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FSF1_YEAST
ID   FSF1_YEAST              Reviewed;         327 AA.
AC   Q12029; D6W2X1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Sideroflexin FSF1 {ECO:0000305};
DE   AltName: Full=Fungal sideroflexin-1 {ECO:0000303|PubMed:17240176};
GN   Name=FSF1 {ECO:0000303|PubMed:17240176, ECO:0000312|SGD:S000005797};
GN   OrderedLocusNames=YOR271C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896271;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA   Cheret G., Bernardi A., Sor F.J.;
RT   "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT   Saccharomyces cerevisiae.";
RL   Yeast 12:1059-1064(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [7]
RP   GENE NAME.
RX   PubMed=17240176; DOI=10.1016/j.fgb.2006.12.004;
RA   Miotto G., Tessaro S., Rotta G.A., Bonatto D.;
RT   "In silico analyses of Fsf1 sequences, a new group of fungal proteins
RT   orthologous to the metazoan sideroblastic anemia-related sideroflexin
RT   family.";
RL   Fungal Genet. Biol. 44:740-753(2007).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [9]
RP   FUNCTION, 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 amino-acid transporter that mediates transport
CC       of serine into mitochondria. {ECO:0000269|PubMed:30442778}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:30442778}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- MISCELLANEOUS: Present with 9290 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
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DR   EMBL; X89633; CAA61777.1; -; Genomic_DNA.
DR   EMBL; Z75179; CAA99495.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11037.1; -; Genomic_DNA.
DR   PIR; S67168; S67168.
DR   RefSeq; NP_014914.1; NM_001183690.1.
DR   AlphaFoldDB; Q12029; -.
DR   BioGRID; 34660; 70.
DR   DIP; DIP-3828N; -.
DR   IntAct; Q12029; 21.
DR   STRING; 4932.YOR271C; -.
DR   TCDB; 2.A.54.1.4; the sideroflexin (sfxn) family (formerly the mitochondrial tricarboxylate carrier (mtc) family.
DR   iPTMnet; Q12029; -.
DR   MaxQB; Q12029; -.
DR   PaxDb; Q12029; -.
DR   PRIDE; Q12029; -.
DR   EnsemblFungi; YOR271C_mRNA; YOR271C; YOR271C.
DR   GeneID; 854445; -.
DR   KEGG; sce:YOR271C; -.
DR   SGD; S000005797; FSF1.
DR   VEuPathDB; FungiDB:YOR271C; -.
DR   eggNOG; KOG3767; Eukaryota.
DR   GeneTree; ENSGT01030000234641; -.
DR   HOGENOM; CLU_039425_0_0_1; -.
DR   InParanoid; Q12029; -.
DR   OMA; GRVRHCA; -.
DR   BioCyc; YEAST:G3O-33761-MON; -.
DR   PRO; PR:Q12029; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12029; protein.
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   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..327
FT                   /note="Sideroflexin FSF1"
FT                   /id="PRO_0000237642"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   327 AA;  35414 MW;  FD175626E63B8619 CRC64;
     MASSVPGPID LPESRYDLST YWGRIRHCAE ISDPTMLLTT EKDLAHAREI ISAYRHGELK
     ETTPEFWRAK KQLDSTVHPD TGKTVLLPFR MSSNVLSNLV VTVGMLTPGL GTAGTVFWQW
     ANQSLNVAVN SANANKSHPM STSQLLTNYA AAVTASCGVA LGLNNLVPRL KNISPHSKLI
     LGRLVPFAAV VSAGIVNVFL MRGNEIRKGI SVFDSNGDEV GKSKKAAFMA VGETALSRVI
     NATPTMVIPP LILVRLQRGV LKGKSLGVQT LANLGLISVT MFSALPFALG IFPQRQAIHL
     NKLEPELHGK KDKDGKPIEK VYFNRGI
 
 
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