UBA5_BOVIN
ID UBA5_BOVIN Reviewed; 404 AA.
AC A7MAZ3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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 (By similarity). Ufmylation is essential for erythroid
CC differentiation of both megakaryocytes and erythrocytes (By
CC similarity). {ECO:0000250|UniProtKB:Q8VE47,
CC 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 UIS motif) with GABARAPL2 and,
CC with lower affinity, with GABARAP and GABARAPL1. Interacts (via C-
CC terminus) with UFC1. {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}. Note=Localizes mainly in the cytoplasm,
CC while it localizes to the nucleus in presence of SUMO2. Interaction
CC with GABARAPL2 promotes localization to the endoplasmic reticulum
CC membrane. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- DOMAIN: The UFM1-interacting sequence (UIS) motif mediates interaction
CC with both UFM1 and LC3/GABARAP proteins (GABARAP, GABARAPL1 and
CC GABARAPL2). {ECO:0000250|UniProtKB:Q9GZZ9}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
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DR EMBL; BC151254; AAI51255.1; -; mRNA.
DR RefSeq; NP_001094537.1; NM_001101067.2.
DR AlphaFoldDB; A7MAZ3; -.
DR SMR; A7MAZ3; -.
DR STRING; 9913.ENSBTAP00000005894; -.
DR PaxDb; A7MAZ3; -.
DR PeptideAtlas; A7MAZ3; -.
DR PRIDE; A7MAZ3; -.
DR Ensembl; ENSBTAT00000005894; ENSBTAP00000005894; ENSBTAG00000004495.
DR GeneID; 509292; -.
DR KEGG; bta:509292; -.
DR CTD; 79876; -.
DR VEuPathDB; HostDB:ENSBTAG00000004495; -.
DR VGNC; VGNC:36564; UBA5.
DR eggNOG; KOG2336; Eukaryota.
DR GeneTree; ENSGT00940000156177; -.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; A7MAZ3; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR TreeFam; TF314168; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000004495; Expressed in caput epididymis and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0050905; P:neuromuscular process; IEA:Ensembl.
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:0033146; P:regulation of intracellular estrogen receptor signaling pathway; 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; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..404
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391931"
FT MOTIF 334..346
FT /note="UFM1-interacting sequence (UIS)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
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 MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VE47"
SQ SEQUENCE 404 AA; 44697 MW; F1FD2BB9A5D1BC6B CRC64;
MAESVERLQQ RVEELERELA QERSRRALGS GDGGGGRARI EKMSSEVVDS NPYSRLMALK
RMGIVSDYEK IRTFTVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFEHF MNRISNGGLE EGKPVDLVLS
CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID
EKTLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
PQCDDRNCRK QQKEYKKKVA ALPKQEVIQE EGEIIHEDNE WGIELVSEIS EEELKKSSGP
IPDLPEGIIV AYTVPQKQED SVPEVTVEDS GESLEDLMAK MKNI
