GEA2_YEAST
ID GEA2_YEAST Reviewed; 1459 AA.
AC P39993; D3DLM6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ARF guanine-nucleotide exchange factor 2;
GN Name=GEA2; OrderedLocusNames=YEL022W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 CHARACTERIZATION.
RX PubMed=8945477; DOI=10.1038/384479a0;
RA Peyroche A., Paris S., Jackson C.L.;
RT "Nucleotide exchange on ARF mediated by yeast Gea1 protein.";
RL Nature 384:479-481(1996).
RN [4]
RP INTERACTION WITH GMH1, AND SUBCELLULAR LOCATION.
RX PubMed=12808035; DOI=10.1091/mbc.e02-10-0693;
RA Chantalat S., Courbeyrette R., Senic-Matuglia F., Jackson C.L., Goud B.,
RA Peyroche A.;
RT "A novel Golgi membrane protein is a partner of the ARF exchange factors
RT Gea1p and Gea2p.";
RL Mol. Biol. Cell 14:2357-2371(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-284, AND
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 SER-284, AND IDENTIFICATION BY
RP 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).
RN [9]
RP FUNCTION.
RX PubMed=25190516; DOI=10.15252/embj.201489039;
RA Ackema K.B., Hench J., Boeckler S., Wang S.C., Sauder U., Mergentaler H.,
RA Westermann B., Bard F., Frank S., Spang A.;
RT "The small GTPase Arf1 modulates mitochondrial morphology and function.";
RL EMBO J. 33:2659-2675(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 558-766 IN COMPLEX WITH GDP AND
RP SEC7.
RX PubMed=11888276; DOI=10.1021/bi012123h;
RA Renault L., Christova P., Guibert B., Pasqualato S., Cherfils J.;
RT "Mechanism of domain closure of Sec7 domains and role in BFA sensitivity.";
RL Biochemistry 41:3605-3612(2002).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in maintaining mitochondrial morphology
CC (PubMed:25190516). {ECO:0000269|PubMed:25190516}.
CC -!- SUBUNIT: Interacts with GMH1. {ECO:0000269|PubMed:11888276,
CC ECO:0000269|PubMed:12808035}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12808035}.
CC Membrane {ECO:0000269|PubMed:12808035}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12808035}. Note=Soluble and partially membrane-
CC bound. {ECO:0000269|PubMed:12808035}.
CC -!- MISCELLANEOUS: Present with 7700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18530; AAB64499.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07630.1; -; Genomic_DNA.
DR PIR; S50437; S50437.
DR RefSeq; NP_010892.1; NM_001178837.1.
DR PDB; 1KU1; X-ray; 1.93 A; A/B=558-766.
DR PDBsum; 1KU1; -.
DR AlphaFoldDB; P39993; -.
DR SMR; P39993; -.
DR BioGRID; 36707; 55.
DR DIP; DIP-6816N; -.
DR IntAct; P39993; 16.
DR STRING; 4932.YEL022W; -.
DR CarbonylDB; P39993; -.
DR iPTMnet; P39993; -.
DR MaxQB; P39993; -.
DR PaxDb; P39993; -.
DR PRIDE; P39993; -.
DR EnsemblFungi; YEL022W_mRNA; YEL022W; YEL022W.
DR GeneID; 856691; -.
DR KEGG; sce:YEL022W; -.
DR SGD; S000000748; GEA2.
DR VEuPathDB; FungiDB:YEL022W; -.
DR eggNOG; KOG0928; Eukaryota.
DR GeneTree; ENSGT00940000176690; -.
DR HOGENOM; CLU_001204_0_1_1; -.
DR InParanoid; P39993; -.
DR OMA; WQHQWHT; -.
DR BioCyc; YEAST:G3O-30146-MON; -.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR EvolutionaryTrace; P39993; -.
DR PRO; PR:P39993; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39993; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IGI:SGD.
DR GO; GO:0033363; P:secretory granule organization; IMP:SGD.
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 InterPro; IPR032691; Sec7_N.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1459
FT /note="ARF guanine-nucleotide exchange factor 2"
FT /id="PRO_0000120213"
FT DOMAIN 570..714
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 1412..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 558..572
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:1KU1"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 592..601
FT /evidence="ECO:0007829|PDB:1KU1"
FT TURN 602..605
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 621..629
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 638..645
FT /evidence="ECO:0007829|PDB:1KU1"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 655..671
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 695..712
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 723..729
FT /evidence="ECO:0007829|PDB:1KU1"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:1KU1"
FT HELIX 741..753
FT /evidence="ECO:0007829|PDB:1KU1"
SQ SEQUENCE 1459 AA; 165668 MW; 99DB9FDD34F863FA CRC64;
MSDREFVTVD PVTIIIKECI NLSTAMRKYS KFTSQSGVAA LLGGGSEIFS NQDDYLAHTF
NNLNTNKHND PFLSGFIQLR LMLNKLKNLD NIDSLTILQP FLLIVSTSSI SGYITSLALD
SLQKFFTLNI INESSQNYIG AHRATVNALT HCRFEGSQQL SDDSVLLKVV FLLRSIVDSP
YGDLLSNSII YDVLQTILSL ACNNRRSEVL RNAAQSTMIA VTVKIFSKLK TIEPVNVNQI
YINDESYTND VLKADTIGTN VESKEEGSQE DPIGMKVNNE EAISEDDGIE EEHIHSEKST
NGAEQLDIVQ KTTRSNSRIQ AYADDNYGLP VVRQYLNLLL SLIAPENELK HSYSTRIFGL
ELIQTALEIS GDRLQLYPRL FTLISDPIFK SILFIIQNTT KLSLLQATLQ LFTTLVVILG
NNLQLQIELT LTRIFSILLD DGTANNSSSE NKNKPSIIKE LLIEQISILW TRSPSFFTST
FINFDCNLDR ADVSINFLKA LTKLALPESA LTTTESVPPI CLEGLVSLVD DMFDHMKDID
REEFGRQKNE MEILKKRDRK TEFIECTNAF NEKPKKGIPM LIEKGFIASD SDKDIAEFLF
NNNNRMNKKT IGLLLCHPDK VSLLNEYIRL FDFSGLRVDE AIRILLTKFR LPGESQQIER
IIEAFSSAYC ENQDYDPSKI SDNAEDDIST VQPDADSVFI LSYSIIMLNT DLHNPQVKEH
MSFEDYSGNL KGCCNHKDFP FWYLDRIYCS IRDKEIVMPE EHHGNEKWFE DAWNNLISST
TVITEIKKDT QSVMDKLTPL ELLNFDRAIF KQVGPSIVST LFNIYVVASD DHISTRMITS
LDKCSYISAF FDFKDLFNDI LNSIAKGTTL INSSHDDELS TLAFEYGPMP LVQIKFEDTN
TEIPVSTDAV RFGRSFKGQL NTVVFFRIIR RNKDPKIFSK ELWLNIVNII LTLYEDLILS
PDIFPDLQKR LKLSNLPKPS PEISINKSKE SKGLLSTFAS YLKGDEEPTE EEIKSSKKAM
ECIKSSNIAA SVFGNESNIT ADLIKTLLDS AKTEKNADNS RYFEAELLFI IELTIALFLF
CKEEKELGKF ILQKVFQLSH TKGLTKRTVR RMLTYKILLI SLCADQTEYL SKLINDELLK
KGDIFTQKFF ATNQGKEFLK RLFSLTESEF YRGFLLGNEN FWKFLRKVTA MKEQSESIFE
YLNESIKTDS NILTNENFMW VLGLLDEISS MGAVGNHWEI EYKKLTESGH KIDKENPYKK
SIELSLKSIQ LTSHLLEDNN DLRKNEIFAI IQALAHQCIN PCKQISEFAV VTLEQTLINK
IEIPTNEMES VEELIEGGLL PLLNSSETQE DQKILISSIL TIISNVYLHY LKLGKTSNET
FLKILSIFNK FVEDSDIEKK LQQLILDKKS IEKGNGSSSH GSAHEQTPES NDVEIEATAP
IDDNTDDDNK PKLSDVEKD
