FLC3_YEAST
ID FLC3_YEAST Reviewed; 802 AA.
AC P53121; D6VU10;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative flavin carrier protein 3;
DE AltName: Full=FAD transporter 3;
DE AltName: Full=TRP-like ion channel FLC3;
DE Flags: Precursor;
GN Name=FLC3; OrderedLocusNames=YGL139W; ORFNames=G2812;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-749.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 616-802.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840506;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<887::aid-yea971>3.0.co;2-d;
RA Escribano V., Eraso P., Portillo F., Mazon M.J.;
RT "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae
RT chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-
RT dependent enzyme and six new open reading frames.";
RL Yeast 12:887-892(1996).
RN [5]
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616; SER-779 AND SER-782, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616; SER-635; SER-779 AND
RP SER-782, AND 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:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16717099}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16717099}.
CC -!- SIMILARITY: Belongs to the transient receptor potential (TRP) ion
CC channel family. {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; X99960; CAA68223.1; -; Genomic_DNA.
DR EMBL; Z72661; CAA96851.1; -; Genomic_DNA.
DR EMBL; Z72660; CAA96850.1; -; Genomic_DNA.
DR EMBL; X92670; CAA63357.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07971.1; -; Genomic_DNA.
DR PIR; S64153; S64153.
DR RefSeq; NP_011376.3; NM_001181004.3.
DR AlphaFoldDB; P53121; -.
DR BioGRID; 33113; 43.
DR DIP; DIP-5496N; -.
DR STRING; 4932.YGL139W; -.
DR iPTMnet; P53121; -.
DR MaxQB; P53121; -.
DR PaxDb; P53121; -.
DR PRIDE; P53121; -.
DR EnsemblFungi; YGL139W_mRNA; YGL139W; YGL139W.
DR GeneID; 852738; -.
DR KEGG; sce:YGL139W; -.
DR SGD; S000003107; FLC3.
DR VEuPathDB; FungiDB:YGL139W; -.
DR eggNOG; ENOG502QSVZ; Eukaryota.
DR GeneTree; ENSGT00940000176312; -.
DR HOGENOM; CLU_010226_0_0_1; -.
DR InParanoid; P53121; -.
DR OMA; SIMGWVF; -.
DR BioCyc; YEAST:G3O-30634-MON; -.
DR PRO; PR:P53121; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53121; protein.
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:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015230; F:FAD transmembrane transporter activity; ISS:SGD.
DR GO; GO:0015883; P:FAD transport; ISS:SGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:SGD.
DR GO; GO:0055085; P:transmembrane transport; ISS: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; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..802
FT /note="Putative flavin carrier protein 3"
FT /id="PRO_0000202738"
FT TOPO_DOM 29..169
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..229
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..323
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..405
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..495
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..557
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 629..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 802 AA; 90761 MW; 7BA13714AD912295 CRC64;
MRFLQVYKSS ALIGLIILLA SKVNLAEAKR KLVATSLVTC MENSQLSANS FDVVFNPDDR
SLHYDLDMST QIDSYIFADI DVYAYGFKII TKNVDLCSIN WKQFCPVHPG NIQIDSIEYI
SSEYVNEIPG IAYQVPDIDA YARVKITNNV SEYLACIQIY FSNGKTVSQI GVKWATAVVA
GIGLLLSAIL STFGNSTAAS HISANTMSLF LYFQSVVVVA MQHVHRVPPI AAAWAENLVW
SMGLIRISFM QRIFRWYVQS TGGTPSLYLT STSMSVLAQR SWQYLMELPL IKRATNVLYG
NANTLIFRGI KRLGYKMGIE NTSIVCTGFT FFVLCGYVLA GFIIVFKCCV ELATRLGWIQ
KARFWEFRKQ WRMILKGALL RYIYIGFVQL TILSFWEFTE RDSPAVIVIA CLFILLSCGL
MLWAAWRTVF FARRSVALYN NPAALLYGDE YVLHKYGFFY TMFNANHYWW NIVLLSYIFV
KSLLVGFAQA SGQTQVLFMF ILDLFYFVAI IYYKPYLDRP TNIMNILIAT VTVVNSFLFM
FFSDLFNQSY KVAAIMGWIF FIMNAAFSFI LLMMILAFAG MMLFSKNPDL RFKPAKDDRT
SFQRNTMKPE GTVNRSVANE LLALGNVAKD HDDNSDYESN DTGVNDELKQ AQDETTPTTV
TSSDDNKPTF SEKILSKFSR PKNENASTDA LRVEAPKQQT FPHNLTNLSR ENLSTLGSKP
YPGHTRSQSD AHNGLINSFE EEDTSSNTDP FHDSTEGDLL DTSSSDGGFR SQNYVRDDSI
NSLGNNKQPL RKPPGFFDEG FM
