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Database: UniProt
Entry: I3N744_ICTTR
LinkDB: I3N744_ICTTR
Original site: I3N744_ICTTR 
ID   I3N744_ICTTR            Unreviewed;       538 AA.
AC   I3N744;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|ARBA:ARBA00015407, ECO:0000256|PIRNR:PIRNR039099};
GN   Name=NAE1 {ECO:0000313|Ensembl:ENSSTOP00000020190.2};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000020190.2, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000020190.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Regulatory 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.
CC       {ECO:0000256|PIRNR:PIRNR039099}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC       {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|PIRNR:PIRNR039099}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006868,
CC       ECO:0000256|PIRNR:PIRNR039099}.
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DR   EMBL; AGTP01009760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3N744; -.
DR   STRING; 43179.ENSSTOP00000020190; -.
DR   Ensembl; ENSSTOT00000027900.2; ENSSTOP00000020190.2; ENSSTOG00000029230.2.
DR   GeneTree; ENSGT00550000074901; -.
DR   HOGENOM; CLU_019618_2_1_1; -.
DR   InParanoid; I3N744; -.
DR   TreeFam; TF313972; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
DR   CDD; cd01493; APPBP1_RUB; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR030667; APP-BP1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PIRSF; PIRSF039099; APP-BP1; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT   DOMAIN          13..534
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   538 AA;  60776 MW;  7B893BB4AAE1297F CRC64;
     MAQPGKLLKE QKYDRQLRLW GDHGQEALES AHVCLIHATA TGTEILKNLV LPGIGSFTIV
     DGNQVSGEDA GNKYVLFFSN ICMLGKGNRA EAAMEFLQEL NNDVSGSFVE ESPENLLDND
     PSFFCRFTVV VATQLHESTL LRLADVLWNS EIPLLICRTY GLVGYMRIII KEHPVIESHP
     DNALEDLRLD KPFPELREHF QSYDLDHMEK KDHSHTPWIV IVAKYLAQWY SETNGRIPKT
     YKEKEDFRDL IRQGILKNEN GAPEDEENFE EAIKNVNTAL NTTQIPSSIE DIFNDDRCIN
     ITKQTPPFWI LARALKEFVA KEGQGNLPVR GTIPDMIADS GKYIKLQNVY REKAKKDAAA
     VGNHVAKLLQ SIGQAPESIS EKELKLLCSN SAFLRVVRCR SLAEEYGLDT INKDEIISSM
     DNPDNEIVLY LMLRAVDRFH KQHGRYPGVS NYQVEEDIGK LKSCLTGFLQ EYGLSVMVKD
     DYIHEFCRYG AAEPHTIAAF LGGAAAQEVI KIITKQFVIF NNTYIYSGMS QTSATFQL
//
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