URM1_DROME
ID URM1_DROME Reviewed; 101 AA.
AC Q7KU86; A8E6X7; C1C595;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ubiquitin-related modifier 1 homolog {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=Urm1 {ECO:0000303|PubMed:26715182, ECO:0000312|FlyBase:FBgn0053276};
GN ORFNames=CG33276 {ECO:0000312|FlyBase:FBgn0053276};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:ABV82301.1, ECO:0000312|EMBL:ACO72861.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABV82301.1, ECO:0000312|EMBL:ACO72861.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 100-GLY-GLY-101.
RX PubMed=26715182; DOI=10.1007/s00018-015-2121-x;
RA Khoshnood B., Dacklin I., Grabbe C.;
RT "Urm1: an essential regulator of JNK signaling and oxidative stress in
RT Drosophila melanogaster.";
RL Cell. Mol. Life Sci. 73:1939-1954(2016).
RN [5]
RP FUNCTION, AND INTERACTION WITH CER.
RX PubMed=28953965; DOI=10.1371/journal.pone.0185611;
RA Khoshnood B., Dacklin I., Grabbe C.;
RT "A proteomics approach to identify targets of the ubiquitin-like molecule
RT Urm1 in Drosophila melanogaster.";
RL PLoS ONE 12:E0185611-E0185611(2017).
CC -!- FUNCTION: Acts as a sulfur carrier required for 2-thiolation of
CC mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu)
CC and tRNA(Gln) (By similarity). Serves as sulfur donor in tRNA 2-
CC thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus
CC by MOCS3 (By similarity). The sulfur is then transferred to tRNA to
CC form 2-thiolation of mcm(5)S(2)U (By similarity). Also acts as a
CC ubiquitin-like protein (UBL) that is covalently conjugated via an
CC isopeptide bond to lysine residues of target proteins such as Jafrac1,
CC Ciao1, Eip71CD and GILT1 (PubMed:26715182, PubMed:28953965). The
CC thiocarboxylated form serves as substrate for conjugation and oxidative
CC stress specifically induces the formation of UBL-protein conjugates (By
CC similarity). Plays a role in the regulation of JNK signaling in
CC response to oxidative stress (PubMed:26715182). {ECO:0000255|HAMAP-
CC Rule:MF_03048, ECO:0000269|PubMed:26715182,
CC ECO:0000269|PubMed:28953965}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- SUBUNIT: Interacts with cer. {ECO:0000269|PubMed:28953965}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048,
CC ECO:0000269|PubMed:26715182}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during all embryonic
CC stages, third instar larval imaginal disk, early pupal stages and in
CC the adult (at protein level). {ECO:0000269|PubMed:26715182}.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) via the hesA/moeB/thiF part of the MOCS3 homolog,
CC then thiocarboxylated (-COSH) via the rhodanese domain of the MOCS3
CC homolog. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- DISRUPTION PHENOTYPE: Lethal; most flies die by the pupal stages
CC (PubMed:26715182). Escapers are small, less active, display a
CC significantly reduced fecundity, shortened lifespan, increased
CC resistance to oxidative stress, up-regulation of the JNK signaling
CC pathway and increased expression of Jafrac1 and GstD1
CC (PubMed:26715182). Simultaneous knockout of Jafrac1 restores normal
CC sensitivity to oxidative stress (PubMed:26715182). RNAi-mediated
CC knockdown leads to higher tolerance to oxidative stress
CC (PubMed:26715182). {ECO:0000269|PubMed:26715182}.
CC -!- SIMILARITY: Belongs to the URM1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03048}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACO72861.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAS65063.2; -; Genomic_DNA.
DR EMBL; BT030919; ABV82301.1; -; mRNA.
DR EMBL; BT082024; ACO72861.1; ALT_INIT; mRNA.
DR RefSeq; NP_996018.2; NM_206296.3.
DR AlphaFoldDB; Q7KU86; -.
DR SMR; Q7KU86; -.
DR BioGRID; 77798; 4.
DR IntAct; Q7KU86; 4.
DR STRING; 7227.FBpp0113022; -.
DR PaxDb; Q7KU86; -.
DR DNASU; 2768949; -.
DR EnsemblMetazoa; FBtr0114530; FBpp0113022; FBgn0053276.
DR GeneID; 2768949; -.
DR KEGG; dme:Dmel_CG33276; -.
DR UCSC; CG33276-RB; d. melanogaster.
DR CTD; 81605; -.
DR FlyBase; FBgn0053276; Urm1.
DR VEuPathDB; VectorBase:FBgn0053276; -.
DR eggNOG; KOG4146; Eukaryota.
DR GeneTree; ENSGT00390000005101; -.
DR HOGENOM; CLU_148208_0_1_1; -.
DR InParanoid; Q7KU86; -.
DR OMA; DYELQPN; -.
DR OrthoDB; 1541629at2759; -.
DR PhylomeDB; Q7KU86; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 2768949; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 2768949; -.
DR PRO; PR:Q7KU86; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0053276; Expressed in wing disc and 24 other tissues.
DR ExpressionAtlas; Q7KU86; baseline and differential.
DR Genevisible; Q7KU86; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR CDD; cd01764; Ubl_Urm1; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03048; Urm1; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR015221; Urm1.
DR PANTHER; PTHR14986; PTHR14986; 1.
DR Pfam; PF09138; Urm1; 1.
DR PIRSF; PIRSF037379; Ubiquitin-related_modifier_1; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Reference proteome; tRNA processing;
KW Ubl conjugation pathway.
FT CHAIN 1..101
FT /note="Ubiquitin-related modifier 1 homolog"
FT /id="PRO_0000367858"
FT MOD_RES 101
FT /note="1-thioglycine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT MUTAGEN 100..101
FT /note="Missing: Loss of conjugation of target proteins
FT results in loss of urmylation and response to oxidative
FT stress."
FT /evidence="ECO:0000269|PubMed:26715182"
SQ SEQUENCE 101 AA; 11486 MW; C272BE2413E5050F CRC64;
MGTPELKIIL EFSAGAELLF GNIKRRELNL DGKQKWTIAN LLKWMHANIL TERPELFLQG
DTVRPGILVL INDTDWELLG ELDYELQPND NVLFISTLHG G
