YEL1_YEAST
ID YEL1_YEAST Reviewed; 687 AA.
AC P34225; D6VPT9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Guanine-nucleotide exchange factor YEL1;
DE AltName: Full=EFA6-like protein 1;
GN Name=YEL1; OrderedLocusNames=YBL060W; ORFNames=YBL0507, YBL0517;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17786213; DOI=10.1371/journal.pone.0000842;
RA Gillingham A.K., Munro S.;
RT "Identification of a guanine nucleotide exchange factor for Arf3, the yeast
RT orthologue of mammalian Arf6.";
RL PLoS ONE 2:E842-E842(2007).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18397879; DOI=10.1074/jbc.m802550200;
RA Tsai P.-C., Lee S.-W., Liu Y.-W., Chu C.-W., Chen K.-Y., Ho J.-C.,
RA Lee F.-J.;
RT "Afi1p functions as an Arf3p polarization-specific docking factor for
RT development of polarity.";
RL J. Biol. Chem. 283:16915-16927(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION BY
RP 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18208507; DOI=10.1111/j.1600-0854.2008.00708.x;
RA Smaczynska-de Rooij I.I., Costa R., Ayscough K.R.;
RT "Yeast Arf3p modulates plasma membrane PtdIns(4,5)P2 levels to facilitate
RT endocytosis.";
RL Traffic 9:559-573(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290; SER-293 AND SER-299, 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: 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:0000269|PubMed:17786213,
CC ECO:0000269|PubMed:18208507, ECO:0000269|PubMed:18397879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein. Bud neck. Bud tip. Note=Localizes at the cell membrane only at
CC the bud neck and bud tip and this localization is ARF3-dependent.
CC -!- SIMILARITY: Belongs to the YEL1 family. {ECO:0000305}.
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DR EMBL; Z23261; CAA80787.1; -; Genomic_DNA.
DR EMBL; Z35821; CAA84880.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07059.1; -; Genomic_DNA.
DR PIR; S39828; S39828.
DR RefSeq; NP_009493.1; NM_001178300.1.
DR AlphaFoldDB; P34225; -.
DR SMR; P34225; -.
DR BioGRID; 32638; 57.
DR IntAct; P34225; 2.
DR MINT; P34225; -.
DR STRING; 4932.YBL060W; -.
DR iPTMnet; P34225; -.
DR MaxQB; P34225; -.
DR PaxDb; P34225; -.
DR PRIDE; P34225; -.
DR EnsemblFungi; YBL060W_mRNA; YBL060W; YBL060W.
DR GeneID; 852219; -.
DR KEGG; sce:YBL060W; -.
DR SGD; S000000156; YEL1.
DR VEuPathDB; FungiDB:YBL060W; -.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_017717_0_0_1; -.
DR OMA; CHIVLFS; -.
DR BioCyc; YEAST:G3O-28958-MON; -.
DR PRO; PR:P34225; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P34225; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
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 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..687
FT /note="Guanine-nucleotide exchange factor YEL1"
FT /id="PRO_0000120222"
FT DOMAIN 61..266
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:0007744|PubMed:19779198"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
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
