SFXN3_MOUSE
ID SFXN3_MOUSE Reviewed; 321 AA.
AC Q91V61; Q544M7; Q8C1Z2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sideroflexin-3 {ECO:0000303|PubMed:11274051};
GN Name=Sfxn3 {ECO:0000303|PubMed:11274051, ECO:0000312|MGI:MGI:2137679};
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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 15-23; 55-69; 72-85; 178-196; 199-213; 223-252 AND
RP 303-319, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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).
CC -!- FUNCTION: Mitochondrial serine transporter that mediates transport of
CC serine into mitochondria, an important step of the one-carbon
CC metabolism pathway. Mitochondrial serine is converted to glycine and
CC formate, which then exits to the cytosol where it is used to generate
CC the charged folates that serve as one-carbon donors.
CC {ECO:0000250|UniProtKB:Q9BWM7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000250|UniProtKB:Q9BWM7};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9BWM7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91V61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91V61-2; Sequence=VSP_007388;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11274051}.
CC -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
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DR EMBL; AF325262; AAK39430.1; -; mRNA.
DR EMBL; AK034514; BAC28739.1; -; mRNA.
DR EMBL; AK089985; BAC41029.1; -; mRNA.
DR EMBL; BC012208; AAH12208.1; -; mRNA.
DR CCDS; CCDS29856.1; -. [Q91V61-1]
DR CCDS; CCDS50448.1; -. [Q91V61-2]
DR RefSeq; NP_001171483.1; NM_001178012.1. [Q91V61-2]
DR RefSeq; NP_444427.1; NM_053197.4. [Q91V61-1]
DR RefSeq; XP_006527556.1; XM_006527493.2. [Q91V61-1]
DR AlphaFoldDB; Q91V61; -.
DR BioGRID; 220499; 15.
DR IntAct; Q91V61; 8.
DR MINT; Q91V61; -.
DR STRING; 10090.ENSMUSP00000059419; -.
DR TCDB; 2.A.54.1.6; the sideroflexin (sfxn) family (formerly the mitochondrial tricarboxylate carrier (mtc) family.
DR iPTMnet; Q91V61; -.
DR PhosphoSitePlus; Q91V61; -.
DR SwissPalm; Q91V61; -.
DR EPD; Q91V61; -.
DR jPOST; Q91V61; -.
DR MaxQB; Q91V61; -.
DR PaxDb; Q91V61; -.
DR PeptideAtlas; Q91V61; -.
DR PRIDE; Q91V61; -.
DR ProteomicsDB; 256974; -. [Q91V61-1]
DR ProteomicsDB; 256975; -. [Q91V61-2]
DR Antibodypedia; 2332; 145 antibodies from 25 providers.
DR DNASU; 94280; -.
DR Ensembl; ENSMUST00000062213; ENSMUSP00000059419; ENSMUSG00000025212. [Q91V61-1]
DR Ensembl; ENSMUST00000111954; ENSMUSP00000107585; ENSMUSG00000025212. [Q91V61-2]
DR GeneID; 94280; -.
DR KEGG; mmu:94280; -.
DR UCSC; uc012bml.1; mouse. [Q91V61-1]
DR UCSC; uc012bmm.1; mouse. [Q91V61-2]
DR CTD; 81855; -.
DR MGI; MGI:2137679; Sfxn3.
DR VEuPathDB; HostDB:ENSMUSG00000025212; -.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR InParanoid; Q91V61; -.
DR OMA; STPICCA; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q91V61; -.
DR TreeFam; TF313205; -.
DR BioGRID-ORCS; 94280; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sfxn3; mouse.
DR PRO; PR:Q91V61; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91V61; protein.
DR Bgee; ENSMUSG00000025212; Expressed in aortic valve and 233 other tissues.
DR ExpressionAtlas; Q91V61; baseline and differential.
DR Genevisible; Q91V61; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0022889; F:serine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990542; P:mitochondrial transmembrane 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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Amino-acid transport;
KW Direct protein sequencing; Membrane; Mitochondrion; One-carbon metabolism;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Sideroflexin-3"
FT /id="PRO_0000177038"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
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:Q9BWM7"
FT VAR_SEQ 112..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007388"
FT CONFLICT 243
FT /note="P -> A (in Ref. 2; BAC41029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35406 MW; 9B9816A54B23F4EC CRC64;
MGDLPLNINI QEPRWDQSTF LGRARHFFTV TDPRNLLLSG EQLEASRNIV QNYRAGVATP
GLTEDQLWRA KYVYDSAFHP DTGEKVVLIG RMSAQVPMNM TITGCMLTFY RKTPTVVFWQ
WVNQSFNAIV NYSNRSGDAP ITVQQLGTAY VSATTGAVAT ALGLKSLTKH LPPLVGRFVP
FAAVAAANCI NIPLMRQREL QVGIPVTDEA GQRLGHSVTA AKQGIFQVVI SRIGMAIPAM
AIPPVIMNTL EKKDFLKRRP WLGAPLQVGL VGFCLVFATP LCCALFPQRS SIHVTRLEPE
LRAQIQAQNP SIDVVYYNKG L
