MUB3_ARATH
ID MUB3_ARATH Reviewed; 118 AA.
AC Q9SW27; Q9ZRD4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Membrane-anchored ubiquitin-fold protein 3;
DE Short=AtMUB3;
DE Short=Membrane-anchored ub-fold protein 3;
DE AltName: Full=ATGP4;
DE Flags: Precursor;
GN Name=MUB3; OrderedLocusNames=At4g24990; ORFNames=F13M23.130;
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].
RA Biermann B.J., Price J.R., Crowell D.N., Randall S.K.;
RT "A collection of cDNAs encoding isoprenylated plant proteins.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, NOMENCLATURE, ISOPRENYLATION AT CYS-115, METHYLATION AT
RP CYS-115, MUTAGENESIS OF CYS-115, TISSUE SPECIFICITY, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16831869; DOI=10.1074/jbc.m602283200;
RA Downes B.P., Saracco S.A., Lee S.S., Crowell D.N., Vierstra R.D.;
RT "MUBS: a family of ubiquitin-fold proteins that are plasma membrane-
RT anchored by prenylation.";
RL J. Biol. Chem. 281:27145-27157(2006).
CC -!- FUNCTION: May serve as docking site to facilitate the association of
CC other proteins to the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16831869};
CC Lipid-anchor {ECO:0000269|PubMed:16831869}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, but three fold higher expression in
CC senescing leaves. {ECO:0000269|PubMed:16831869}.
CC -!- INDUCTION: Not induced by pathogens, cycloheximide and ozone treatment.
CC {ECO:0000269|PubMed:16831869}.
CC -!- MISCELLANEOUS: Heat stable and remains soluble at temperatures
CC exceeding 90 degrees Celsius.
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DR EMBL; U64921; AAD00115.1; -; mRNA.
DR EMBL; AL035523; CAB36741.1; -; Genomic_DNA.
DR EMBL; AL161562; CAB79408.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84989.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67200.1; -; Genomic_DNA.
DR EMBL; BT003091; AAO23656.1; -; mRNA.
DR EMBL; AK227315; BAE99330.1; -; mRNA.
DR PIR; T05520; T05520.
DR RefSeq; NP_001329044.1; NM_001341720.1.
DR RefSeq; NP_194229.1; NM_118631.3.
DR PDB; 4X57; X-ray; 2.80 A; B/D=1-118.
DR PDBsum; 4X57; -.
DR AlphaFoldDB; Q9SW27; -.
DR SMR; Q9SW27; -.
DR BioGRID; 13890; 9.
DR IntAct; Q9SW27; 2.
DR STRING; 3702.AT4G24990.1; -.
DR PaxDb; Q9SW27; -.
DR PRIDE; Q9SW27; -.
DR ProteomicsDB; 238657; -.
DR DNASU; 828602; -.
DR EnsemblPlants; AT4G24990.1; AT4G24990.1; AT4G24990.
DR EnsemblPlants; AT4G24990.2; AT4G24990.2; AT4G24990.
DR GeneID; 828602; -.
DR Gramene; AT4G24990.1; AT4G24990.1; AT4G24990.
DR Gramene; AT4G24990.2; AT4G24990.2; AT4G24990.
DR KEGG; ath:AT4G24990; -.
DR Araport; AT4G24990; -.
DR TAIR; locus:2117383; AT4G24990.
DR eggNOG; ENOG502RZEB; Eukaryota.
DR HOGENOM; CLU_136465_1_0_1; -.
DR InParanoid; Q9SW27; -.
DR OMA; TIAQCKT; -.
DR OrthoDB; 1555986at2759; -.
DR PhylomeDB; Q9SW27; -.
DR PRO; PR:Q9SW27; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SW27; baseline and differential.
DR Genevisible; Q9SW27; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR InterPro; IPR017000; MUB.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR040015; UBL3-like.
DR InterPro; IPR039540; UBL3-like_ubiquitin_dom.
DR PANTHER; PTHR13169; PTHR13169; 1.
DR Pfam; PF13881; Rad60-SLD_2; 1.
DR PIRSF; PIRSF032572; MUB; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Methylation; Palmitate;
KW Prenylation; Reference proteome.
FT CHAIN 1..115
FT /note="Membrane-anchored ubiquitin-fold protein 3"
FT /id="PRO_0000248165"
FT PROPEP 116..118
FT /note="Removed in mature form"
FT /id="PRO_0000248166"
FT DOMAIN 7..73
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOD_RES 115
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:16831869"
FT LIPID 113
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 115
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:16831869"
FT MUTAGEN 115
FT /note="C->S: Loss of prenylation and membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:16831869"
FT CONFLICT 59
FT /note="S -> T (in Ref. 1; AAD00115)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4X57"
FT TURN 76..81
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4X57"
SQ SEQUENCE 118 AA; 12836 MW; 57811616C7B2AB44 CRC64;
MPEEESIDIK FRLYDGSDIG PFRYSAASTV DFLKQRVVSD WPKGKTVVPK GINEVKLISS
GKILENNKTV GQCKTPFGDI AGGVIVMHVV VQPSLAKSKT EKKVDKAPKA VICTCTIL
