GOGC6_ARATH
ID GOGC6_ARATH Reviewed; 914 AA.
AC B0F9L4; Q940C3; Q9LT59;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Golgin candidate 6;
DE Short=AtGC6;
DE AltName: Full=Protein MAIGO 4 {ECO:0000303|PubMed:20837504};
GN Name=GC6; Synonyms=MAG4 {ECO:0000303|PubMed:20837504};
GN OrderedLocusNames=At3g27530; ORFNames=MMJ24.8, MMJ24_7;
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 [MRNA], SUBCELLULAR LOCATION, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=18182439; DOI=10.1093/jxb/erm304;
RA Latijnhouwers M., Gillespie T., Boevink P., Kriechbaumer V., Hawes C.,
RA Carvalho C.M.;
RT "Localization and domain characterization of Arabidopsis golgin
RT candidates.";
RL J. Exp. Bot. 58:4373-4386(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-914.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND DOMAIN.
RX PubMed=20837504; DOI=10.1093/pcp/pcq137;
RA Takahashi H., Tamura K., Takagi J., Koumoto Y., Hara-Nishimura I.,
RA Shimada T.;
RT "MAG4/Atp115 is a golgi-localized tethering factor that mediates efficient
RT anterograde transport in Arabidopsis.";
RL Plant Cell Physiol. 51:1777-1787(2010).
CC -!- FUNCTION: Golgi matrix protein playing a role in tethering of vesicles
CC to Golgi membranes and in maintaining the overall structure of the
CC Golgi apparatus. Functions in the anterograde transport of storage
CC protein precursors from the endoplasmic reticulum (ER) to the Golgi
CC complex. {ECO:0000269|PubMed:20837504}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:18182439}.
CC Golgi apparatus, Golgi stack {ECO:0000269|PubMed:20837504}.
CC Note=Concentrates only on one side of the Golgi bodies.
CC {ECO:0000269|PubMed:18182439}.
CC -!- DOMAIN: The C-terminal domain (689-914) is necessary and sufficient for
CC Golgi targeting. {ECO:0000269|PubMed:18182439}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants and accumulation of the precursors
CC of the two major storage proteins albumin 2S and globulin 12S in dry
CC seeds. {ECO:0000269|PubMed:20837504}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL07004.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB01283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EU249327; ABY67247.1; -; mRNA.
DR EMBL; AB025626; BAB01283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77334.1; -; Genomic_DNA.
DR EMBL; AY056118; AAL07004.1; ALT_FRAME; mRNA.
DR EMBL; BT001017; AAN46771.1; -; mRNA.
DR RefSeq; NP_566820.1; NM_113669.3.
DR AlphaFoldDB; B0F9L4; -.
DR SMR; B0F9L4; -.
DR BioGRID; 7705; 2.
DR STRING; 3702.AT3G27530.1; -.
DR iPTMnet; B0F9L4; -.
DR PaxDb; B0F9L4; -.
DR PRIDE; B0F9L4; -.
DR ProteomicsDB; 248453; -.
DR EnsemblPlants; AT3G27530.1; AT3G27530.1; AT3G27530.
DR GeneID; 822375; -.
DR Gramene; AT3G27530.1; AT3G27530.1; AT3G27530.
DR KEGG; ath:AT3G27530; -.
DR Araport; AT3G27530; -.
DR TAIR; locus:2091438; AT3G27530.
DR eggNOG; KOG0946; Eukaryota.
DR HOGENOM; CLU_006318_3_0_1; -.
DR InParanoid; B0F9L4; -.
DR OMA; YSRACKQ; -.
DR OrthoDB; 1273987at2759; -.
DR PhylomeDB; B0F9L4; -.
DR PRO; PR:B0F9L4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; B0F9L4; baseline and differential.
DR Genevisible; B0F9L4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR GO; GO:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:TAIR.
DR GO; GO:0045056; P:transcytosis; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006955; Uso1_p115_C.
DR InterPro; IPR006953; Vesicle_Uso1_P115_head.
DR Pfam; PF04871; Uso1_p115_C; 1.
DR Pfam; PF04869; Uso1_p115_head; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..914
FT /note="Golgin candidate 6"
FT /id="PRO_0000348540"
FT COILED 723..837
FT /evidence="ECO:0000255"
FT COILED 863..901
FT /evidence="ECO:0000255"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT CONFLICT 93
FT /note="L -> V (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Q -> H (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="R -> G (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="H -> P (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="M -> I (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="T -> A (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="K -> I (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="S -> P (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="N -> Y (in Ref. 1; ABY67247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 101834 MW; E1D968FD2CC103E3 CRC64;
MDLASRYKGV VGMVFGDNQS SNEDSYIQRL LDRISNGTLP DDRRTAIVEL QSVVAESNAA
QLAFGAAGFP VIVGILKDQR DDLEMVRGAL ETLLGALTPI DHARAQKTEV QAALMNSDLL
SREAENITLL LSLLEEEDFY VRYYTLQILT ALLMNSQNRL QEAILTTPRG ITRLMDMLMD
REVIRNEALL LLTHLTREAE EIQKIVVFEG AFEKIFSIIK EEGGSDGDVV VQDCLELLNN
LLRSSSSNQI LLRETMGFEP IISILKLRGI TYKFTQQKTV NLLSALETIN MLIMGRADTE
PGKDSNKLAN RTVLVQKKLL DYLLMLGVES QWAPVAVRCM TFKCIGDLID GHPKNRDILA
SKVLGEDRQV EPALNSILRI ILQTSSIQEF VAADYVFKTF CEKNTEGQTM LASTLIPQPH
PTSRDHLEDD VHMSFGSMLL RGLCSGEADG DLETCCRAAS ILSHVVKDNL RCKEKALKIV
LESPMPSMGT PEPLFQRIVR YLAVASSMKS KEKSSTLGKS YIQQIILKLL VTWTVDCPTA
VQCFLDSRHH LTFLLELVTD PAATVCIRGL ASILLGECVI YNKSIENGKD AFSVVDAVGQ
KMGLTSYFSK FEEMQNSFIF SPSKKPPQGY KPLTRTPTPS EAEINEVDEV DEMVKGNEDH
PMLLSLFDAS FIGLVKSLEG NIRERIVDVY SRPKSEVAVV PADLEQKSGE NEKDYINRLK
AFIEKQCSEI QNLLARNAAL AEDVASSGRN EQSQGSEQRA STVMDKVQME SIRRELQETS
QRLETVKAEK AKIESEASSN KNMAAKLEFD LKSLSDAYNS LEQANYHLEQ EVKSLKGGES
PMQFPDIEAI KEEVRKEAQK ESEDELNDLL VCLGQEESKV EKLSAKLIEL GVDVDKLLED
IGDESEAQAE SEED
