MAG2_ARATH
ID MAG2_ARATH Reviewed; 795 AA.
AC Q9STU3; Q8RWD1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=RINT1-like protein MAG2 {ECO:0000305};
DE AltName: Full=Protein MAIGO 2 {ECO:0000303|PubMed:17194767};
GN Name=MAG2 {ECO:0000303|PubMed:17194767};
GN OrderedLocusNames=At3g47700 {ECO:0000312|Araport:AT3G47700};
GN ORFNames=T23J7.30 {ECO:0000312|EMBL:CAB41853.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, INTERACTION WITH SEC20 AND SYP81, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-265; VAL-330 AND LEU-348.
RX PubMed=17194767; DOI=10.1105/tpc.106.046151;
RA Li L., Shimada T., Takahashi H., Ueda H., Fukao Y., Kondo M., Nishimura M.,
RA Hara-Nishimura I.;
RT "MAIGO2 is involved in exit of seed storage proteins from the endoplasmic
RT reticulum in Arabidopsis thaliana.";
RL Plant Cell 18:3535-3547(2006).
RN [5]
RP FUNCTION, INTERACTION WITH ZW10, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23025793; DOI=10.1111/j.1399-3054.2012.01704.x;
RA Zhao P., Liu F., Zhang B., Liu X., Wang B., Gong J., Yu G., Ma M., Lu Y.,
RA Sun J., Wang Z., Jia P., Liu H.;
RT "MAIGO2 is involved in abscisic acid-mediated response to abiotic stresses
RT and Golgi-to-ER retrograde transport.";
RL Physiol. Plantarum 148:246-260(2013).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH ZW10/MIP1;
RP MIP2 AND MIP3, AND DISRUPTION PHENOTYPE.
RX PubMed=24118572; DOI=10.1111/tpj.12347;
RA Li L., Shimada T., Takahashi H., Koumoto Y., Shirakawa M., Takagi J.,
RA Zhao X., Tu B., Jin H., Shen Z., Han B., Jia M., Kondo M., Nishimura M.,
RA Hara-Nishimura I.;
RT "MAG2 and three MAG2-INTERACTING PROTEINs form an ER-localized complex to
RT facilitate storage protein transport in Arabidopsis thaliana.";
RL Plant J. 76:781-791(2013).
CC -!- FUNCTION: Functions in the anterograde transport of storage protein
CC precursors from the endoplasmic reticulum (ER) to the Golgi complex and
CC in the retrograde transport from the Golgi complex to the ER
CC (PubMed:17194767, PubMed:23025793). Forms a complex with ZW10/MIP1,
CC MIP2 and MIP3 on the ER that may be responsible for efficient transport
CC of seed storage proteins (PubMed:24118572). Required for the responses
CC to environmental stresses during seed germination and vegetative
CC growth. Probably not involved in the retrograde transport from the ER
CC to the apoplast (PubMed:23025793). {ECO:0000269|PubMed:17194767,
CC ECO:0000269|PubMed:23025793, ECO:0000269|PubMed:24118572}.
CC -!- SUBUNIT: Interacts with SEC20 and SYP81 (PubMed:17194767). Interacts
CC with ZW10 (via the central region) (PubMed:23025793). Forms a complex
CC with ZW10/MIP1, MIP2 and MIP3 on the endoplasmic reticulum
CC (PubMed:24118572). {ECO:0000269|PubMed:17194767,
CC ECO:0000269|PubMed:23025793, ECO:0000269|PubMed:24118572}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein {ECO:0000269|PubMed:17194767,
CC ECO:0000269|PubMed:23025793}.
CC -!- TISSUE SPECIFICITY: Highly expressed in dry seeds. Expressed at low
CC levels in roots, rosette and cauline leaves, stems and flowers.
CC {ECO:0000269|PubMed:23025793}.
CC -!- INDUCTION: By salt and osmotic stresses. {ECO:0000269|PubMed:23025793}.
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 (PubMed:17194767). Increased sensitivity to salt stress, osmotic stress
CC and abscisic acid (ABA) during germination and vegetative growth
CC (PubMed:23025793). {ECO:0000269|PubMed:17194767,
CC ECO:0000269|PubMed:23025793}.
CC -!- SIMILARITY: Belongs to the RINT1 family. {ECO:0000305}.
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DR EMBL; AL049746; CAB41853.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78320.1; -; Genomic_DNA.
DR EMBL; AY093173; AAM13172.1; -; mRNA.
DR PIR; T07709; T07709.
DR RefSeq; NP_190354.1; NM_114638.3.
DR AlphaFoldDB; Q9STU3; -.
DR SMR; Q9STU3; -.
DR BioGRID; 9244; 3.
DR STRING; 3702.AT3G47700.1; -.
DR iPTMnet; Q9STU3; -.
DR PaxDb; Q9STU3; -.
DR PRIDE; Q9STU3; -.
DR ProteomicsDB; 238231; -.
DR EnsemblPlants; AT3G47700.1; AT3G47700.1; AT3G47700.
DR GeneID; 823924; -.
DR Gramene; AT3G47700.1; AT3G47700.1; AT3G47700.
DR KEGG; ath:AT3G47700; -.
DR Araport; AT3G47700; -.
DR TAIR; locus:2100327; AT3G47700.
DR eggNOG; KOG2218; Eukaryota.
DR HOGENOM; CLU_384326_0_0_1; -.
DR InParanoid; Q9STU3; -.
DR OMA; FRTGWVE; -.
DR OrthoDB; 1393136at2759; -.
DR PhylomeDB; Q9STU3; -.
DR PRO; PR:Q9STU3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STU3; baseline and differential.
DR Genevisible; Q9STU3; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0070939; C:Dsl1/NZR complex; IBA:GO_Central.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR007528; RINT1_Tip20.
DR PANTHER; PTHR13520; PTHR13520; 1.
DR Pfam; PF04437; RINT1_TIP1; 1.
DR PROSITE; PS51386; RINT1_TIP20; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..795
FT /note="RINT1-like protein MAG2"
FT /id="PRO_0000430530"
FT DOMAIN 207..795
FT /note="RINT1/TIP20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00717"
FT REGION 91..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..64
FT /evidence="ECO:0000255"
FT MUTAGEN 265
FT /note="S->N: In mag2-5; accumulation of precursors of
FT storage proteins in dry seeds."
FT /evidence="ECO:0000269|PubMed:17194767"
FT MUTAGEN 330
FT /note="V->M: In mag2-6; accumulation of precursors of
FT storage proteins in dry seeds."
FT /evidence="ECO:0000269|PubMed:17194767"
FT MUTAGEN 348
FT /note="L->F: In mag2-7; accumulation of precursors of
FT storage proteins in dry seeds."
FT /evidence="ECO:0000269|PubMed:17194767"
FT CONFLICT 227
FT /note="R -> Q (in Ref. 3; AAM13172)"
SQ SEQUENCE 795 AA; 90233 MW; 3E4A3E8D36105088 CRC64;
MEAIKPLPQV SSFSASVFSF LDGRFKESTD LSHSTGLVSE LQTEISELDQ RLAGLNRQLE
SGLAAYASFS DRVGGLFFEV NAKLADLSSS TSVTRSASDS GKEEEATEHV AGEDLPSLAK
EVAQVESVRA YAETALKLDT LVGDIEDAVM SSLNKNLRTS RSSGFEEVRL HAIKTLKTTE
EILSSVAKRH PRWARLVSAV DHRVDRALAM MRPQAIADYR ALLSSLRWPP QLSTLTSASL
DSKSENVQNP LFNMEGSLKS QYCGSFHALC SLQGLQLQRK SRQLGIHKGE NVLFHQPLWA
IEELVNPLTV ASQRHFTKWS EKPEFIFALV YKITRDYVDS MDELLQPLVD EAKLAGYSCR
EEWVSAMVSS LSLYLVKEIF PIYVGQLDEA NETDLRSEAK VSWLHLIDLM ISFDKRVQSL
VSQSGILSLQ EDGNLLRISS LSVFCDRPDW LDLWAEIELD ERLVKFKEEI DNDRNWTAKV
QDELISSSNV YRPPIISSIF LQHLSSIIER SKSVPALYLR ARFLRLAASP TIHKFLDCLL
LRCQDADGLT ALTENNDLIK VSNSINAGHY IESVLEEWSE DVFFLEMGTG QHDPQEVPGL
ENFTEPSEGI FGEEFEKLEK FRLEWINKLS VVILRGFDAR IREYIKNRKQ WQEKKDKEWT
VSRALVGALD YLQGKTSIIE ENLNKADFTA MWRTLASEID KLFFNSILMA NVKFTNDGVE
RLKVDMEVLY GVFRTWCVRP EGFFPKLSEG LTLLKMEEKQ VKDGLSRGDK WLRENRIRYL
SEAEAKKVAK SRVFS
