MUB5_ARATH
ID MUB5_ARATH Reviewed; 120 AA.
AC Q9SH14; Q8LB82;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Membrane-anchored ubiquitin-fold protein 5;
DE Short=AtMUB5;
DE Short=Membrane-anchored ub-fold protein 5;
DE Flags: Precursor;
GN Name=MUB5; OrderedLocusNames=At1g77870; ORFNames=F28K19.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION, NOMENCLATURE, ISOPRENYLATION AT CYS-117, METHYLATION AT
RP CYS-117, MUTAGENESIS OF CYS-117, 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. {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; AC009243; AAF17678.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36037.1; -; Genomic_DNA.
DR EMBL; AY087365; AAM64915.1; -; mRNA.
DR PIR; E96808; E96808.
DR RefSeq; NP_177910.1; NM_106436.5.
DR AlphaFoldDB; Q9SH14; -.
DR SMR; Q9SH14; -.
DR BioGRID; 29342; 4.
DR STRING; 3702.AT1G77870.1; -.
DR PaxDb; Q9SH14; -.
DR PRIDE; Q9SH14; -.
DR ProteomicsDB; 238455; -.
DR EnsemblPlants; AT1G77870.1; AT1G77870.1; AT1G77870.
DR GeneID; 844123; -.
DR Gramene; AT1G77870.1; AT1G77870.1; AT1G77870.
DR KEGG; ath:AT1G77870; -.
DR Araport; AT1G77870; -.
DR TAIR; locus:2029466; AT1G77870.
DR eggNOG; ENOG502S2V5; Eukaryota.
DR HOGENOM; CLU_136465_1_0_1; -.
DR InParanoid; Q9SH14; -.
DR OMA; HCVCCIL; -.
DR OrthoDB; 1555986at2759; -.
DR PhylomeDB; Q9SH14; -.
DR PRO; PR:Q9SH14; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SH14; baseline and differential.
DR Genevisible; Q9SH14; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane; Lipoprotein; Membrane; Methylation; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1..117
FT /note="Membrane-anchored ubiquitin-fold protein 5"
FT /id="PRO_0000248169"
FT PROPEP 118..120
FT /note="Removed in mature form"
FT /id="PRO_0000248170"
FT DOMAIN 7..72
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOD_RES 117
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:16831869"
FT LIPID 115
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 117
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:16831869"
FT MUTAGEN 117
FT /note="C->S: Loss of prenylation and membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:16831869"
FT CONFLICT 78
FT /note="T -> P (in Ref. 3; AAM64915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13487 MW; 590C5F7E927193B0 CRC64;
MGDEDLIELK FRLADGTDIG PSKYSQFMTV ASLKEKIIAQ WPKDKENAPK MINEVKLING
GKILENNKTL SEARSLITIG ELPGIVTTMH VVLRPPLFEK KKEKLQNDPP RKSHCVCCIL
