MUB1_ARATH
ID MUB1_ARATH Reviewed; 117 AA.
AC Q9MAB9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Membrane-anchored ubiquitin-fold protein 1;
DE Short=AtMUB1;
DE Short=Membrane-anchored ub-fold protein 1;
DE Flags: Precursor;
GN Name=MUB1; OrderedLocusNames=At3g01050; ORFNames=T4P13.27;
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION, NOMENCLATURE, ISOPRENYLATION AT CYS-114, METHYLATION AT
RP CYS-114, MUTAGENESIS OF CYS-114, AND 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).
RN [5]
RP STRUCTURE BY NMR OF 2-117.
RX PubMed=15782178; DOI=10.1038/nmeth716;
RA Vinarov D.A., Lytle B.L., Peterson F.C., Tyler E.M., Volkman B.F.,
RA Markley J.L.;
RT "Cell-free protein production and labeling protocol for NMR-based
RT structural proteomics.";
RL Nat. Methods 1:149-153(2004).
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 -!- MISCELLANEOUS: Heat stable and remains soluble at temperatures
CC exceeding 90 degrees Celsius.
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DR EMBL; AC008261; AAF26169.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73600.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65143.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65144.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65145.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65146.1; -; Genomic_DNA.
DR EMBL; BT010661; AAR20718.1; -; mRNA.
DR EMBL; BT012419; AAS92335.1; -; mRNA.
DR RefSeq; NP_001319438.1; NM_001337306.1.
DR RefSeq; NP_001327137.1; NM_001337308.1.
DR RefSeq; NP_001327138.1; NM_001337307.1.
DR RefSeq; NP_001327139.1; NM_001337309.1.
DR RefSeq; NP_186754.1; NM_110970.2.
DR PDB; 1SE9; NMR; -; A=2-117.
DR PDBsum; 1SE9; -.
DR AlphaFoldDB; Q9MAB9; -.
DR BMRB; Q9MAB9; -.
DR SMR; Q9MAB9; -.
DR BioGRID; 6640; 7.
DR IntAct; Q9MAB9; 2.
DR STRING; 3702.AT3G01050.1; -.
DR PaxDb; Q9MAB9; -.
DR PRIDE; Q9MAB9; -.
DR ProteomicsDB; 238655; -.
DR EnsemblPlants; AT3G01050.1; AT3G01050.1; AT3G01050.
DR EnsemblPlants; AT3G01050.2; AT3G01050.2; AT3G01050.
DR EnsemblPlants; AT3G01050.3; AT3G01050.3; AT3G01050.
DR EnsemblPlants; AT3G01050.4; AT3G01050.4; AT3G01050.
DR EnsemblPlants; AT3G01050.5; AT3G01050.5; AT3G01050.
DR GeneID; 821307; -.
DR Gramene; AT3G01050.1; AT3G01050.1; AT3G01050.
DR Gramene; AT3G01050.2; AT3G01050.2; AT3G01050.
DR Gramene; AT3G01050.3; AT3G01050.3; AT3G01050.
DR Gramene; AT3G01050.4; AT3G01050.4; AT3G01050.
DR Gramene; AT3G01050.5; AT3G01050.5; AT3G01050.
DR KEGG; ath:AT3G01050; -.
DR Araport; AT3G01050; -.
DR TAIR; locus:2102172; AT3G01050.
DR eggNOG; ENOG502RZYK; Eukaryota.
DR HOGENOM; CLU_136465_1_0_1; -.
DR InParanoid; Q9MAB9; -.
DR OMA; DIGPIAF; -.
DR OrthoDB; 1555986at2759; -.
DR PhylomeDB; Q9MAB9; -.
DR EvolutionaryTrace; Q9MAB9; -.
DR PRO; PR:Q9MAB9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MAB9; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR DisProt; DP02643; -.
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..114
FT /note="Membrane-anchored ubiquitin-fold protein 1"
FT /id="PRO_0000114927"
FT PROPEP 115..117
FT /note="Removed in mature form"
FT /id="PRO_0000248163"
FT DOMAIN 8..74
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOD_RES 114
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:16831869"
FT LIPID 112
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 114
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:16831869"
FT MUTAGEN 114
FT /note="C->S: Loss of prenylation and membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:16831869"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1SE9"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:1SE9"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:1SE9"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1SE9"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1SE9"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1SE9"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1SE9"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1SE9"
SQ SEQUENCE 117 AA; 12821 MW; F2D0AC4441A3211F CRC64;
MAEVHNQLEI KFRLTDGSDI GPKAFPDATT VSALKETVIS EWPREKENGP KTVKEVKLIS
AGKVLENSKT VKDYRSPVSN LAGAVTTMHV IIQAPVTEKE KKPKGDPKMN KCVCSVM
