MEB1_ARATH
ID MEB1_ARATH Reviewed; 611 AA.
AC Q8W4P8; C0Z3G6; F4JJT0; Q9STP0;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Membrane protein of ER body 1;
GN Name=MEB1; OrderedLocusNames=At4g27860; ORFNames=T27E11.100;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP INTERACTION WITH NAI2.
RC STRAIN=cv. Columbia;
RX PubMed=23166355; DOI=10.1104/pp.112.207654;
RA Yamada K., Nagano A.J., Nishina M., Hara-Nishimura I., Nishimura M.;
RT "Identification of two novel endoplasmic reticulum body-specific integral
RT membrane proteins.";
RL Plant Physiol. 161:108-120(2013).
CC -!- FUNCTION: May sequester excess cytosolic iron and manganese into
CC endoplasmic reticulum to reduce metal ion toxicity. Not essential for
CC the accumulation of ER body components, including PYK10.
CC {ECO:0000269|PubMed:23166355}.
CC -!- SUBUNIT: Interacts directly or indirectly with NAI2.
CC {ECO:0000269|PubMed:23166355}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23166355}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23166355}. Note=Located in ER bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8W4P8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W4P8-2; Sequence=VSP_056761;
CC Name=3;
CC IsoId=Q8W4P8-3; Sequence=VSP_056760, VSP_056761;
CC -!- INDUCTION: Induced by NAI1. {ECO:0000269|PubMed:23166355}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on pathogen
CC sensitivity. {ECO:0000269|PubMed:23166355}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention in
CC isoform 2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CCC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43974.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81435.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL078579; CAB43974.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81435.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85401.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85402.1; -; Genomic_DNA.
DR EMBL; AY062118; AAL32990.1; -; mRNA.
DR EMBL; BT010175; AAQ22644.1; -; mRNA.
DR EMBL; AK319130; BAH57245.1; -; mRNA.
DR PIR; T09025; T09025.
DR RefSeq; NP_001190855.1; NM_001203926.1. [Q8W4P8-2]
DR RefSeq; NP_567788.1; NM_118924.2. [Q8W4P8-1]
DR AlphaFoldDB; Q8W4P8; -.
DR BioGRID; 14186; 3.
DR STRING; 3702.AT4G27860.1; -.
DR iPTMnet; Q8W4P8; -.
DR PaxDb; Q8W4P8; -.
DR PRIDE; Q8W4P8; -.
DR ProteomicsDB; 239050; -. [Q8W4P8-1]
DR EnsemblPlants; AT4G27860.1; AT4G27860.1; AT4G27860. [Q8W4P8-1]
DR EnsemblPlants; AT4G27860.2; AT4G27860.2; AT4G27860. [Q8W4P8-2]
DR GeneID; 828899; -.
DR Gramene; AT4G27860.1; AT4G27860.1; AT4G27860. [Q8W4P8-1]
DR Gramene; AT4G27860.2; AT4G27860.2; AT4G27860. [Q8W4P8-2]
DR KEGG; ath:AT4G27860; -.
DR Araport; AT4G27860; -.
DR TAIR; locus:2137375; AT4G27860.
DR eggNOG; ENOG502QQ85; Eukaryota.
DR InParanoid; Q8W4P8; -.
DR OMA; HEQGSES; -.
DR PRO; PR:Q8W4P8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W4P8; baseline and differential.
DR Genevisible; Q8W4P8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010168; C:ER body; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR InterPro; IPR008217; Ccc1_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR31851; PTHR31851; 2.
DR SUPFAM; SSF50353; SSF50353; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..611
FT /note="Membrane protein of ER body 1"
FT /id="PRO_0000430467"
FT TRANSMEM 209..229
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_056760"
FT VAR_SEQ 313..327
FT /note="Missing (in isoform 3 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_056761"
SQ SEQUENCE 611 AA; 68170 MW; 7E154E953D9DCFCD CRC64;
MDPTMNPTPT PSSAGNSVCT DELTNLPPED SPLDSEKDDS VDFSQEQGSE SNEAIDTENG
SRSVDKNQYS ETEVVVRAKD LQTEPDSLDD DVEIVIKNQH KYYIYCPCCG EDITKTVKLV
KISDPKHTKD HDKAVDSDTE NGSKSKDKNT KVPSWFSDFI QPLFSSEDRG KKGVVDSELL
GTYEDLGIIG EEPSIDVSNE KDRPSFPKWY LDVFAWLFLC IIIALSVLST SPPPFIQPHL
QLPSMPTLRM PSASVLLLLP TSAVLLLFII SMRSRFTPRY HKEKGEVVPK STDSKSHDDQ
AANTDQDFDK KTDNKRNRLT PIYPSSLEKP SKQTVNKETQ NHDKEAADPD QDVDKETENQ
KSHLTPIYPS PLEQPSKQII NKETQTEPML PPNAQSEIPN SVEPRKGGNK VEILKSIVYG
GLTESITSLC TVTSAAASGA STLNVLALGV ANLSSGLLLT VHSLQELINE KPRKQTNTDD
SPEEGEGEED RYEEVLGRRE YSRIHRVIAI SSFVIFGLIP PLVYGFSFRK KMEKRQEYKV
LAVYAVSLLC IVLLSIAKAY VSKKRDYVKT LFRYTTTATT ASGFSQFVGY LVSQWLEKSG
FYDDSPETQR V
