UBA5_XENTR
ID UBA5_XENTR Reviewed; 399 AA.
AC Q6GLG7;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000305};
DE Short=Ubiquitin-activating enzyme 5 {ECO:0000250|UniProtKB:Q9GZZ9};
DE AltName: Full=UFM1-activating enzyme {ECO:0000305};
GN Name=uba5 {ECO:0000250|UniProtKB:Q9GZZ9};
GN ORFNames=TNeu098a04.1 {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1-like enzyme which specifically catalyzes the first step in
CC ufmylation. Activates ufm1 by first adenylating its C-terminal glycine
CC residue with ATP, and thereafter linking this residue to the side chain
CC of a cysteine residue in E1, yielding a ufm1-E1 thioester and free AMP.
CC Activates ufm1 via a trans-binding mechanism, in which ufm1 interacts
CC with distinct sites in both subunits of the uba5 homodimer. Trans-
CC binding also promotes stabilization of the uba5 homodimer, and enhances
CC ATP-binding. Transfer of ufm1 from uba5 to the E2-like enzyme UFC1 also
CC takes place using a trans mechanism. Ufmylation is involved in
CC reticulophagy (also called ER-phagy) induced in response to endoplasmic
CC reticulum stress. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for ufm1 activation.
CC Interacts (via UIS motif) with ufm1; binds ufm1 via a trans-binding
CC mechanism in which ufm1 interacts with distinct sites in both subunits
CC of the uba5 homodimer. Interacts (via C-terminus) with ufc1.
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9GZZ9}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
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DR EMBL; CR760171; CAJ82881.1; -; mRNA.
DR EMBL; BC074525; AAH74525.1; -; mRNA.
DR RefSeq; NP_001004790.1; NM_001004790.1.
DR AlphaFoldDB; Q6GLG7; -.
DR SMR; Q6GLG7; -.
DR STRING; 8364.ENSXETP00000054036; -.
DR PaxDb; Q6GLG7; -.
DR DNASU; 448010; -.
DR Ensembl; ENSXETT00000054036; ENSXETP00000054036; ENSXETG00000025266.
DR GeneID; 448010; -.
DR KEGG; xtr:448010; -.
DR CTD; 79876; -.
DR Xenbase; XB-GENE-955661; uba5.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; Q6GLG7; -.
DR OMA; CPTKEGS; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; Q6GLG7; -.
DR TreeFam; TF314168; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025266; Expressed in neurula embryo and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030219; P:megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; ISS:UniProtKB.
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; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..399
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391934"
FT MOTIF 331..343
FT /note="UFM1-interacting sequence (UIS)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT ACT_SITE 246
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
SQ SEQUENCE 399 AA; 44463 MW; 14DE1F439061102E CRC64;
MEKLIEELRS RVSELEEELH RVRNGEQVHE GHRAKINTMS AEVVDSNPYS RLMALKRMGI
VEDYEKIRTF TVAVVGVGGV GSVTAEMLTR CGIGKLLLFD YDKVEMANMN RLFFQPHQAG
LSKVEAAEHT LRNINPDVQF EVHNYNITTL DNFQHFMDRI SKGGLKEGTP VDLVLSCVDN
FEARMAINTA CNELVQIWME SGVSENAVSG HIQLIKPGET ACFACAPPLV VAANIDEKTL
KREGVCAASL PTTMGVVAGM LVQNVLKYLL NFGTVSFYLG YNAMQDFFPT MAMKPNPQCG
DKYCRKQQEE FKLKEAARPK QEPIVVKEEE IVHEDNDWGI ELVSEVSEEE LKAASGPVPE
LPEGIKVAYT VPITEPTSGF IVEDSEQSLD ELMAQMKNL
