SFXN1_CAEEL
ID SFXN1_CAEEL Reviewed; 329 AA.
AC Q09201;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sideroflexin-1.1 {ECO:0000305};
GN Name=sfxn-1.1 {ECO:0000312|WormBase:AH6.2}; ORFNames=AH6.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Amino acid transporter importing serine, an essential
CC substrate of the mitochondrial branch of the one-carbon pathway, into
CC mitochondria. Mitochondrial serine is then converted to glycine and
CC formate, which exits to the cytosol where it is used to generate the
CC charged folates that serve as one-carbon donors. May also transport
CC other amino acids including alanine and cysteine.
CC {ECO:0000250|UniProtKB:Q9H9B4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000250|UniProtKB:Q9H9B4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719,
CC ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q9H9B4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) = L-cysteine(out); Xref=Rhea:RHEA:29655,
CC ChEBI:CHEBI:35235; Evidence={ECO:0000250|UniProtKB:Q9H9B4};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9H9B4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
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DR EMBL; Z48009; CAA88076.1; -; Genomic_DNA.
DR PIR; T18612; T18612.
DR RefSeq; NP_496040.1; NM_063639.1.
DR AlphaFoldDB; Q09201; -.
DR BioGRID; 46677; 2.
DR DIP; DIP-25194N; -.
DR STRING; 6239.AH6.2; -.
DR TCDB; 2.A.54.1.2; the sideroflexin (sfxn) family (formerly the mitochondrial tricarboxylate carrier (mtc) family.
DR PaxDb; Q09201; -.
DR EnsemblMetazoa; AH6.2.1; AH6.2.1; WBGene00007080.
DR GeneID; 181807; -.
DR KEGG; cel:CELE_AH6.2; -.
DR CTD; 181807; -.
DR WormBase; AH6.2; CE01456; WBGene00007080; sfxn-1.1.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR HOGENOM; CLU_039425_1_0_1; -.
DR InParanoid; Q09201; -.
DR OMA; AIAVANC; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q09201; -.
DR PRO; PR:Q09201; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007080; Expressed in material anatomical entity and 2 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0022889; F:serine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IBA:GO_Central.
DR GO; GO:0140300; P:serine import into mitochondrion; IBA:GO_Central.
DR InterPro; IPR004686; Mtc.
DR PANTHER; PTHR11153; PTHR11153; 1.
DR Pfam; PF03820; SFXNs; 1.
DR TIGRFAMs; TIGR00798; mtc; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..329
FT /note="Sideroflexin-1.1"
FT /id="PRO_0000177046"
FT TRANSMEM 100..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 329 AA; 36755 MW; 0F2D38989D438288 CRC64;
MNNLVVNQTV LPDISKPKWD QGTYAGRAKH FFSSTNPLTL FSSRIQQEKC KEIVTNYKTG
VISPTLTVDE LWKAKTLYDS TYHPDTGEKM FFLGRMSAQM PGNMVTTGML LGLYRTLPGV
VFSHWFNQSF NAVVNYTNRS GNSKATNERL FVSYCCATSG AMTVALGLNK MVKNSHGLAA
RLVPFAAIAL ANAINIPMMR SNEASEGMEL KDENDQLVGK SQKMAALSIA QVTLSRIAMA
MPYMVMTPII MNRITRTAYY RTRPWMQKYS EIPIQTLIAG IGLYFTTPLC CALFPQKSSV
EVEKLESSVQ KEIMSRPNPP KIVYYNKGL