UFM1_DROME
ID UFM1_DROME Reviewed; 87 AA.
AC A8DYH2; C9QNX3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000312|FlyBase:FBgn0085220};
DE Flags: Precursor;
GN Name=Ufm1 {ECO:0000312|FlyBase:FBgn0085220};
GN ORFNames=CG34191 {ECO:0000312|FlyBase:FBgn0085220};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND 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: Ubiquitin-like modifier which can be covalently attached via
CC an isopeptide bond to substrate proteins as a monomer or a lysine-
CC linked polymer (By similarity). The so-called ufmylation, requires the
CC UFM1-activating E1 enzyme Uba5, the UFM1-conjugating E2 enzyme Ufc1,
CC and the UFM1-ligase E3 enzyme Ufl1 (By similarity). This post-
CC translational modification on lysine residues of proteins may play a
CC crucial role in a number of cellular processes (By similarity). The
CC Ufm1 cascade might play a role in the development of the neuromuscular
CC junctions (PubMed:26872069). {ECO:0000250|UniProtKB:P61960,
CC ECO:0000269|PubMed:26872069}.
CC -!- SUBUNIT: Interacts with Uba5. {ECO:0000250|UniProtKB:P61960}.
CC -!- INTERACTION:
CC A8DYH2; Q4V6M7: UFSP1; NbExp=4; IntAct=EBI-15116417, EBI-15116415;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61960}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61960}.
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. RNAi-mediated
CC knockdown in the nervous system results also in aberrant neuromuscular
CC junctions characterized by reduced number of type Ib boutons and
CC increased bouton size in the larval muscle.
CC {ECO:0000269|PubMed:26872069}.
CC -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACX30017.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013599; ABV53832.1; -; Genomic_DNA.
DR EMBL; BT099855; ACX30017.1; ALT_INIT; mRNA.
DR EMBL; BT100274; ACY72393.1; -; mRNA.
DR RefSeq; NP_001097354.1; NM_001103884.4.
DR RefSeq; NP_001286507.1; NM_001299578.1.
DR AlphaFoldDB; A8DYH2; -.
DR SMR; A8DYH2; -.
DR BioGRID; 625346; 1.
DR IntAct; A8DYH2; 3.
DR STRING; 7227.FBpp0111299; -.
DR PaxDb; A8DYH2; -.
DR PRIDE; A8DYH2; -.
DR DNASU; 5740715; -.
DR EnsemblMetazoa; FBtr0112384; FBpp0111299; FBgn0085220.
DR EnsemblMetazoa; FBtr0340071; FBpp0309077; FBgn0085220.
DR GeneID; 5740715; -.
DR KEGG; dme:Dmel_CG34191; -.
DR UCSC; CG34191-RA; d. melanogaster.
DR CTD; 51569; -.
DR FlyBase; FBgn0085220; Ufm1.
DR VEuPathDB; VectorBase:FBgn0085220; -.
DR eggNOG; KOG3483; Eukaryota.
DR GeneTree; ENSGT00390000010391; -.
DR HOGENOM; CLU_175114_0_0_1; -.
DR InParanoid; A8DYH2; -.
DR OMA; INPAQNA; -.
DR OrthoDB; 1575050at2759; -.
DR PhylomeDB; A8DYH2; -.
DR BioGRID-ORCS; 5740715; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 5740715; -.
DR PRO; PR:A8DYH2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0085220; Expressed in saliva-secreting gland and 13 other tissues.
DR ExpressionAtlas; A8DYH2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:FlyBase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR005375; UFM1.
DR PANTHER; PTHR15825; PTHR15825; 1.
DR Pfam; PF03671; Ufm1; 1.
DR PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..83
FT /note="Ubiquitin-fold modifier 1"
FT /id="PRO_0000392003"
FT PROPEP 84..87
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT /id="PRO_0000392004"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1)"
FT /evidence="ECO:0000250|UniProtKB:P61960"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 87 AA; 9438 MW; 30F1746229E71C55 CRC64;
MSKVTFKITL TSDPKLPFKV LSVPEGTPFT AVLKFASEEF KVPAETSAII TDDGIGISPQ
QTAGNVFLKH GSELRLIPRD RVGHQLS
