GEA1_YEAST
ID GEA1_YEAST Reviewed; 1408 AA.
AC P47102; D6VWK4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ARF guanine-nucleotide exchange factor 1;
GN Name=GEA1; OrderedLocusNames=YJR031C; ORFNames=J1580;
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].
RX PubMed=8619316; DOI=10.1002/yea.320111208;
RA Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J.,
RA Herbert C.J.;
RT "The sequence of 24.3 kb from chromosome X reveals five complete open
RT reading frames, all of which correspond to new genes, and a tandem
RT insertion of a Ty1 transposon.";
RL Yeast 11:1179-1186(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 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 [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 INTERACTION WITH GMH1, AND MUTAGENESIS OF LEU-862.
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 [7]
RP INTERACTION WITH SEC21.
RX PubMed=19039328; DOI=10.1038/embor.2008.221;
RA Deng Y., Golinelli-Cohen M.P., Smirnova E., Jackson C.L.;
RT "A COPI coat subunit interacts directly with an early-Golgi localized Arf
RT exchange factor.";
RL EMBO Rep. 10:58-64(2009).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in maintaining mitochondrial morphology, and in the
CC turnover of mitochondria through mitophagy (PubMed:25190516).
CC {ECO:0000269|PubMed:25190516}.
CC -!- SUBUNIT: Interacts with GMH1. Interacts (via N-terminal region) with
CC SEC21 (via C-terminus). {ECO:0000269|PubMed:12808035,
CC ECO:0000269|PubMed:19039328}.
CC -!- INTERACTION:
CC P47102; P32074: SEC21; NbExp=6; IntAct=EBI-7539, EBI-4891;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P39993}. Membrane
CC {ECO:0000250|UniProtKB:P39993}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P39993}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:25190516}. Mitochondrion
CC {ECO:0000269|PubMed:25190516}. Note=Soluble and partially membrane-
CC bound. {ECO:0000250|UniProtKB:P39993}.
CC -!- DOMAIN: The SEC7 domain is sufficient for stimulation of nucleotide
CC exchange on myristoylated yeast ARF2.
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49531; CAA89558.1; -; Genomic_DNA.
DR EMBL; X87297; CAA60724.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08820.1; -; Genomic_DNA.
DR PIR; S57049; S57049.
DR RefSeq; NP_012565.1; NM_001181689.1.
DR PDB; 1RE0; X-ray; 2.40 A; B=540-754.
DR PDBsum; 1RE0; -.
DR AlphaFoldDB; P47102; -.
DR SMR; P47102; -.
DR BioGRID; 33784; 102.
DR DIP; DIP-5697N; -.
DR IntAct; P47102; 7.
DR MINT; P47102; -.
DR STRING; 4932.YJR031C; -.
DR CarbonylDB; P47102; -.
DR MaxQB; P47102; -.
DR PaxDb; P47102; -.
DR PRIDE; P47102; -.
DR EnsemblFungi; YJR031C_mRNA; YJR031C; YJR031C.
DR GeneID; 853488; -.
DR KEGG; sce:YJR031C; -.
DR SGD; S000003792; GEA1.
DR VEuPathDB; FungiDB:YJR031C; -.
DR eggNOG; KOG0928; Eukaryota.
DR GeneTree; ENSGT00940000176690; -.
DR HOGENOM; CLU_001204_0_1_1; -.
DR InParanoid; P47102; -.
DR BioCyc; YEAST:G3O-31669-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; P47102; -.
DR PRO; PR:P47102; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47102; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 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; Endoplasmic reticulum;
KW Guanine-nucleotide releasing factor; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1408
FT /note="ARF guanine-nucleotide exchange factor 1"
FT /id="PRO_0000120212"
FT DOMAIN 552..706
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 262..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39993"
FT MUTAGEN 862
FT /note="L->S: Abolishes interaction with GMH1."
FT /evidence="ECO:0000269|PubMed:12808035"
FT HELIX 540..554
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 556..565
FT /evidence="ECO:0007829|PDB:1RE0"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 574..584
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 590..597
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 603..610
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 620..627
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 637..653
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 687..705
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 715..721
FT /evidence="ECO:0007829|PDB:1RE0"
FT TURN 722..725
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 733..745
FT /evidence="ECO:0007829|PDB:1RE0"
FT HELIX 751..753
FT /evidence="ECO:0007829|PDB:1RE0"
SQ SEQUENCE 1408 AA; 159437 MW; 3385C8FA4252EBBE CRC64;
MHDVPMETVL AVNPATMIVK ECINLCSAMN KQSRDKSQTS VAALLGGGSD IFLSQSDSFV
DSFHNLPTSS YHDPLISGLV QLRLKINDLK GLDSLNALEL LKPFLEIVSA SSVSGYTTSL
ALDSLQKVFT LKIINKTFND IQIAVRETVV ALTHCRFEAS KQISDDSVLL KVVTLLRDII
TSSFGDYLSD TIIYDVLQTT LSLACNTQRS EVLRKTAEVT IAGITVKLFT KLKLLDPPTK
TEKYINDESY TDNNLKDDII GTTTSDNDLS STDDDSAVAD DNKNEKPVQQ VIREQENDEE
TAEKAENVEP NYGITVIKDY LGLLLSLVMP ENRMKHTTSA MKLSLQLINA AIEISGDKFP
LYPRLFSLIS DPIFKSVLFI IQSSTQYSLL QATLQLFTSL VVILGDYLPM QIELTLRRIF
EILEDTTISG DVSKQKPPAI RELIIEQLSI LWIHSPAFFL QLFVNFDCNL DRSDLSIDFI
KELTKFSLPA AAVNTSNNIP PICLEGVLSL IENIYNDLQR FDRAEFVKNQ KEIDILKQRD
RKTEFILCVE TFNEKAKKGI QMLIEKGFID SDSNRDIASF LFLNNGRLNK KTIGLLLCDP
KKTSLLKEFI DLFDFKGLRV DEAIRILLTK FRLPGESQQI ERIVEAFSSK YSADQSNDKV
ELEDKKAGKN GSESMTEDDI IHVQPDADSV FVLSYSIIML NTDSHNPQVK DHMTFDDYSN
NLRGCYNGKD FPRWYLHKIY TSIKVKEIVM PEEHHGNERW FEDAWNNLIS STSVMTEMQR
DFTNPISKLA QIDILQYEKA IFSNVRDIIL KTLFKIFTVA SSDQISLRIL DAISKCTFIN
YYFSFDQSYN DTVLHLGEMT TLAQSSAKAV ELDVDSIPLV EIFVEDTGSK ISVSNQSIRL
GQNFKAQLCT VLYFQIIKEI SDPSIVSTRL WNQIVQLILK LFENLLMEPN LPFFTNFHSL
LKLPELPLPD PDISIRKAKM SRSLLSTFAS YLKGDEEPSE EDIDFSIKAF ECVKASHPLS
SVFENNQLVS PKMIETLLSS LVIEKTSENS PYFEQELLFL LEISIILISE ASYGQEFGAL
IADHMINISN LDGLSKEAIA RLASYKMFLV SRFDNPRDIL SDLIEHDFLV KNEIFNTKYY
ESEWGKQVIN DLFTHLNDVK YNERALKNVK FWNFLRILIS AKDRQFAVYT FLEKYIQNGD
IFVDDGNFMN ILSLLDEMSC AGAVGTKWEQ NYENSVEDGC EAPESNPYRS IIDLSSRSIN
ITADLLSTVG RSNSALNKNE IIAAIQGLAH QCLNPCDELG MQALQALENI LLSRASQLRT
EKVAVDNLLE TGLLPIFELD EIQDVKMKRI TSILSVLSKI FLGQLVEGVT SNETFLRVLN
VFNKYVDDPT VERQLQELII SKREIEKE
