SFXN1_RAT
ID SFXN1_RAT Reviewed; 322 AA.
AC Q63965;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sideroflexin-1;
DE AltName: Full=Tricarboxylate carrier protein {ECO:0000303|PubMed:8132491};
DE Short=TCC {ECO:0000303|PubMed:8132491};
GN Name=Sfxn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CAUTION.
RC TISSUE=Liver;
RX PubMed=8132491; DOI=10.1007/bf01108408;
RA Azzi A., Glerum M., Koller R., Mertens W., Spycher S.;
RT "The mitochondrial tricarboxylate carrier.";
RL J. Bioenerg. Biomembr. 25:515-524(1993).
RN [2]
RP CAUTION.
RX PubMed=30442778; DOI=10.1126/science.aat9528;
RA Kory N., Wyant G.A., Prakash G., Uit de Bos J., Bottanelli F., Pacold M.E.,
RA Chan S.H., Lewis C.A., Wang T., Keys H.R., Guo Y.E., Sabatini D.M.;
RT "SFXN1 is a mitochondrial serine transporter required for one-carbon
RT metabolism.";
RL Science 362:0-0(2018).
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}.
CC -!- CAUTION: Originally identified from a mitochondrial tricarboxylate
CC carrier purification (PubMed:8132491). The physiological relevance of
CC this remains unclear (PubMed:30442778). {ECO:0000269|PubMed:8132491,
CC ECO:0000303|PubMed:30442778}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB30258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S70011; AAB30258.1; ALT_INIT; mRNA.
DR PIR; I55210; I55210.
DR AlphaFoldDB; Q63965; -.
DR IntAct; Q63965; 2.
DR MINT; Q63965; -.
DR STRING; 10116.ENSRNOP00000024707; -.
DR CarbonylDB; Q63965; -.
DR SwissPalm; Q63965; -.
DR jPOST; Q63965; -.
DR PaxDb; Q63965; -.
DR PRIDE; Q63965; -.
DR RGD; 1308482; Sfxn1.
DR eggNOG; KOG3767; Eukaryota.
DR InParanoid; Q63965; -.
DR PhylomeDB; Q63965; -.
DR PRO; PR:Q63965; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0042945; F:D-serine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; ISS:UniProtKB.
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:0042942; P:D-serine transport; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0006826; P:iron ion transport; ISO:RGD.
DR GO; GO:0015808; P:L-alanine transport; ISS:UniProtKB.
DR GO; GO:0015825; P:L-serine transport; ISS:UniProtKB.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; ISS:UniProtKB.
DR GO; GO:0140300; P:serine import into mitochondrion; ISS:UniProtKB.
DR InterPro; IPR004686; Mtc.
DR PANTHER; PTHR11153; PTHR11153; 1.
DR Pfam; PF03820; SFXNs; 1.
DR TIGRFAMs; TIGR00798; mtc; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Amino-acid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; One-carbon metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B4"
FT CHAIN 2..322
FT /note="Sideroflexin-1"
FT /id="PRO_0000177034"
FT TOPO_DOM 2..102
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B4"
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..146
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..228
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..266
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..322
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B4"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B4"
SQ SEQUENCE 322 AA; 35546 MW; D28CBD898E8ABC5D CRC64;
MSGEVPPNIN IKEPRWDQST FIGRASHFFT VTDPKNILLT NEQLENARKV VHDYRQGIVP
AGLTENELWR AKYAYDSAFH PDTGEKMTLI GRMSAQVPMN MTITGCMMTF YRTTPAVLFW
QWINQSFNAV VNYTNRSGDA PLTVNELGTA YVSATTGAVA TALGLNALTK HVSPLIGRFV
PFAAVAAANC INIPLMRQRE LKVGIPVTDE NGTRLGESTN AAKQAITQVV ISRILMAAPG
MAIPPFIMNT LEKKAFLKRF PWMSAPIQVT LVGFCLVFAT PLCCALFPQK SSMSVTSLED
DLQASIQKSH PELRRVYFNK GL
