ID   YEL1_YEAS7              Reviewed;         687 AA.
AC   A6ZKN8;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Guanine-nucleotide exchange factor YEL1;
DE   AltName: Full=EFA6-like protein 1;
GN   Name=YEL1; ORFNames=SCY_0158;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000011; EDN64557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZKN8; -.
DR   SMR; A6ZKN8; -.
DR   EnsemblFungi; EDN64557; EDN64557; SCY_0158.
DR   HOGENOM; CLU_017717_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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_0000404228"
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