YEL1_YEAS8
ID YEL1_YEAS8 Reviewed; 687 AA.
AC C8Z3N7;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Guanine-nucleotide exchange factor YEL1;
DE AltName: Full=EFA6-like protein 1;
GN Name=YEL1; ORFNames=EC1118_1B15_0573g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF3 required for
CC localization of ARF3 to the bud neck and tip and involved in actin
CC patch polarization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Bud neck
CC {ECO:0000250}. Bud tip {ECO:0000250}. Note=Localizes at the cell
CC membrane only at the bud neck and bud tip and this localization is
CC ARF3-dependent. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the YEL1 family. {ECO:0000305}.
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DR EMBL; FN393060; CAY77725.1; -; Genomic_DNA.
DR AlphaFoldDB; C8Z3N7; -.
DR SMR; C8Z3N7; -.
DR EnsemblFungi; CAY77725; CAY77725; EC1118_1B15_0573g.
DR HOGENOM; CLU_017717_0_0_1; -.
DR Proteomes; UP000000286; Chromosome II, Scaffold EC1118_1B15.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0051641; P:cellular localization; IEA:UniProt.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein.
FT CHAIN 1..687
FT /note="Guanine-nucleotide exchange factor YEL1"
FT /id="PRO_0000404229"
FT DOMAIN 57..264
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 412..551
FT /note="PH"
FT REGION 14..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P34225"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34225"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34225"
SQ SEQUENCE 687 AA; 78768 MW; FBE491AABC5988E0 CRC64;
MCASLNEVKK NDTYGVSQKG YNDNFSESEG VLHGSKSMPT SMKNMLQSPT MVNMCDILQN
KEAANDEKPV IPTTDTATAG TGTEDISSTQ SEETDQNSHL IASEILEGTF KDVSYKEYAN
FLGNDNNNQV LTEFVKLLSP LPSSLLETLF NLSKSIYFIA EAQNIDRILE CLSIEWIACH
PNTHWKSGYK SCHIVLFSLL ILNSDLHNNF QVDHKKIKFS MVAFINNTLR ALREENEYEE
LKIYSREHLI IEELSEYYKT LNETPLPLCT ESRTSINISD NQSSLKRFST LGSREFSTSN
LRSVNSNSTT LYSRDGQVSV REMSAKSNKN FHNNHPMDAL YLKESFDDGL ITENGSSWFM
DDLILISKKS LPRKYSKRDK DQVAAPKMTS KRNKSFFGWL KPSKTTTLIE HTSRRTSLSY
LNKDSEWERV KIQVKEGRIF IFKIKPDVKD IIQSSETDSA TIDYFKDISS SYFAYSLLEA
EAHVVQDNII IGSGAMKSNV CNKNTKRKSG NFTVSFPENI NGPKLVLEFQ TRSVEEAHKF
MDCINFWAGR ISPVPLTQFE AVSNAEYGWS DKILTEHASL NLKNIVVSEW KPLLGLELLY
EDAKDVEMVE LKERLKELMN FTRQLGIWID KHNEIKDKLV EIWSFDDNYF EAVMNNWNSR
YLYMNNQYKK RLSYLKALQK AMGSVQF