FLC1_YEAST
ID FLC1_YEAST Reviewed; 793 AA.
AC Q08967; D6W3E9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Flavin carrier protein 1;
DE AltName: Full=Bypass of PAM1 protein 1;
DE AltName: Full=FAD transporter 1;
DE AltName: Full=Heme utilization factor 1;
DE AltName: Full=TRP-like ion channel protein FLC1;
DE Flags: Precursor;
GN Name=FLC1; Synonyms=BOP1, HUF1; OrderedLocusNames=YPL221W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771, AND IDENTIFICATION BY
RP 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-626; SER-771 AND SER-774, AND
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 -!- SIMILARITY: Belongs to the transient receptor potential (TRP) ion
CC channel family. {ECO:0000305}.
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DR EMBL; Z73577; CAA97936.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11215.1; -; Genomic_DNA.
DR PIR; S65240; S65240.
DR RefSeq; NP_015103.1; NM_001184035.1.
DR AlphaFoldDB; Q08967; -.
DR BioGRID; 35964; 68.
DR DIP; DIP-3965N; -.
DR IntAct; Q08967; 32.
DR MINT; Q08967; -.
DR STRING; 4932.YPL221W; -.
DR TCDB; 1.A.4.9.1; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; Q08967; -.
DR MaxQB; Q08967; -.
DR PaxDb; Q08967; -.
DR PRIDE; Q08967; -.
DR EnsemblFungi; YPL221W_mRNA; YPL221W; YPL221W.
DR GeneID; 855880; -.
DR KEGG; sce:YPL221W; -.
DR SGD; S000006142; FLC1.
DR VEuPathDB; FungiDB:YPL221W; -.
DR eggNOG; ENOG502QSVZ; Eukaryota.
DR GeneTree; ENSGT00940000176312; -.
DR HOGENOM; CLU_010226_0_0_1; -.
DR InParanoid; Q08967; -.
DR OMA; YTIVKGM; -.
DR BioCyc; YEAST:G3O-34110-MON; -.
DR PRO; PR:Q08967; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08967; protein.
DR GO; GO:0005935; C:cellular bud neck; 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:0000324; C:fungal-type vacuole; HDA:SGD.
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: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; IBA:GO_Central.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..793
FT /note="Flavin carrier protein 1"
FT /id="PRO_0000252267"
FT TOPO_DOM 22..163
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..223
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..317
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..484
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..551
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 649..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53121"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 793 AA; 89291 MW; FAB678C0038E2604 CRC64;
MQVLVTLWCL ICTCLVLPVA AKKRTLTASS LVTCMENSQL SANSFDVSFS PDDRSLHYDL
DMTTQIDSYI YAYVDVYAYG FKIITENFDV CSMGWKQFCP VHPGNIQIDS IEYIAQKYVK
MIPGIAYQVP DIDAYVRLNI YNNVSENLAC IQVFFSNGKT VSQIGVKWVT AVIAGIGLLT
SAVLSTFGNS TAASHISANT MSLFLYFQSV AVVAMQHVDS VPPIAAAWSE NLAWSMGLIR
ITFMQKIFRW YVEATGGSAS LYLTATTMSV LTQRGLDYLK NTSVYKRAEN VLYGNSNTLI
FRGIKRMGYR MKIENTAIVC TGFTFFVLCG YFLAGFIMAC KYSIELCIRC GWMRSDRFYQ
FRKNWRSVLK GSLLRYIYIG FTQLTILSFW EFTERDSAGV IVIACLFIVL SCGLMAWAAY
RTIFFASKSV EMYNNPAALL YGDEYVLNKY GFFYTMFNAK HYWWNALLTT YILVKALFVG
FAQASGKTQA LAIFIIDLAY FVAIIRYKPY LDRPTNIVNI FICTVTLVNS FLFMFFSNLF
NQKYAVSAIM GWVFFIMNAA FSLLLLLMIL AFTTIILFSK NPDSRFKPAK DDRASFQKHA
IPHEGALNKS VANELMALGN VAKDHTENWE YELKSQEGKS EDNLFGVEYD DEKTGTNSEN
AESSSKETTR PTFSEKVLRS LSIKRNKSKL GSFKRSAPDK ITQQEVSPDR ASSSPNSKSY
PGVSHTRQES EANNGLINAY EDEQFSLMEP SILEDAASST QMHAMPARDL SLSSVANAQD
VTKKANILDP DYL
