTD; 51629; -.
DR MGI; MGI:1196386; Slc25a39.
DR VEuPathDB; HostDB:ENSMUSG00000018677; -.
DR eggNOG; KOG0761; Eukaryota.
DR GeneTree; ENSGT00940000156382; -.
DR InParanoid; Q9D8K8; -.
DR OMA; DQTSVGA; -.
DR OrthoDB; 1007936at2759; -.
DR PhylomeDB; Q9D8K8; -.
DR TreeFam; TF314720; -.
DR BioGRID-ORCS; 68066; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Slc25a39; mouse.
DR PRO; PR:Q9D8K8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D8K8; protein.
DR Bgee; ENSMUSG00000018677; Expressed in right kidney and 172 other tissues.
DR ExpressionAtlas; Q9D8K8; baseline and differential.
DR Genevisible; Q9D8K8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0160007; P:glutathione import into mitochondrion; ISS:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR045315; Mtm1-like.
DR PANTHER; PTHR45760; PTHR45760; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Heme biosynthesis; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..359
FT /note="Probable mitochondrial glutathione transporter
FT SLC25A39"
FT /id="PRO_0000090597"
FT TRANSMEM 15..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 9..151
FT /note="Solcar 1"
FT REPEAT 159..243
FT /note="Solcar 2"
FT REPEAT 253..347
FT /note="Solcar 3"
SQ SEQUENCE 359 AA; 39221 MW; ED986C79395DBFCA CRC64;
MDDQDPGGIS PLQQMVASGA GAVVTSLFMT PLDVVKVRLQ SQRPSATSEL TTPSRFWSLS
YTKSSSALQS PGKCLLYCNG VLEPLYLCPN GTRCATWFQD PTRFTGTLDA FVKIVRHEGT
RTLWSGLPAT LVMTVPATAI YFTAYDQLKA FLCGQSLTSD LYAPMVAGAL ARMGTVTVVS
PLELVRTKLQ AQHVSYRELA SSVQAAVTQG GWRSLWLGWG PTALRDVPFS ALYWFNYELV
KSWLSGLRPK DQTSVGISFV AGGISGMVAA TLTLPFDVVK TQRQMSLGAV EAVRVKPPRV
DSTWLLLRRI RAESGTRGLF AGFLPRIIKA APSCAIMIST YEFGKSFFQR LNQEQPLGR
