SFXN1_MOUSE
ID SFXN1_MOUSE Reviewed; 322 AA.
AC Q99JR1; Q3UB44; Q9CZG4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Sideroflexin-1 {ECO:0000303|PubMed:11274051};
GN Name=Sfxn1 {ECO:0000303|PubMed:11274051, ECO:0000312|MGI:MGI:2137677};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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 STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
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].
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 16-24; 73-86; 179-197; 203-214 AND 224-233, AND
RP 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, Liver, Lung, Pancreas,
RC Spleen, 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: 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:0000305|PubMed:11274051}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in kidney
CC and liver. {ECO:0000269|PubMed:11274051}.
CC -!- DEVELOPMENTAL STAGE: Very high levels in the liver during the period of
CC embryonic hepatic hemopoiesis. {ECO:0000269|PubMed:11274051}.
CC -!- DISRUPTION PHENOTYPE: Defects in Sfxn1 are the cause of a transitory
CC hypochromic, microcytic anemia characterized by a large number of
CC siderocytes containing non-heme iron granules (PubMed:11274051). The
CC anemia begins at 12 dpc, is most intense at 15 dpc and is still severe
CC at birth, but disappears by 2 weeks of age (PubMed:11274051). Mutant
CC adults are no longer anemic, but they have an impaired response to
CC hemopoietic stress (PubMed:11274051). Most homozygotes also have flexed
CC tails and a belly spot (PubMed:11274051).
CC {ECO:0000269|PubMed:11274051}.
CC -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK012650; Type=Frameshift; Evidence={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; AF325260; AAK39428.1; -; mRNA.
DR EMBL; AK012650; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK151110; BAE30120.1; -; mRNA.
DR EMBL; BC005743; AAH05743.1; -; mRNA.
DR CCDS; CCDS26525.1; -.
DR RefSeq; NP_081600.1; NM_027324.5.
DR RefSeq; XP_006516912.2; XM_006516849.3.
DR RefSeq; XP_006516913.1; XM_006516850.3.
DR AlphaFoldDB; Q99JR1; -.
DR BioGRID; 199565; 16.
DR IntAct; Q99JR1; 12.
DR MINT; Q99JR1; -.
DR STRING; 10090.ENSMUSP00000021930; -.
DR iPTMnet; Q99JR1; -.
DR PhosphoSitePlus; Q99JR1; -.
DR SwissPalm; Q99JR1; -.
DR EPD; Q99JR1; -.
DR jPOST; Q99JR1; -.
DR MaxQB; Q99JR1; -.
DR PaxDb; Q99JR1; -.
DR PeptideAtlas; Q99JR1; -.
DR PRIDE; Q99JR1; -.
DR ProteomicsDB; 257212; -.
DR Antibodypedia; 17087; 172 antibodies from 26 providers.
DR DNASU; 14057; -.
DR Ensembl; ENSMUST00000021930; ENSMUSP00000021930; ENSMUSG00000021474.
DR GeneID; 14057; -.
DR KEGG; mmu:14057; -.
DR UCSC; uc007qoa.2; mouse.
DR CTD; 94081; -.
DR MGI; MGI:2137677; Sfxn1.
DR VEuPathDB; HostDB:ENSMUSG00000021474; -.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR HOGENOM; CLU_039425_1_0_1; -.
DR InParanoid; Q99JR1; -.
DR OMA; GRVRHCA; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q99JR1; -.
DR TreeFam; TF313205; -.
DR BioGRID-ORCS; 14057; 6 hits in 70 CRISPR screens.
DR ChiTaRS; Sfxn1; mouse.
DR PRO; PR:Q99JR1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99JR1; protein.
DR Bgee; ENSMUSG00000021474; Expressed in epididymal fat pad and 251 other tissues.
DR Genevisible; Q99JR1; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
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:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0006826; P:iron ion transport; IMP:MGI.
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 1: Evidence at protein level;
KW Acetylation; Amino-acid transport; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; One-carbon metabolism;
KW Reference proteome; 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_0000177033"
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; 35649 MW; E3B055CB03CEDFA7 CRC64;
MSGEVPPNIN IKEPRWDQST FIGRASHFFT VTDPRNILLT NEQLENARKV VHDYRQGIVP
AGLTENELWR AKYAYDSAFH PDTGEKMTLI GRMSAQVPMN MTITGCMMTF YRTTPAVLFW
QWINQSFNAV VNYTNRSGDA PLTVNELGTA YVSATTGAVA TALGLNALTK RVSPLIGRFV
PFAAVAAANC INIPLMRQRE LKVGIPVTDE NGTRLGESTN AAKQAITQVV ISRILMAAPG
MAIPPFIMNT LEKKAFLKRF PWMSAPIQVT LVGFCLVFAT PLCCALFPQK SSMSVTSLED
ELQASIQRTH PEIRRVYFNK GL
