UBA3_DANRE
ID UBA3_DANRE Reviewed; 462 AA.
AC Q7ZVX6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit;
DE EC=6.2.1.64;
DE AltName: Full=NEDD8-activating enzyme E1C;
DE AltName: Full=Ubiquitin-activating enzyme E1C;
DE AltName: Full=Ubiquitin-like modifier-activating enzyme 3;
DE Short=Ubiquitin-activating enzyme 3;
GN Name=uba3; Synonyms=ube1c; ORFNames=zgc:55528;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the dimeric uba3-nae1 E1 enzyme. E1
CC activates nedd8 by first adenylating its C-terminal glycine residue
CC with ATP, thereafter linking this residue to the side chain of the
CC catalytic cysteine, yielding a nedd8-uba3 thioester and free AMP. E1
CC finally transfers nedd8 to the catalytic cysteine of ube2m (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Heterodimer of uba3 and nae1. Interacts with nedd8, ube2f and
CC ube2m (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Arg-210 acts as a selectivity gate, preventing
CC misactivation of ubiquitin by this NEDD8-specific E1 complex.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000305}.
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DR EMBL; BC045372; AAH45372.1; -; mRNA.
DR RefSeq; NP_998632.1; NM_213467.1.
DR AlphaFoldDB; Q7ZVX6; -.
DR SMR; Q7ZVX6; -.
DR STRING; 7955.ENSDARP00000075198; -.
DR PaxDb; Q7ZVX6; -.
DR Ensembl; ENSDART00000080752; ENSDARP00000075198; ENSDARG00000057987.
DR GeneID; 406776; -.
DR KEGG; dre:406776; -.
DR CTD; 9039; -.
DR ZFIN; ZDB-GENE-040426-2825; uba3.
DR eggNOG; KOG2015; Eukaryota.
DR GeneTree; ENSGT00550000074831; -.
DR HOGENOM; CLU_013325_13_1_1; -.
DR InParanoid; Q7ZVX6; -.
DR OMA; CGGSCEW; -.
DR OrthoDB; 686413at2759; -.
DR PhylomeDB; Q7ZVX6; -.
DR TreeFam; TF300499; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q7ZVX6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000057987; Expressed in cleaving embryo and 29 other tissues.
DR ExpressionAtlas; Q7ZVX6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR Gene3D; 1.10.10.520; -; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030468; Uba3.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF6; PTHR10953:SF6; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..462
FT /note="NEDD8-activating enzyme E1 catalytic subunit"
FT /id="PRO_0000194945"
FT REGION 52..69
FT /note="Interaction with ube2m N-terminus"
FT /evidence="ECO:0000250"
FT REGION 156..160
FT /note="Interaction with ube2m N-terminus"
FT /evidence="ECO:0000250"
FT REGION 191..216
FT /note="Interaction with ube2m N-terminus"
FT /evidence="ECO:0000250"
FT REGION 226..228
FT /note="Interaction with nedd8"
FT /evidence="ECO:0000250"
FT REGION 241..247
FT /note="Interaction with nae1"
FT /evidence="ECO:0000250"
FT REGION 291..294
FT /note="Interaction with nae1"
FT /evidence="ECO:0000250"
FT REGION 330..337
FT /note="Interaction with ube2m N-terminus"
FT /evidence="ECO:0000250"
FT REGION 351..356
FT /note="Interaction with nedd8"
FT /evidence="ECO:0000250"
FT REGION 367..462
FT /note="Interaction with ube2m core domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 99..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 147..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Determines specificity for nedd8"
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 51663 MW; B51202589DBF6543 CRC64;
MAEGEEPEKK RRRIEELNEK MVVDGGSGDR SEWQGRWDHV RKFLERTGPF THPDFEASTE
SLQFLLDTCK ILVIGAGGLG CELLKDLALS GFRHIHVVDM DTIDVSNLNR QFLFRPKDVG
RPKAEVAADF VNDRVPGCSV VPHFKKIQDL DETFYRQFHI VVCGLDSVIA RRWMNGMLLS
LLIYEDGVLD PSSIIPLIDG GTEGFKGNAR VILPGMTACI DCTLELYPPQ INFPMCTIAS
MPRLPEHCVE YVRMLLWPKE KPFGDGVVLD GDDPKHIQWV YQKSLERAAE FNITGVTYRL
TQGVVKRIIP AVASTNAVIA AACATEVFKI ATSAYVPLNN YLVFNDVDGL YTYTFEAERK
ENCSACSQVP QDMQFTPSAK LQEVLDYLTE NASLQMKSPA ITTTLDGKNK TLYLQTVASI
EERTRPNLSK TLKELGLVDG QELAVADVTT PQTVLFKLKF IS
