UBA5_DROME
ID UBA5_DROME Reviewed; 404 AA.
AC Q9VYY3; B4F5S5; B4F5S6; B4F5S7; B4F5S8; B4F5S9; B4F5T0; B4F5T1; B4F5T3;
AC C0MLQ2; C0MLQ9; C0MLR0; Q8SYN2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000305};
DE Short=Ubiquitin-activating enzyme 5 {ECO:0000303|PubMed:26872069};
DE AltName: Full=UFM1-activating enzyme {ECO:0000305};
GN Name=Uba5 {ECO:0000303|PubMed:26872069, ECO:0000312|FlyBase:FBgn0030305};
GN ORFNames=CG1749 {ECO:0000312|FlyBase:FBgn0030305};
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 [GENOMIC DNA], AND VARIANTS SER-17; LEU-GLU-THR-GLU-22
RP INS; ASP-73; SER-163; GLN-169; ILE-309; ILE-309-310-ILE; SER-333; ARG-335
RP AND THR-385.
RC STRAIN=ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377,
RC ZBMEL384, ZBMEL398, ZBMEL84, and ZBMEL95;
RX PubMed=18477586; DOI=10.1093/molbev/msn111;
RA Baines J.F., Sawyer S.A., Hartl D.L., Parsch J.;
RT "Effects of X-linkage and sex-biased gene expression on the rate of
RT adaptive protein evolution in Drosophila.";
RL Mol. Biol. Evol. 25:1639-1650(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-73; LYS-325 AND
RP GLN-364.
RC STRAIN=MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17,
RC MEL18, MEL19, and MEL20;
RX PubMed=19126864; DOI=10.1093/molbev/msn297;
RA Parsch J., Zhang Z., Baines J.F.;
RT "The influence of demography and weak selection on the McDonald-Kreitman
RT test: an empirical study in Drosophila.";
RL Mol. Biol. Evol. 26:691-698(2009).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=26872069; DOI=10.1371/journal.pone.0149039;
RA Duan R., Shi Y., Yu L., Zhang G., Li J., Lin Y., Guo J., Wang J., Shen L.,
RA Jiang H., Wang G., Tang B.;
RT "UBA5 mutations cause a new form of autosomal recessive cerebellar
RT ataxia.";
RL PLoS ONE 11:E0149039-E0149039(2016).
CC -!- FUNCTION: E1-like enzyme which activates UFM1.
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SUBUNIT: Interacts (via C-terminus) with Ufc1. Interacts with Ufm1.
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown shows aberrant
CC neuromuscular junctions in the larval muscle and abnormal wings,
CC locomotive defects and a shortened lifespan in the adult fly. RNAi-
CC mediated knockdown in the nervous system results also in aberrant
CC neuromuscular junctions characterized by reduced number of type Ib
CC boutons and increased bouton size in the larval muscle.
CC {ECO:0000269|PubMed:26872069}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL49051.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM999161; CAQ53523.1; -; Genomic_DNA.
DR EMBL; AM999162; CAQ53524.1; -; Genomic_DNA.
DR EMBL; AM999163; CAQ53525.1; -; Genomic_DNA.
DR EMBL; AM999164; CAQ53526.1; -; Genomic_DNA.
DR EMBL; AM999165; CAQ53527.1; -; Genomic_DNA.
DR EMBL; AM999166; CAQ53528.1; -; Genomic_DNA.
DR EMBL; AM999167; CAQ53529.1; -; Genomic_DNA.
DR EMBL; AM999168; CAQ53530.1; -; Genomic_DNA.
DR EMBL; AM999169; CAQ53531.1; -; Genomic_DNA.
DR EMBL; AM999170; CAQ53532.1; -; Genomic_DNA.
DR EMBL; FM246273; CAR94199.1; -; Genomic_DNA.
DR EMBL; FM246274; CAR94200.1; -; Genomic_DNA.
DR EMBL; FM246275; CAR94201.1; -; Genomic_DNA.
DR EMBL; FM246276; CAR94202.1; -; Genomic_DNA.
DR EMBL; FM246277; CAR94203.1; -; Genomic_DNA.
DR EMBL; FM246278; CAR94204.1; -; Genomic_DNA.
DR EMBL; FM246279; CAR94205.1; -; Genomic_DNA.
DR EMBL; FM246280; CAR94206.1; -; Genomic_DNA.
DR EMBL; FM246281; CAR94207.1; -; Genomic_DNA.
DR EMBL; FM246282; CAR94208.1; -; Genomic_DNA.
DR EMBL; FM246283; CAR94209.1; -; Genomic_DNA.
DR EMBL; FM246284; CAR94210.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48050.1; -; Genomic_DNA.
DR EMBL; AY071429; AAL49051.1; ALT_FRAME; mRNA.
DR RefSeq; NP_572722.2; NM_132494.3.
DR AlphaFoldDB; Q9VYY3; -.
DR SMR; Q9VYY3; -.
DR BioGRID; 58505; 3.
DR IntAct; Q9VYY3; 2.
DR STRING; 7227.FBpp0073354; -.
DR PaxDb; Q9VYY3; -.
DR PRIDE; Q9VYY3; -.
DR DNASU; 32094; -.
DR EnsemblMetazoa; FBtr0073505; FBpp0073354; FBgn0030305.
DR GeneID; 32094; -.
DR KEGG; dme:Dmel_CG1749; -.
DR UCSC; CG1749-RA; d. melanogaster.
DR CTD; 79876; -.
DR FlyBase; FBgn0030305; Uba5.
DR VEuPathDB; VectorBase:FBgn0030305; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; Q9VYY3; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; Q9VYY3; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 32094; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 32094; -.
DR PRO; PR:Q9VYY3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030305; Expressed in spermathecum and 46 other tissues.
DR ExpressionAtlas; Q9VYY3; baseline and differential.
DR Genevisible; Q9VYY3; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0019008; C:molybdopterin synthase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; ISS:FlyBase.
DR GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; ISS:FlyBase.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Golgi apparatus; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..404
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391944"
FT REGION 372..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT VARIANT 17
FT /note="T -> S (in strain: ZBMEL157 and ZBMEL377)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 22
FT /note="E -> ELETE (in strain: ZBMEL186 and ZBMEL191)"
FT VARIANT 73
FT /note="Y -> D (in strain: MEL02, ZBMEL84, ZBMEL145,
FT ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384
FT and ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:18477586,
FT ECO:0000269|PubMed:19126864"
FT VARIANT 163
FT /note="T -> S (in strain: ZBMEL95)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 169
FT /note="R -> Q (in strain: ZBMEL229)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 309..310
FT /note="LV -> II (in strain: ZBMEL145, ZBMEL191)"
FT VARIANT 309
FT /note="L -> I (in strain: ZBMEL84, ZBMEL384 and ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 325
FT /note="E -> K (in strain: MEL18)"
FT /evidence="ECO:0000269|PubMed:19126864"
FT VARIANT 333
FT /note="P -> S (in strain: ZBMEL384)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 335
FT /note="H -> R (in strain: ZBMEL186)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 364
FT /note="E -> Q (in strain: MEL17)"
FT /evidence="ECO:0000269|PubMed:19126864"
FT VARIANT 385
FT /note="S -> T (in strain: ZBMEL186 and ZBMEL384)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT CONFLICT 177
FT /note="L -> M (in Ref. 5; AAL49051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 44167 MW; C9C2EFE14D18062F CRC64;
MSHAIDELQA IIADLKTELE TEPKSSGGVA SNSRLARDRI DRMSAEVVDS NPYSRLMALQ
RMNIVKDYER IRYKAVAIVG VGGVGSVTAD MLTRCGIGKL ILFDYDKVEL ANMNRLFFTP
DQAGLSKVAA AAATLSFINP DVEIETHNYN ITTVENFDRF LDTISQGGRI AGQPVDLVLS
CVDNFEARMA INAACNERNL NWFESGVSEN AVSGHIQFIR PGDTACFACA PPLVVAENID
EKTLKREGVC AASLPTTMGI TAGFLVQNAL KYLLNFGEVS DYLGYNALSD FFPKMTLKPN
PQCDDRNCLV RQKEFQARPK PVLIEEKAVS EEPLHATNEW GIELVAEDAP ESNTTPAETP
VMGEGLRLAY EAPEKSSETS EETVSAATAD ETSLEDLMAQ MKSM
