ID   ULA1_DANRE              Reviewed;         533 AA.
AC   Q7SXP2; A7MBR8; Q7ZUA4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit;
DE   AltName: Full=APP-BP1;
DE   AltName: Full=Amyloid protein-binding protein 1;
GN   Name=nae1; Synonyms=appbp1;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=SJD; TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Heterodimer of uba3 and nae1. The complex binds nedd8 and
CC       ube2m (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7SXP2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7SXP2-2; Sequence=VSP_016394;
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50171.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC050171; AAH50171.1; ALT_INIT; mRNA.
DR   EMBL; BC055513; AAH55513.1; -; mRNA.
DR   EMBL; BC151887; AAI51888.1; -; mRNA.
DR   RefSeq; NP_956793.1; NM_200499.1.
DR   AlphaFoldDB; Q7SXP2; -.
DR   SMR; Q7SXP2; -.
DR   STRING; 7955.ENSDARP00000026192; -.
DR   PaxDb; Q7SXP2; -.
DR   GeneID; 573336; -.
DR   KEGG; dre:573336; -.
DR   CTD; 8883; -.
DR   ZFIN; ZDB-GENE-040426-1552; nae1.
DR   eggNOG; KOG2016; Eukaryota.
DR   InParanoid; Q7SXP2; -.
DR   OrthoDB; 454386at2759; -.
DR   PhylomeDB; Q7SXP2; -.
DR   Reactome; R-DRE-8951664; Neddylation.
DR   UniPathway; UPA00885; -.
DR   PRO; PR:Q7SXP2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   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; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PIRSF; PIRSF039099; APP-BP1; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..533
FT                   /note="NEDD8-activating enzyme E1 regulatory subunit"
FT                   /id="PRO_0000194955"
FT   REGION          330..343
FT                   /note="Interaction with uba3"
FT                   /evidence="ECO:0000250"
FT   SITE            210
FT                   /note="Interaction with uba3"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         259..332
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_016394"
FT   CONFLICT        11
FT                   /note="K -> R (in Ref. 1; AAH55513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="R -> G (in Ref. 1; AAH55513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="Y -> H (in Ref. 1; AAI51888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="N -> T (in Ref. 1; AAI51888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        488
FT                   /note="E -> G (in Ref. 1; AAI51888)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  60404 MW;  C9DC6D4F4C04514A CRC64;
     MTDPKTSKEQ KYDRQLRLWG DHGQEALENA HVCLINATAS GTEILKNLVL PGIGAFTIVD
     GHKVSGEDVG NNFFLSSSAI GKNRAQAATE LLQELNSDVS GNFVEESPDK LLDNDCEFFH
     RFSLVIAVQL PESTCLRLGA VLWEAGVPFL VCRTYGLIGY MRLIVKEHTV VESHPDNALE
     DLRLDQPFTE LKRHVESYDL DNMEKKDHSH TPWIIVVARY LEKWYNENNS QLPKNYKEKE
     AFRQLLREGI LKNENGGLED EENFEEAIKN VNTALNPTKI SSGTQDIFNA EQCENITSQS
     SSFWVMAHGV RDFVQNEGNG NLPVRGSIPD MIADSDKFIK LQNVYRDKAM RDAAVVSKHV
     EMLLQSVGKT PESISEQEIK LFCKNAAFLR VVRCRSLADE YSVDTFNKDE ITSCMDSPDS
     EMVLYLMLRS VDRFYQQHSR YPGVYNYQVE EDINKLKLCV NSLLQEYSLN VNVKDDYIHE
     FCRYGAAEPH TVAAFLGGSA AQEAIKIITH QFVPFNNTFL YNAMSQTSAT FQL