SFXN1_BOVIN
ID SFXN1_BOVIN Reviewed; 322 AA.
AC Q5E9M8;
DT 22-AUG-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Sideroflexin-1;
GN Name=SFXN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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}.
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DR EMBL; BT020892; AAX08909.1; -; mRNA.
DR EMBL; BC103181; AAI03182.1; -; mRNA.
DR RefSeq; NP_001015574.1; NM_001015574.1.
DR AlphaFoldDB; Q5E9M8; -.
DR STRING; 9913.ENSBTAP00000019322; -.
DR PaxDb; Q5E9M8; -.
DR PeptideAtlas; Q5E9M8; -.
DR PRIDE; Q5E9M8; -.
DR Ensembl; ENSBTAT00000019322; ENSBTAP00000019322; ENSBTAG00000014536.
DR GeneID; 511375; -.
DR KEGG; bta:511375; -.
DR CTD; 94081; -.
DR VEuPathDB; HostDB:ENSBTAG00000014536; -.
DR VGNC; VGNC:34530; SFXN1.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR HOGENOM; CLU_039425_1_0_1; -.
DR InParanoid; Q5E9M8; -.
DR OMA; GRVRHCA; -.
DR OrthoDB; 881974at2759; -.
DR TreeFam; TF313205; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000014536; Expressed in liver and 102 other tissues.
DR ExpressionAtlas; Q5E9M8; baseline and differential.
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:0022889; F:serine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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_0000247974"
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; 35690 MW; 9C8F2DB1FDBE8D17 CRC64;
MSGELPPNIN IKEPRWDQST FIGRAKHFFT VTDPRNILLT NEQLEAARKV VHDYRQGIIP
SGLTENELWR AKYIYDSAFH PDTGEKMILI GRMSAQVPMN MTITGCMMTF YRTTPAVLFW
QWINQSFNAV VNYTNRSGDA PLTVNELGTA YVSATTGAVA TALGLNALTK HVSPLIGRFV
PFAAVAAANC INIPLMRQRE LKVGIPVTDE NGNRLGESAN AAKQAITQVV VSRILMAAPG
MAIPPFIMNT LEKKAFLKRF PWMSAPVQVG IVGFCLVFAT PLCCALFPQK SSMSVTSLEA
ELQARIRETY PELRRVYFNK GL
