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Database: UniProt
Entry: MUB2_ARATH
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Original site: MUB2_ARATH 
ID   MUB2_ARATH              Reviewed;         124 AA.
AC   Q8LCS8; Q9LF36;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   RecName: Full=Membrane-anchored ubiquitin-fold protein 2;
DE            Short=AtMUB2;
DE            Short=Membrane-anchored ub-fold protein 2;
DE   AltName: Full=NTGP5;
GN   Name=MUB2; OrderedLocusNames=At5g15460; ORFNames=T20K14.70;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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   [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, PALMITOYLATION AT CYS-115;
RP   CYS-117; CYS-119 AND CYS-124, MUTAGENESIS OF CYS-115; CYS-117; CYS-119;
RP   CYS-124 AND 115-CYS--CYS-124, 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       stamens. {ECO:0000269|PubMed:16831869}.
CC   -!- INDUCTION: Not induced by pathogens, cycloheximide and ozone treatment.
CC       {ECO:0000269|PubMed:16831869}.
CC   -!- PTM: Acylated protein. Probably modified with palmitate
CC       (PubMed:16831869). {ECO:0000269|PubMed:16831869}.
CC   -!- MISCELLANEOUS: Heat stable and remains soluble at temperatures
CC       exceeding 90 degrees Celsius.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01745.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL391143; CAC01745.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92163.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92164.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69826.1; -; Genomic_DNA.
DR   EMBL; BT006108; AAP04093.1; -; mRNA.
DR   EMBL; BT005773; AAO64177.1; -; mRNA.
DR   EMBL; AY086424; AAM63426.1; -; mRNA.
DR   EMBL; AK228599; BAF00514.1; -; mRNA.
DR   PIR; T51524; T51524.
DR   RefSeq; NP_001318568.1; NM_001343401.1.
DR   RefSeq; NP_568315.1; NM_121550.3.
DR   RefSeq; NP_850824.1; NM_180493.4.
DR   AlphaFoldDB; Q8LCS8; -.
DR   SMR; Q8LCS8; -.
DR   BioGRID; 16675; 4.
DR   STRING; 3702.Q8LCS8; -.
DR   PaxDb; 3702-AT5G15460-2; -.
DR   ProteomicsDB; 250741; -.
DR   EnsemblPlants; AT5G15460.1; AT5G15460.1; AT5G15460.
DR   EnsemblPlants; AT5G15460.2; AT5G15460.2; AT5G15460.
DR   EnsemblPlants; AT5G15460.4; AT5G15460.4; AT5G15460.
DR   GeneID; 831399; -.
DR   Gramene; AT5G15460.1; AT5G15460.1; AT5G15460.
DR   Gramene; AT5G15460.2; AT5G15460.2; AT5G15460.
DR   Gramene; AT5G15460.4; AT5G15460.4; AT5G15460.
DR   KEGG; ath:AT5G15460; -.
DR   Araport; AT5G15460; -.
DR   TAIR; AT5G15460; MUB2.
DR   eggNOG; ENOG502RZYK; Eukaryota.
DR   HOGENOM; CLU_136465_1_0_1; -.
DR   InParanoid; Q8LCS8; -.
DR   OMA; CRSPICD; -.
DR   OrthoDB; 312659at2759; -.
DR   PhylomeDB; Q8LCS8; -.
DR   PRO; PR:Q8LCS8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LCS8; baseline and differential.
DR   Genevisible; Q8LCS8; AT.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd01814; Ubl_MUBs_plant; 1.
DR   InterPro; IPR017000; MUB.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR040015; UBL3-like.
DR   InterPro; IPR039540; UBL3-like_ubiquitin_dom.
DR   PANTHER; PTHR13169:SF26; MEMBRANE-ANCHORED UBIQUITIN-FOLD PROTEIN 2; 1.
DR   PANTHER; PTHR13169; UBIQUITIN-LIKE PROTEIN 3 HCG-1 PROTEIN; 1.
DR   Pfam; PF13881; Rad60-SLD_2; 1.
DR   PIRSF; PIRSF032572; MUB; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome.
FT   CHAIN           1..124
FT                   /note="Membrane-anchored ubiquitin-fold protein 2"
FT                   /id="PRO_0000248164"
FT   DOMAIN          8..74
FT                   /note="Ubiquitin-like"
FT   LIPID           115
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           117
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           119
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:16831869"
FT   LIPID           124
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:16831869"
FT   MUTAGEN         115..124
FT                   /note="CVCLCFGARC->SVSLSFGARS: Loss of membrane
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:16831869"
FT   MUTAGEN         115
FT                   /note="C->S: No effect on localization."
FT                   /evidence="ECO:0000269|PubMed:16831869"
FT   MUTAGEN         117
FT                   /note="C->S: No effect on localization."
FT                   /evidence="ECO:0000269|PubMed:16831869"
FT   MUTAGEN         119
FT                   /note="C->S: Loss of membrane localization."
FT                   /evidence="ECO:0000269|PubMed:16831869"
FT   MUTAGEN         124
FT                   /note="C->S: Loss of membrane localization."
FT                   /evidence="ECO:0000269|PubMed:16831869"
SQ   SEQUENCE   124 AA;  13709 MW;  F8F27BE021537DC2 CRC64;
     MAEVKDQLEI KFRLNDGSDI GPKLFPDATT VATLKETVVA QWPRDKENGP KTVKDVKLIS
     AGRILENNKT VGDCRSPVGN FSGAVTTMHV IIQHQVTEKE KKKKKPKGDL KQNKCVCLCF
     GARC
//
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