ID G3QSS8_GORGO Unreviewed; 359 AA.
AC G3QSS8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Mitochondrial glutathione transporter SLC25A39 {ECO:0000256|RuleBase:RU369018};
DE AltName: Full=Solute carrier family 25 member 39 {ECO:0000256|RuleBase:RU369018};
GN Name=SLC25A39 {ECO:0000313|Ensembl:ENSGGOP00000005726.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000005726.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000005726.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000005726.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000005726.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mitochondrial transporter required for glutathione import
CC into mitochondria. Glutathione, which plays key roles in oxidative
CC metabolism, is produced exclusively in the cytosol and is imported in
CC many organelles. Mitochondrial glutathione is required for the activity
CC and stability of proteins containing iron-sulfur clusters, as well as
CC erythropoiesis. {ECO:0000256|RuleBase:RU369018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione(in) = glutathione(out); Xref=Rhea:RHEA:74819,
CC ChEBI:CHEBI:57925; Evidence={ECO:0000256|ARBA:ARBA00036017};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448,
CC ECO:0000256|RuleBase:RU369018}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU369018}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU369018}.
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DR EMBL; CABD030037676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004041616.1; XM_004041568.2.
DR AlphaFoldDB; G3QSS8; -.
DR Ensembl; ENSGGOT00000005876.3; ENSGGOP00000005726.2; ENSGGOG00000005843.3.
DR GeneID; 101134102; -.
DR CTD; 51629; -.
DR eggNOG; KOG0761; Eukaryota.
DR GeneTree; ENSGT00940000156382; -.
DR HOGENOM; CLU_015166_0_0_1; -.
DR OrthoDB; 3490716at2759; -.
DR TreeFam; TF314720; -.
DR Proteomes; UP000001519; Chromosome 5.
DR Bgee; ENSGGOG00000005843; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IEA:InterPro.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR045315; Mtm1-like.
DR PANTHER; PTHR45760; FI19922P1-RELATED; 1.
DR PANTHER; PTHR45760:SF1; MITOCHONDRIAL GLUTATHIONE TRANSPORTER SLC25A39-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 4.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Mitochondrion {ECO:0000256|RuleBase:RU369018};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU369018};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|RuleBase:RU369018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|RuleBase:RU369018};
KW Transport {ECO:0000256|RuleBase:RU000488}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369018"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369018"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369018"
FT TRANSMEM 255..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369018"
FT REPEAT 9..151
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 159..243
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 253..347
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 359 AA; 39244 MW; 746AE398F95514BF CRC64;
MADQDPAGIS PLQQMVASGA GAVVTSLFMT PLDVVKVRLQ SQRPSMASEL MPSSRLWSLS
YTKLPSSLQS TGKCLLYCNG VLEPLYLCPN GARCATWFQD PTRFTGTMDA FVKIVRHEGT
RTLWSGLPAT LVMTVPATAI YFTAYDQLKA FLCGRALTSD LYAPMVAGAL ARLGTVTVIS
PLELMRTKLQ AQHVSYRELG ACVRTAVAQG GWRSLWLGWG PTALRDVPFS ALYWFNYELV
KSWLNGLRRK DQTSVGMSFV AGGISGTVAA VLTLPFDVVK TQRQVALGAM EAVRVNPLHV
DSTWLLLRRI RAESGTKGLF AGFLPRIIKA APSCAIMIST YEFGKSFFQR LNQDRLLGG
//
