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Database: UniProt
Entry: H2QD69_PANTR
LinkDB: H2QD69_PANTR
Original site: H2QD69_PANTR 
ID   H2QD69_PANTR            Unreviewed;       359 AA.
AC   H2QD69; A0A2J8J4J2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 74.
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|EMBL:JAA11175.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000015771.5, ECO:0000313|VGNC:VGNC:9620};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000015771.5, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000015771.5, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA11175.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA11175.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA42216.1}, Skin {ECO:0000313|EMBL:JAA27576.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA15712.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000015771.5}
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; AACZ04050588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01000163; JAA11175.1; -; mRNA.
DR   EMBL; GABF01006433; JAA15712.1; -; mRNA.
DR   EMBL; GABD01005524; JAA27576.1; -; mRNA.
DR   EMBL; GABE01002523; JAA42216.1; -; mRNA.
DR   RefSeq; XP_016787153.1; XM_016931664.1.
DR   STRING; 9598.ENSPTRP00000075114; -.
DR   PaxDb; 9598-ENSPTRP00000015771; -.
DR   Ensembl; ENSPTRT00000017037.6; ENSPTRP00000015771.5; ENSPTRG00000009272.6.
DR   GeneID; 739075; -.
DR   CTD; 51629; -.
DR   VGNC; VGNC:9620; SLC25A39.
DR   eggNOG; KOG0761; Eukaryota.
DR   GeneTree; ENSGT00940000156382; -.
DR   HOGENOM; CLU_015166_0_0_1; -.
DR   OrthoDB; 3490716at2759; -.
DR   TreeFam; TF314720; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000009272; Expressed in cortex of kidney and 21 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   2: Evidence at transcript level;
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:UP000002277};
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   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;  39217 MW;  1B19E541D7B74454 CRC64;
     MADQDPAGIS PLQQMVASGA GAVVTSLFMT PLDVVKVRLQ SQRPSMASEL MPSSRLWSLS
     YTKLPFSLQS TGKCLLYCNG VLEPLYLCPN GARCATWFQD PTRFTGTMDA FVKIVRHEGT
     RTLWSGLPAT LVMTVPATAI YFTAYDQLKA FLCGRALTSD LYAPMVAGAL ARLGTVTVIS
     PLELMRTKLQ AQHVSYRELG ACVRTAVAQG GWRSLWLGWG PTALRDVPFS ALYWFNYELV
     KSWLNGLRPK DQTSVGMSFV AGGISGTVAA VLTLPFDVVK TQRQVALGAM EAVRVNPLHV
     DSTWLLLQRI RAESGTKGLF AGFLPRIIKA APSCAIMIST YEFGKSFFQR LNQDRLLGG
//
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