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Protein

Flavin carrier protein 1

Gene

FLC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding.1 Publication

GO - Molecular functioni

  • FAD transmembrane transporter activity Source: SGD

GO - Biological processi

  • FAD transmembrane transport Source: GOC
  • FAD transport Source: SGD
  • fungal-type cell wall biogenesis Source: SGD
  • protein folding Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-34110-MONOMER.

Protein family/group databases

TCDBi1.A.4.9.1. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavin carrier protein 1
Alternative name(s):
Bypass of PAM1 protein 1
FAD transporter 1
Heme utilization factor 1
TRP-like ion channel protein FLC1
Gene namesi
Name:FLC1
Synonyms:BOP1, HUF1
Ordered Locus Names:YPL221W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL221W.
SGDiS000006142. FLC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 163142LumenalSequence analysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence analysisAdd
BLAST
Topological domaini185 – 19410CytoplasmicSequence analysis
Transmembranei195 – 21521HelicalSequence analysisAdd
BLAST
Topological domaini216 – 2238LumenalSequence analysis
Transmembranei224 – 24421HelicalSequence analysisAdd
BLAST
Topological domaini245 – 2495CytoplasmicSequence analysis
Transmembranei250 – 27223HelicalSequence analysisAdd
BLAST
Topological domaini273 – 31745LumenalSequence analysisAdd
BLAST
Transmembranei318 – 33821HelicalSequence analysisAdd
BLAST
Topological domaini339 – 37234CytoplasmicSequence analysisAdd
BLAST
Transmembranei373 – 39321HelicalSequence analysisAdd
BLAST
Topological domaini394 – 3974LumenalSequence analysis
Transmembranei398 – 41821HelicalSequence analysisAdd
BLAST
Topological domaini419 – 46143CytoplasmicSequence analysisAdd
BLAST
Transmembranei462 – 48221HelicalSequence analysisAdd
BLAST
Topological domaini483 – 4842LumenalSequence analysis
Transmembranei485 – 50521HelicalSequence analysisAdd
BLAST
Topological domaini506 – 51611CytoplasmicSequence analysisAdd
BLAST
Transmembranei517 – 53721HelicalSequence analysisAdd
BLAST
Topological domaini538 – 55114LumenalSequence analysisAdd
BLAST
Transmembranei552 – 57221HelicalSequence analysisAdd
BLAST
Topological domaini573 – 793221CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 793772Flavin carrier protein 1PRO_0000252267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence analysis
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis
Modified residuei610 – 6101PhosphoserineBy similarity
Modified residuei626 – 6261PhosphothreonineCombined sources
Modified residuei771 – 7711PhosphoserineCombined sources
Modified residuei774 – 7741PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ08967.

PTM databases

iPTMnetiQ08967.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CHS3P294651EBI-36673,EBI-4632
ERG11P106141EBI-36673,EBI-5127
FTR1P400881EBI-36673,EBI-7138
GPA2P108231EBI-36673,EBI-7382
HNM1P198071EBI-36673,EBI-8409
HSP30P256191EBI-36673,EBI-8563
ITR1P306051EBI-36673,EBI-2050956
KEX1P096201EBI-36673,EBI-9653
KEX2P131341EBI-36673,EBI-9658
LSP1Q122301EBI-36673,EBI-34978
MEP3P533901EBI-36673,EBI-10729
MUP1P502761EBI-36673,EBI-11624
OSH7P387551EBI-36673,EBI-12641
PIN2Q120571EBI-36673,EBI-29838
PLM2Q043831EBI-36673,EBI-2079237
PST2Q123351EBI-36673,EBI-14064
SEC7P110751EBI-36673,EBI-16882
SFK1P357351EBI-36673,EBI-26678
SYP1P256231EBI-36673,EBI-21900
TCB3Q036401EBI-36673,EBI-27872
TPO4Q122561EBI-36673,EBI-37213
YOR1P530491EBI-36673,EBI-29324

Protein-protein interaction databases

BioGridi35964. 38 interactions.
DIPiDIP-3965N.
IntActiQ08967. 22 interactions.
MINTiMINT-523610.

Structurei

3D structure databases

ProteinModelPortaliQ08967.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000065299.
HOGENOMiHOG000168830.
InParanoidiQ08967.
OMAiFVAIIRY.
OrthoDBiEOG7TBC9V.

Family and domain databases

InterProiIPR010308. TRP-like_family.
IPR032800. TRP_N.
[Graphical view]
PfamiPF06011. TRP. 1 hit.
PF14558. TRP_N. 1 hit.
[Graphical view]
SMARTiSM01320. TRP_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVLVTLWCL ICTCLVLPVA AKKRTLTASS LVTCMENSQL SANSFDVSFS
60 70 80 90 100
PDDRSLHYDL DMTTQIDSYI YAYVDVYAYG FKIITENFDV CSMGWKQFCP
110 120 130 140 150
VHPGNIQIDS IEYIAQKYVK MIPGIAYQVP DIDAYVRLNI YNNVSENLAC
160 170 180 190 200
IQVFFSNGKT VSQIGVKWVT AVIAGIGLLT SAVLSTFGNS TAASHISANT
210 220 230 240 250
MSLFLYFQSV AVVAMQHVDS VPPIAAAWSE NLAWSMGLIR ITFMQKIFRW
260 270 280 290 300
YVEATGGSAS LYLTATTMSV LTQRGLDYLK NTSVYKRAEN VLYGNSNTLI
310 320 330 340 350
FRGIKRMGYR MKIENTAIVC TGFTFFVLCG YFLAGFIMAC KYSIELCIRC
360 370 380 390 400
GWMRSDRFYQ FRKNWRSVLK GSLLRYIYIG FTQLTILSFW EFTERDSAGV
410 420 430 440 450
IVIACLFIVL SCGLMAWAAY RTIFFASKSV EMYNNPAALL YGDEYVLNKY
460 470 480 490 500
GFFYTMFNAK HYWWNALLTT YILVKALFVG FAQASGKTQA LAIFIIDLAY
510 520 530 540 550
FVAIIRYKPY LDRPTNIVNI FICTVTLVNS FLFMFFSNLF NQKYAVSAIM
560 570 580 590 600
GWVFFIMNAA FSLLLLLMIL AFTTIILFSK NPDSRFKPAK DDRASFQKHA
610 620 630 640 650
IPHEGALNKS VANELMALGN VAKDHTENWE YELKSQEGKS EDNLFGVEYD
660 670 680 690 700
DEKTGTNSEN AESSSKETTR PTFSEKVLRS LSIKRNKSKL GSFKRSAPDK
710 720 730 740 750
ITQQEVSPDR ASSSPNSKSY PGVSHTRQES EANNGLINAY EDEQFSLMEP
760 770 780 790
SILEDAASST QMHAMPARDL SLSSVANAQD VTKKANILDP DYL
Length:793
Mass (Da):89,291
Last modified:November 1, 1996 - v1
Checksum:iFAB678C0038E2604
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73577 Genomic DNA. Translation: CAA97936.1.
BK006949 Genomic DNA. Translation: DAA11215.1.
PIRiS65240.
RefSeqiNP_015103.1. NM_001184035.1.

Genome annotation databases

EnsemblFungiiYPL221W; YPL221W; YPL221W.
GeneIDi855880.
KEGGisce:YPL221W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73577 Genomic DNA. Translation: CAA97936.1.
BK006949 Genomic DNA. Translation: DAA11215.1.
PIRiS65240.
RefSeqiNP_015103.1. NM_001184035.1.

3D structure databases

ProteinModelPortaliQ08967.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35964. 38 interactions.
DIPiDIP-3965N.
IntActiQ08967. 22 interactions.
MINTiMINT-523610.

Protein family/group databases

TCDBi1.A.4.9.1. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

iPTMnetiQ08967.

Proteomic databases

MaxQBiQ08967.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL221W; YPL221W; YPL221W.
GeneIDi855880.
KEGGisce:YPL221W.

Organism-specific databases

EuPathDBiFungiDB:YPL221W.
SGDiS000006142. FLC1.

Phylogenomic databases

GeneTreeiENSGT00530000065299.
HOGENOMiHOG000168830.
InParanoidiQ08967.
OMAiFVAIIRY.
OrthoDBiEOG7TBC9V.

Enzyme and pathway databases

BioCyciYEAST:G3O-34110-MONOMER.

Miscellaneous databases

PROiQ08967.

Family and domain databases

InterProiIPR010308. TRP-like_family.
IPR032800. TRP_N.
[Graphical view]
PfamiPF06011. TRP. 1 hit.
PF14558. TRP_N. 1 hit.
[Graphical view]
SMARTiSM01320. TRP_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  4. "A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum."
    Protchenko O., Rodriguez-Suarez R., Androphy R., Bussey H., Philpott C.C.
    J. Biol. Chem. 281:21445-21457(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-626; SER-771 AND SER-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFLC1_YEAST
AccessioniPrimary (citable) accession number: Q08967
Secondary accession number(s): D6W3E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.