SFXN3_RAT
ID SFXN3_RAT Reviewed; 321 AA.
AC Q9JHY2; G3V804;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sideroflexin-3;
GN Name=Sfxn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Mashima H., Kojima I.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
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DR EMBL; AF276997; AAF78249.1; -; mRNA.
DR EMBL; AC121209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473986; EDL94301.1; -; Genomic_DNA.
DR RefSeq; NP_075237.1; NM_022948.1.
DR RefSeq; XP_006231625.1; XM_006231563.3.
DR RefSeq; XP_006231627.1; XM_006231565.3.
DR RefSeq; XP_006231628.1; XM_006231566.2.
DR RefSeq; XP_008758673.1; XM_008760451.2.
DR AlphaFoldDB; Q9JHY2; -.
DR BioGRID; 249235; 2.
DR IntAct; Q9JHY2; 2.
DR MINT; Q9JHY2; -.
DR STRING; 10116.ENSRNOP00000021171; -.
DR CarbonylDB; Q9JHY2; -.
DR iPTMnet; Q9JHY2; -.
DR PhosphoSitePlus; Q9JHY2; -.
DR SwissPalm; Q9JHY2; -.
DR jPOST; Q9JHY2; -.
DR PaxDb; Q9JHY2; -.
DR PRIDE; Q9JHY2; -.
DR Ensembl; ENSRNOT00000021171.5; ENSRNOP00000021171.4; ENSRNOG00000015442.7.
DR GeneID; 65042; -.
DR KEGG; rno:65042; -.
DR UCSC; RGD:620716; rat.
DR CTD; 81855; -.
DR RGD; 620716; Sfxn3.
DR VEuPathDB; HostDB:ENSRNOG00000015442; -.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR HOGENOM; CLU_039425_1_0_1; -.
DR InParanoid; Q9JHY2; -.
DR OMA; RMSMFLP; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q9JHY2; -.
DR TreeFam; TF313205; -.
DR PRO; PR:Q9JHY2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000015442; Expressed in stomach and 20 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; TAS:RGD.
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:0005371; F:tricarboxylate secondary active transmembrane transporter activity; TAS:RGD.
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 2: Evidence at transcript 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_0000177040"
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 CONFLICT 116
FT /note="M -> V (in Ref. 1; AAF78249)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="K -> N (in Ref. 1; AAF78249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35465 MW; 8BD8D4DD9B73DA8F CRC64;
MGDLPLNINI QEPRWDQSTF LGRARHFFTV TDPRNLLLSG KQLEASRNIV QNYRAGVVTP
GLTEDQLWRA KYVYDSAFHP DTGEKVVLIG RMSAQVPMNM TITGCMLTFY RKTPTMVFWQ
WVNQSFNAIV NYSNRSGDAP ITVQQLGTAY VSATTGAVAT ALGLKSLTKH LPPLVGRFVP
FAAVAAANCI NIPLMRQREL QVGIPVTDEA GQRLGHSVTA AKQGIFQVVV SRIGMAIPAM
AIPPVIMNTL EKKDFLKRRP WLGAPLQVGL VGFCLVFATP LCCALFPQRS SIHVTRLEPE
LRAQIQAQKP SIDVVYYNKG L
