SFXN2_MOUSE
ID SFXN2_MOUSE Reviewed; 322 AA.
AC Q925N2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sideroflexin-2 {ECO:0000303|PubMed:11274051};
GN Name=Sfxn2 {ECO:0000303|PubMed:11274051, ECO:0000312|MGI:MGI:2137678};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11274051; DOI=10.1101/gad.873001;
RA Fleming M.D., Campagna D.R., Haslett J.N., Trenor C.C. III, Andrews N.C.;
RT "A mutation in a mitochondrial transmembrane protein is responsible for the
RT pleiotropic hematological and skeletal phenotype of flexed-tail (f/f)
RT mice.";
RL Genes Dev. 15:652-657(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=30570704; DOI=10.1007/s12576-018-0652-2;
RA Mon E.E., Wei F.Y., Ahmad R.N.R., Yamamoto T., Moroishi T., Tomizawa K.;
RT "Regulation of mitochondrial iron homeostasis by sideroflexin 2.";
RL J. Physiol. Sci. 69:359-373(2019).
CC -!- FUNCTION: Mitochondrial amino-acid transporter that mediates transport
CC of serine into mitochondria (By similarity). Involved in mitochondrial
CC iron homeostasis by regulating heme biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q96NB2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000250|UniProtKB:Q96NB2};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q96NB2}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96NB2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, spleen, thymus,
CC liver, stomach and skin. {ECO:0000269|PubMed:11274051,
CC ECO:0000269|PubMed:30570704}.
CC -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
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DR EMBL; AF325261; AAK39429.1; -; mRNA.
DR EMBL; BC019808; AAH19808.1; -; mRNA.
DR CCDS; CCDS29880.1; -.
DR RefSeq; NP_444426.3; NM_053196.3.
DR AlphaFoldDB; Q925N2; -.
DR BioGRID; 220498; 1.
DR STRING; 10090.ENSMUSP00000026011; -.
DR iPTMnet; Q925N2; -.
DR PhosphoSitePlus; Q925N2; -.
DR SwissPalm; Q925N2; -.
DR jPOST; Q925N2; -.
DR MaxQB; Q925N2; -.
DR PaxDb; Q925N2; -.
DR PRIDE; Q925N2; -.
DR ProteomicsDB; 257213; -.
DR Antibodypedia; 18077; 81 antibodies from 17 providers.
DR DNASU; 94279; -.
DR Ensembl; ENSMUST00000026011; ENSMUSP00000026011; ENSMUSG00000025036.
DR GeneID; 94279; -.
DR KEGG; mmu:94279; -.
DR UCSC; uc008htu.1; mouse.
DR CTD; 118980; -.
DR MGI; MGI:2137678; Sfxn2.
DR VEuPathDB; HostDB:ENSMUSG00000025036; -.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR HOGENOM; CLU_039425_1_0_1; -.
DR InParanoid; Q925N2; -.
DR OMA; RIVMCAP; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q925N2; -.
DR TreeFam; TF313205; -.
DR BioGRID-ORCS; 94279; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Sfxn2; mouse.
DR PRO; PR:Q925N2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q925N2; protein.
DR Bgee; ENSMUSG00000025036; Expressed in rostral migratory stream and 246 other tissues.
DR ExpressionAtlas; Q925N2; baseline and differential.
DR Genevisible; Q925N2; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Amino-acid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..322
FT /note="Sideroflexin-2"
FT /id="PRO_0000177036"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB2"
FT CONFLICT 3
FT /note="G -> A (in Ref. 2; AAH19808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 36141 MW; 00D6236898BB983C CRC64;
MEGDLSGFNI DAPRWDQCTF LGRVKHFFNI TDPRTVFASE QELDWAKAVV EKSRMGLVPP
GTQMEQLLYA KKLYDSAFHP DTGEKMNVIG RMSFQVPGGM LITGFMLQFY RTMPAVIFWQ
WVNQSFNALV NYTNRNAASP TSVRQMALSY FTATTTAVAT AVGMNMWTKR APPLVGRWVP
FAAVAAANCV NIPMMRQQEL IQGICVKDRN QNELGHSQRA AAVGIAQVVI SRITMAAPGM
ILLPVIMERL ERLHLMKKVK VMHAPLQVLL CGCFLLFMVP VACGLFPQEC ELSVSYLEPE
LRDTIKAKYG EQVLFVYFNK GL
