SFXN3_HUMAN
ID SFXN3_HUMAN Reviewed; 321 AA.
AC Q9BWM7; Q8NCJ0; Q9NTP4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Sideroflexin-3 {ECO:0000303|PubMed:30442778};
GN Name=SFXN3 {ECO:0000303|PubMed:30442778, ECO:0000312|HGNC:HGNC:16087};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 SUBCELLULAR LOCATION.
RA Rabilloud T.;
RL Submitted (FEB-2002) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP ACETYLATION AT MET-1.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=30442778; DOI=10.1126/science.aat9528;
RA Kory N., Wyant G.A., Prakash G., Uit de Bos J., Bottanelli F., Pacold M.E.,
RA Chan S.H., Lewis C.A., Wang T., Keys H.R., Guo Y.E., Sabatini D.M.;
RT "SFXN1 is a mitochondrial serine transporter required for one-carbon
RT metabolism.";
RL Science 362:0-0(2018).
CC -!- FUNCTION: Mitochondrial serine transporter that mediates transport of
CC serine into mitochondria, an important step of the one-carbon
CC metabolism pathway (PubMed:30442778). Mitochondrial serine is converted
CC to glycine and formate, which then exits to the cytosol where it is
CC used to generate the charged folates that serve as one-carbon donors
CC (PubMed:30442778). {ECO:0000269|PubMed:30442778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000305|PubMed:30442778};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:30442778, ECO:0000269|Ref.4}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00124.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11151.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK074707; BAC11151.1; ALT_INIT; mRNA.
DR EMBL; AL133215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000124; AAH00124.2; ALT_INIT; mRNA.
DR CCDS; CCDS7508.2; -.
DR RefSeq; NP_112233.2; NM_030971.3.
DR AlphaFoldDB; Q9BWM7; -.
DR BioGRID; 123605; 190.
DR IntAct; Q9BWM7; 45.
DR MINT; Q9BWM7; -.
DR STRING; 9606.ENSP00000224807; -.
DR GlyGen; Q9BWM7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWM7; -.
DR PhosphoSitePlus; Q9BWM7; -.
DR SwissPalm; Q9BWM7; -.
DR BioMuta; SFXN3; -.
DR DMDM; 308153497; -.
DR EPD; Q9BWM7; -.
DR jPOST; Q9BWM7; -.
DR MassIVE; Q9BWM7; -.
DR PaxDb; Q9BWM7; -.
DR PeptideAtlas; Q9BWM7; -.
DR PRIDE; Q9BWM7; -.
DR ProteomicsDB; 79293; -.
DR Antibodypedia; 2332; 145 antibodies from 25 providers.
DR DNASU; 81855; -.
DR Ensembl; ENST00000393459.5; ENSP00000377103.1; ENSG00000107819.14.
DR GeneID; 81855; -.
DR KEGG; hsa:81855; -.
DR MANE-Select; ENST00000393459.6; ENSP00000377103.1; NM_030971.6; NP_112233.3.
DR UCSC; uc057vma.1; human.
DR CTD; 81855; -.
DR DisGeNET; 81855; -.
DR GeneCards; SFXN3; -.
DR HGNC; HGNC:16087; SFXN3.
DR HPA; ENSG00000107819; Low tissue specificity.
DR MIM; 615571; gene.
DR neXtProt; NX_Q9BWM7; -.
DR OpenTargets; ENSG00000107819; -.
DR PharmGKB; PA38092; -.
DR VEuPathDB; HostDB:ENSG00000107819; -.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR InParanoid; Q9BWM7; -.
DR OMA; STPICCA; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q9BWM7; -.
DR TreeFam; TF313205; -.
DR PathwayCommons; Q9BWM7; -.
DR SignaLink; Q9BWM7; -.
DR BioGRID-ORCS; 81855; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; SFXN3; human.
DR GenomeRNAi; 81855; -.
DR Pharos; Q9BWM7; Tbio.
DR PRO; PR:Q9BWM7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BWM7; protein.
DR Bgee; ENSG00000107819; Expressed in cerebellar hemisphere and 206 other tissues.
DR ExpressionAtlas; Q9BWM7; baseline and differential.
DR Genevisible; Q9BWM7; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0022889; F:serine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IDA:UniProtKB.
DR GO; GO:0140300; P:serine import into mitochondrion; IDA: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; Membrane; Mitochondrion;
KW One-carbon metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Sideroflexin-3"
FT /id="PRO_0000177037"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
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:0000269|PubMed:25732826"
SQ SEQUENCE 321 AA; 35503 MW; 54718C600B3D34BD CRC64;
MGELPLDINI QEPRWDQSTF LGRARHFFTV TDPRNLLLSG AQLEASRNIV QNYRAGVVTP
GITEDQLWRA KYVYDSAFHP DTGEKVVLIG RMSAQVPMNM TITGCMLTFY RKTPTVVFWQ
WVNQSFNAIV NYSNRSGDTP ITVRQLGTAY VSATTGAVAT ALGLKSLTKH LPPLVGRFVP
FAAVAAANCI NIPLMRQREL QVGIPVADEA GQRLGYSVTA AKQGIFQVVI SRICMAIPAM
AIPPLIMDTL EKKDFLKRRP WLGAPLQVGL VGFCLVFATP LCCALFPQKS SIHISNLEPE
LRAQIHEQNP SVEVVYYNKG L
