FLC2_YEAST
ID FLC2_YEAST Reviewed; 783 AA.
AC P39719; D6VPG5; Q05165;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Flavin carrier protein 2;
DE AltName: Full=FAD transporter 2;
DE AltName: Full=TRP-like ion channel FLC2;
DE Flags: Precursor;
GN Name=FLC2; OrderedLocusNames=YAL053W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 111; 312 AND 641-643.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
RC STRAIN=GRF78;
RX PubMed=7642141; DOI=10.1016/0378-1119(95)00289-i;
RA Kratzer S., Schueller H.-J.;
RT "Carbon source-dependent regulation of the acetyl-coenzyme A synthetase-
RT encoding gene ACS1 from Saccharomyces cerevisiae.";
RL Gene 161:75-79(1995).
RN [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16717099; DOI=10.1074/jbc.m512812200;
RA Protchenko O., Rodriguez-Suarez R., Androphy R., Bussey H., Philpott C.C.;
RT "A screen for genes of heme uptake identifies the FLC family required for
RT import of FAD into the endoplasmic reticulum.";
RL J. Biol. Chem. 281:21445-21457(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May be responsible for the transport of FAD into the
CC endoplasmic reticulum lumen, where it is required for oxidative protein
CC folding. {ECO:0000269|PubMed:16717099}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16717099}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16717099}.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transient receptor potential (TRP) ion
CC channel family. {ECO:0000305}.
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DR EMBL; U12980; AAC04980.1; -; Genomic_DNA.
DR EMBL; X76891; CAA54219.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06935.2; -; Genomic_DNA.
DR PIR; S51968; S51968.
DR RefSeq; NP_009348.2; NM_001178196.2.
DR AlphaFoldDB; P39719; -.
DR BioGRID; 31776; 135.
DR DIP; DIP-6708N; -.
DR IntAct; P39719; 29.
DR MINT; P39719; -.
DR STRING; 4932.YAL053W; -.
DR TCDB; 1.A.4.9.3; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; P39719; -.
DR MaxQB; P39719; -.
DR PaxDb; P39719; -.
DR PRIDE; P39719; -.
DR EnsemblFungi; YAL053W_mRNA; YAL053W; YAL053W.
DR GeneID; 851246; -.
DR KEGG; sce:YAL053W; -.
DR SGD; S000000049; FLC2.
DR VEuPathDB; FungiDB:YAL053W; -.
DR eggNOG; ENOG502QSVZ; Eukaryota.
DR GeneTree; ENSGT00940000176312; -.
DR HOGENOM; CLU_010226_0_1_1; -.
DR InParanoid; P39719; -.
DR OMA; FLYVQFK; -.
DR BioCyc; YEAST:G3O-28858-MON; -.
DR PRO; PR:P39719; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39719; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0015230; F:FAD transmembrane transporter activity; IMP:SGD.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:SGD.
DR GO; GO:0071476; P:cellular hypotonic response; IMP:SGD.
DR GO; GO:0015883; P:FAD transport; IMP:SGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:SGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR InterPro; IPR010308; TRP_C.
DR InterPro; IPR040241; TRP_Flc/Pkd2-like.
DR InterPro; IPR032800; TRP_N.
DR PANTHER; PTHR31145; PTHR31145; 1.
DR Pfam; PF06011; TRP; 1.
DR Pfam; PF14558; TRP_N; 1.
DR SMART; SM01320; TRP_N; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..783
FT /note="Flavin carrier protein 2"
FT /id="PRO_0000202424"
FT TOPO_DOM 23..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..430
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..521
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..581
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 681..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 111
FT /note="C -> S (in Ref. 1; AAC04980)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="N -> D (in Ref. 1; AAC04980)"
FT /evidence="ECO:0000305"
FT CONFLICT 641..643
FT /note="NDS -> IDP (in Ref. 1; AAC04980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 87469 MW; F5944205A7098B89 CRC64;
MIFLNTFARC LLTCFVLCSG TARSSDTNDT TPASAKHLQT TSLLTCMDNS QLTASFFDVK
FYPDNNTVIF DIDATTTLNG NVTVKAELLT YGLKVLDKTF DLCSLGQVSL CPLSAGRIDV
MSTQVIESSI TKQFPGIAYT IPDLDAQVRV VAYAQNDTEF ETPLACVQAI LSNGKTVQTK
YAAWPIAAIS GVGVLTSGFV SVIGYSATAA HIASNSISLF IYFQNLAITA MMGVSRVPPI
AAAWTQNFQW SMGIINTNFM QKIFDWYVQA TNGVSNVVVA NKDVLSISVQ KRAISMASSS
DYNFDTILDD SNLYTTSEKD PSNYSAKILV LRGIERVAYL ANIELSNFFL TGIVFFLFFL
FVVVVSLIFF KALLEVLTRA RILKETSNFF QYRKNWGSII KGTLFRLSII AFPQVSLLAI
WEFTQVNSPA IVVDAVVILL IITGLLVYGT IRVFIKGRES LRLYKNPAYL LYSDTYFLNK
FGFLYVQFKA DKFWWLLPLL SYAFLRSLFV AVLQNQGKAQ AMIIFVIELA YFVCLCWIRP
YLDKRTNVFN IAIHLVNLIN AFFFLFFSNL FKQPAVVSSV MAVILFVLNA VFALFLLLFT
IVTCTLALLH RNPDVRYQPM KDDRVSFIPK IQNDFDGKNK NDSELFELRK AVMDTNENEE
EKMFRDDTFG KNLNANTNTA RLFDDETSSS SFKQNSSPFD ASEVTEQPVQ PTSAVMGTGG
SFLSPQYQRA SSASRTNLAP NNTSTSSLMK PESSLYLGNS NKSYSHFNNN GSNENARNNN
PYL
