GNL1_ARATH
ID GNL1_ARATH Reviewed; 1443 AA.
AC Q9FLY5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=ARF guanine-nucleotide exchange factor GNL1;
DE AltName: Full=Protein ENDOPLASMIC RETICULUM MORPHOLOGY 1;
DE AltName: Full=Protein GNOM-like 1;
GN Name=GNL1; Synonyms=ERMO1, GBF1; OrderedLocusNames=At5g39500;
GN ORFNames=MUL8.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY.
RX PubMed=12553910; DOI=10.1016/s0092-8674(03)00003-5;
RA Geldner N., Anders N., Wolters H., Keicher J., Kornberger W., Muller P.,
RA Delbarre A., Ueda T., Nakano A., Juergens G.;
RT "The Arabidopsis GNOM ARF-GEF mediates endosomal recycling, auxin
RT transport, and auxin-dependent plant growth.";
RL Cell 112:219-230(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14742722; DOI=10.1091/mbc.e03-06-0443;
RA Cox R., Mason-Gamer R.J., Jackson C.L., Segev N.;
RT "Phylogenetic analysis of Sec7-domain-containing Arf nucleotide
RT exchangers.";
RL Mol. Biol. Cell 15:1487-1505(2004).
RN [5]
RP GENE FAMILY, SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17653190; DOI=10.1038/nature05967;
RA Richter S., Geldner N., Schrader J., Wolters H., Stierhof Y.D., Rios G.,
RA Koncz C., Robinson D.G., Juergens G.;
RT "Functional diversification of closely related ARF-GEFs in protein
RT secretion and recycling.";
RL Nature 448:488-492(2007).
RN [6]
RP FUNCTION.
RX PubMed=17653191; DOI=10.1038/nature06023;
RA Teh O.K., Moore I.;
RT "An ARF-GEF acting at the Golgi and in selective endocytosis in polarized
RT plant cells.";
RL Nature 448:493-496(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19933201; DOI=10.1105/tpc.109.068270;
RA Nakano R.T., Matsushima R., Ueda H., Tamura K., Shimada T., Li L.,
RA Hayashi Y., Kondo M., Nishimura M., Hara-Nishimura I.;
RT "GNOM-LIKE1/ERMO1 and SEC24a/ERMO2 are required for maintenance of
RT endoplasmic reticulum morphology in Arabidopsis thaliana.";
RL Plant Cell 21:3672-3685(2009).
RN [8]
RP REVIEW, AND FUNCTION.
RX PubMed=20036441; DOI=10.1016/j.ejcb.2009.11.020;
RA Richter S., Anders N., Wolters H., Beckmann H., Thomann A., Heinrich R.,
RA Schrader J., Singh M.K., Geldner N., Mayer U., Juergens G.;
RT "Role of the GNOM gene in Arabidopsis apical-basal patterning--From mutant
RT phenotype to cellular mechanism of protein action.";
RL Eur. J. Cell Biol. 89:138-144(2010).
RN [9]
RP FUNCTION.
RX PubMed=21118984; DOI=10.1073/pnas.1016260107;
RA Naramoto S., Kleine-Vehn J., Robert S., Fujimoto M., Dainobu T.,
RA Paciorek T., Ueda T., Nakano A., Van Montagu M.C., Fukuda H., Friml J.;
RT "ADP-ribosylation factor machinery mediates endocytosis in plant cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21890-21895(2010).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in vesicular protein sorting. Acts as the major
CC regulator of retrograde Golgi to endoplasmic reticulum trafficking but
CC is also involved in the endocytosis process. Could function redundantly
CC with GNOM. Regulates vesicle trafficking required for the coordinated
CC polar localization of auxin efflux carriers which in turn determines
CC the direction of auxin flow. Mediates the endocytosis of PIN2 from
CC plasma membrane to endosomal compartments. Required for maintenance of
CC endoplasmic reticulum morphology. {ECO:0000269|PubMed:17653190,
CC ECO:0000269|PubMed:17653191, ECO:0000269|PubMed:19933201,
CC ECO:0000269|PubMed:20036441, ECO:0000269|PubMed:21118984}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17653190}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:17653190}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17653190}; Cytoplasmic side
CC {ECO:0000269|PubMed:17653190}. Note=Soluble and partially membrane-
CC bound.
CC -!- DISRUPTION PHENOTYPE: Slightly abnormal Golgi stacks with laterally
CC expanded cisternae. Abnormal formation of spherical bodies in the
CC endoplasmic reticulum. {ECO:0000269|PubMed:17653190,
CC ECO:0000269|PubMed:19933201}.
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DR EMBL; AB009054; BAB11025.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94441.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69458.1; -; Genomic_DNA.
DR RefSeq; NP_001318705.1; NM_001344295.1.
DR RefSeq; NP_198766.1; NM_123312.2.
DR AlphaFoldDB; Q9FLY5; -.
DR SMR; Q9FLY5; -.
DR STRING; 3702.AT5G39500.1; -.
DR iPTMnet; Q9FLY5; -.
DR PaxDb; Q9FLY5; -.
DR PRIDE; Q9FLY5; -.
DR ProteomicsDB; 248536; -.
DR EnsemblPlants; AT5G39500.1; AT5G39500.1; AT5G39500.
DR EnsemblPlants; AT5G39500.2; AT5G39500.2; AT5G39500.
DR GeneID; 833946; -.
DR Gramene; AT5G39500.1; AT5G39500.1; AT5G39500.
DR Gramene; AT5G39500.2; AT5G39500.2; AT5G39500.
DR KEGG; ath:AT5G39500; -.
DR Araport; AT5G39500; -.
DR TAIR; locus:2175728; AT5G39500.
DR eggNOG; KOG0928; Eukaryota.
DR HOGENOM; CLU_001204_1_0_1; -.
DR InParanoid; Q9FLY5; -.
DR OMA; AITHCRF; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; Q9FLY5; -.
DR PRO; PR:Q9FLY5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLY5; baseline and differential.
DR Genevisible; Q9FLY5; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0080119; P:ER body organization; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IMP:UniProtKB.
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 3: Inferred from homology;
KW Cytoplasm; Endocytosis; ER-Golgi transport; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1443
FT /note="ARF guanine-nucleotide exchange factor GNL1"
FT /id="PRO_0000420948"
FT DOMAIN 554..743
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 917..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 658
FT /evidence="ECO:0000250"
SQ SEQUENCE 1443 AA; 161954 MW; 3BAE314E9C082B72 CRC64;
MGYQNHPSGS NSFHGEFKRC HSKPSKGAVA SMINSEIGAV LAVMRRNVRW GVRYIADDDQ
LEHSLIHSLK ELRKQIFSWQ SNWQYVDPRL YIQPFLDVIL SDETGAPITG VALSSVYKIL
TLEVFTLETV NVGEAMHIIV DAVKSCRFEV TDPASEEVVL MKILQVLLAC VKSKASNGLS
NQDICTIVNT CLRVVHQSSS KSELLQRIAR HTMHELIRCI FSQLPFISPL ANECELHVDN
KVGTVDWDPN SGEKRVENGN IASISDTLGT DKDDPSSEMV IPETDLRNDE KKTEVSDDLN
AAANGENAMM APYGIPCMVE IFHFLCTLLN VGENGEVNSR SNPIAFDEDV PLFALGLINS
AIELGGPSFR EHPKLLTLIQ DDLFCNLMQF GMSMSPLILS TVCSIVLNLY LNLRTELKVQ
LEAFFSYVLL RIAQSKHGSS YQQQEVAMEA LVDLCRQHTF IAEVFANFDC DITCSNVFED
VSNLLSKNAF PVNGPLSAMH ILALDGLISM VQGMAERVGE ELPASDVPTH EERYEEFWTV
RCENYGDPNF WVPFVRKVKH IKKKLMLGAD RFNRDPNKGL QYLQGVHLLP EKLDPKSVAC
FFRYTCGLDK NVMGDFLGNH DQFCIQVLHE FAKTFDFQNM NLATALRLFV GTFKLSGEAQ
KIHRVLEAFS ERYYEQSPHI LIDKDAAFVL AYSIILLNTD QHNAQVKTRM TEEDFIRNNR
TINGGADLPR EYLSEIYHSI RHSEIQMDED KGTGFQLMTA SRWISVIYKS KETSPYIQCD
AASHLDRDMF YIVSGPTIAA TSVVFEQAEQ EDVLRRCIDG LLAIAKLSAY YHLNSVLDDL
VVSLCKFTPF FAPLSADEAV LVLGEDARAR MATEAVFLIA NKYGDYISAG WKNILECVLS
LNKLHILPDH IASDAADDPE LSTSNLEQEK PSANPVPVVS QSQPSAMPRK SSSFIGRFLL
SFDSEETKPL PSEEELAAYK HARGIVKDCH IDSIFSDSKF LQAESLQQLV NSLIRASGKD
EASSVFCLEL LIAVTLNNRD RILLIWPTVY EHILGIVQLT LTPCTLVEKA VFGVLKICQR
LLPYKENLTD ELLKSLQLVL KLKAKVADAY CERIAQEVVR LVKANASHVR SRTGWRTIIS
LLSITARHPE ASEAGFEALR FIMSEGAHLL PSNYELCLDA ASHFAESRVG EVDRSISAID
LMSNSVFCLA RWSQEAKNSI GETDAMMKLS EDIGKMWLKL VKNLKKVCLD QRDEVRNHAI
SMLQRAIAGA DGIMLPQPLW FQCFDSAVFI LLDDVLTFSI ENSRKTLKKT VEETLVLATK
LMSKAFLQSL QDISQQPSFC RLWVGVLNRL ETYMSTEFRG KRSEKVNELI PELLKNTLLV
MKATGVLLPG DDIGSDSFWQ LTWLHVNKIS PSLQSEVFPQ EELDQFQRRN AKPEDPPVPG
NEV
