MAG5_ARATH
ID MAG5_ARATH Reviewed; 1350 AA.
AC Q9FGK9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein transport protein SEC16A homolog {ECO:0000305};
DE AltName: Full=Protein MAIGO 5 {ECO:0000303|PubMed:24280388};
GN Name=MAG5 {ECO:0000303|PubMed:24280388};
GN Synonyms=SEC16A {ECO:0000303|PubMed:24280388};
GN OrderedLocusNames=At5g47480 {ECO:0000312|Araport:AT5G47480};
GN ORFNames=MNJ7.7 {ECO:0000312|EMBL:BAB09074.1};
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 {ECO:0000312|EMBL:BAB09074.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY 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 [4]
RP IDENTIFICATION BY 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH SEC13A;
RP SEC13B AND SEC31A, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24280388; DOI=10.1105/tpc.113.118158;
RA Takagi J., Renna L., Takahashi H., Koumoto Y., Tamura K., Stefano G.,
RA Fukao Y., Kondo M., Nishimura M., Shimada T., Brandizzi F.,
RA Hara-Nishimura I.;
RT "MAIGO5 functions in protein export from Golgi-associated endoplasmic
RT reticulum exit sites in Arabidopsis.";
RL Plant Cell 25:4658-4675(2013).
CC -!- FUNCTION: Required for efficient protein export from the endoplasmic
CC reticulum (ER) to the Golgi by regulating COPII coat dynamics at the
CC ER. Functions as a scaffold and regulator of COPII coat assembly at ER
CC exit sites. {ECO:0000269|PubMed:24280388}.
CC -!- SUBUNIT: Interacts with SEC13A, SEC13B and SEC31A.
CC {ECO:0000269|PubMed:24280388}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:24280388}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:24280388}. Note=Localizes at Golgi-associated cup-
CC shaped endoplasmic reticulum exit sites. {ECO:0000269|PubMed:24280388}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but dry seeds of mutant plants accumulate the precursors of
CC the two major storage proteins albumin 2S and globulin 12S.
CC {ECO:0000269|PubMed:24280388}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR EMBL; AB025628; BAB09074.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95524.1; -; Genomic_DNA.
DR RefSeq; NP_199559.1; NM_124121.3.
DR AlphaFoldDB; Q9FGK9; -.
DR STRING; 3702.AT5G47480.1; -.
DR iPTMnet; Q9FGK9; -.
DR PaxDb; Q9FGK9; -.
DR PRIDE; Q9FGK9; -.
DR ProteomicsDB; 239039; -.
DR EnsemblPlants; AT5G47480.1; AT5G47480.1; AT5G47480.
DR GeneID; 834798; -.
DR Gramene; AT5G47480.1; AT5G47480.1; AT5G47480.
DR KEGG; ath:AT5G47480; -.
DR Araport; AT5G47480; -.
DR TAIR; locus:2168998; AT5G47480.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_002428_1_0_1; -.
DR InParanoid; Q9FGK9; -.
DR OMA; FAQQQFI; -.
DR OrthoDB; 106114at2759; -.
DR PhylomeDB; Q9FGK9; -.
DR PRO; PR:Q9FGK9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGK9; baseline and differential.
DR Genevisible; Q9FGK9; AT.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1350
FT /note="Protein transport protein SEC16A homolog"
FT /id="PRO_0000430536"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FGK8"
SQ SEQUENCE 1350 AA; 145879 MW; 0EE50B5BBB0C3934 CRC64;
MASTADFLLD DQTDEDFFDK LVDDSYTPTA SSSAKELKFD DGSDSDDAKA FANLSVVDDV
LGDGDVALNE AGLGNDVANE GTSGSVGKEE PSSSIAPEAV QFVNSDANRL RDVDVVRSEV
DDMALTETGK ESNIVDGSGS PGVKEVDWGS FYADSSVNDG GGFGSYSDFF TELDATAGNV
QGQAEVAVAT GGNLVANDTI NTSVGLDNSA GFEQHQGQVQ HDSGSGQYVD NSQSWENLYP
GWKYDASTGQ WYQVDGQDAT VNSQESYINS TGNWESVAAD NSDVAYLKQS TTSAMAGTAE
SVSTWNQVSQ VGNGYPEHMV FDAQYPGWYY DTIAQEWRSL DSYNQASQTT VTGQAHDQQV
QNGHARTTTY HNNSQSSVYD VNNKNQTFKA QDFAIQGQHG SWDESYYANN QQAGNTWQPV
NVGKAEPAVT SDSLSRFGGN QQVNNLYSTE SVAEQFKPNT IGAQSFIPQH MNVASATQNG
PLSFSNDLYN RQQSVDHAQK SFQNNQLFSP SVGRSSDRRP PHALVSFGFG GKLIVMKDNN
GSLQNTSFGS QGIGGSSITV LNLAEVISGS ASYSSPGEDS LSYFRCLHQQ SLPGPLVGGN
VGSKELHKWI DERLLHCESS NMDFSRGKLL KMLLSLLRIS CQYYGKLRSP FGSDASQKET
DTPEAAVAKL FAFAKKDGIQ NGYAPISQCL QHLPPESQMQ VTASEVQNLL ASGRKMEALQ
CAQEGHLWGP ALVIAAQLGD QFYVDTVKQM ALRQLIPGSP LRTLCLLVAG QPAEVCPTGS
SSSMLDNWEE NLGIITANRT TDDDLVIIHL GDSMWKERGE IIAAHICYLI ADKNFDPYSE
SARLCLVGAD HWKCPRTYAS PDAIQRTELY EYSKTLGNSQ YILLPFQPYK IIYAHMLAEV
GKLSTAQKYC QAVIRCLKTS RSSEVEMWKQ FASSLEERIR SHQEGGNLAP AKLVGKLLNS
LWGMPPPAPH STTGNPQVNE YQHQQQEAAK LSYSQSANTM SSLMPPASIE PVHEWGGNGR
TMAAHSRSVS EPDFSRTPIQ DQTDSSKDKA PDGVTQVKST RKVPSSRFSR FGIGILKNTV
GKVFPSRSSN EAKLGNENQF YYDDNLKRWV ERGVEPPAEE AALPPPPTSV PFRSNSLGHE
NKSEIKNEMS PSSGSWSSGS PTPSENSPGI PPVSQGSNQF SARGRMGVRA RYVDTYNQGS
SSMYQSPPVQ SSKPPIPAKA KFFVPAAPAS FANDQVMESV SAETRQENSG DEAVVGSAGA
PGPSQASFQS PTPSPIAMQR FPSVDNIRRS GSGTSLNGDL PQSVSRRTAS WSGSVNSSSF
MSPTSASTFR PSPLNSSSSS LGEELQEVEL
