ID   SFXN1_SHEEP             Reviewed;         322 AA.
AC   B2LU20;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Sideroflexin-1;
GN   Name=SFXN1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Deng W.;
RT   "Molecular clone and sequence analysis of SFXN1 from black-boned sheep
RT   (Ovis aries).";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU583468; ACB97620.1; -; mRNA.
DR   RefSeq; NP_001119822.1; NM_001126350.1.
DR   AlphaFoldDB; B2LU20; -.
DR   STRING; 9940.ENSOARP00000017892; -.
DR   GeneID; 100145864; -.
DR   KEGG; oas:100145864; -.
DR   CTD; 94081; -.
DR   eggNOG; KOG3767; Eukaryota.
DR   OrthoDB; 881974at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
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:0015808; P:L-alanine transport; ISS:UniProtKB.
DR   GO; GO:0015825; P:L-serine transport; ISS:UniProtKB.
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_0000350611"
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;  35581 MW;  EA892ADC8F3FDA35 CRC64;
     MSGELPPNIN IKEPRWDQST FIGRAKHFFT VTDPRNILLT NAQLEAARKV VHDYRQGIVP
     SGLTENELWR AKYIYDSAFH PDTGEKMILI GRMSAQVPMN MTITGCMMTF YRTTPAVLFW
     QWVNQSFNAV VNYTNRSGDA PLTVNELGTA YVSATTGAVA TALGLNALTK RVSPLVGRFV
     PFAAVAAANC INIPLMRQRE LKVGIPVTDE NGNRLGESAS AAKQAITQVV VSRILMAAPG
     MAIPPFIMNT LEKKAFLKRF PWMSAPVQVG IVGFCLVFAT PLCCALFPQK SSMSVTSLEA
     ELQARIRETY PELRRVYFNK GL