ID   SAE1_RAT                Reviewed;         349 AA.
AC   Q6AXQ0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=SUMO-activating enzyme subunit 1;
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1A;
DE   Contains:
DE     RecName: Full=SUMO-activating enzyme subunit 1, N-terminally processed;
GN   Name=Sae1; Synonyms=Uble1a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3,
CC       and probably SUMO4. It mediates ATP-dependent activation of SUMO
CC       proteins followed by formation of a thioester bond between a SUMO
CC       protein and a conserved active site cysteine residue on UBA2/SAE2 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds
CC       to the two domains that are encoded on a single polypeptide chain in
CC       ubiquitin-activating enzyme E1. Interacts with UBE2I (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
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DR   EMBL; BC079411; AAH79411.1; -; mRNA.
DR   RefSeq; NP_001012063.1; NM_001012063.1.
DR   AlphaFoldDB; Q6AXQ0; -.
DR   SMR; Q6AXQ0; -.
DR   BioGRID; 258986; 1.
DR   STRING; 10116.ENSRNOP00000020402; -.
DR   iPTMnet; Q6AXQ0; -.
DR   PhosphoSitePlus; Q6AXQ0; -.
DR   jPOST; Q6AXQ0; -.
DR   PaxDb; Q6AXQ0; -.
DR   PRIDE; Q6AXQ0; -.
DR   Ensembl; ENSRNOT00000020402; ENSRNOP00000020402; ENSRNOG00000015128.
DR   GeneID; 308384; -.
DR   KEGG; rno:308384; -.
DR   UCSC; RGD:1306098; rat.
DR   CTD; 10055; -.
DR   RGD; 1306098; Sae1.
DR   eggNOG; KOG2014; Eukaryota.
DR   GeneTree; ENSGT00550000075007; -.
DR   HOGENOM; CLU_002556_4_0_1; -.
DR   InParanoid; Q6AXQ0; -.
DR   OMA; TDVWGTF; -.
DR   OrthoDB; 1180926at2759; -.
DR   PhylomeDB; Q6AXQ0; -.
DR   TreeFam; TF315037; -.
DR   Reactome; R-RNO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; R-RNO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   UniPathway; UPA00886; -.
DR   PRO; PR:Q6AXQ0; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015128; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q6AXQ0; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
DR   GO; GO:0043008; F:ATP-dependent protein binding; ISO:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0044388; F:small protein activating enzyme binding; ISO:RGD.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:RGD.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Ligase; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..349
FT                   /note="SUMO-activating enzyme subunit 1"
FT                   /id="PRO_0000423293"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   CHAIN           2..349
FT                   /note="SUMO-activating enzyme subunit 1, N-terminally
FT                   processed"
FT                   /id="PRO_0000268868"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         2
FT                   /note="N-acetylvaline; in SUMO-activating enzyme subunit 1,
FT                   N-terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         201
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1T2"
SQ   SEQUENCE   349 AA;  38513 MW;  EBCF5C53436B2DDD CRC64;
     MVEKEEVSGG GGGISEEEAA QYDRQIRLWG LEAQKRLRAS RVLIVGMKGL GAEIAKNLIL
     AGVKGLTMLD HEQVSPEDLG AQFLIRTGSV GQNRAEASLE RAQNLNPMVD VKVDTEDIEK
     KPESFFTEFD AVCLTCCSKD VIIKVDQICH RNSIKFFTGD VFGYHGYTFA NLGEHEFVEE
     KTKVTKVSQG VEDGPDAKRA KLDSSETTMV KKKVLFCPVK EALAVDWSGE KAQAALKRTA
     PDYFLLQVLL KFRTDKGRDP TSDSYSEDAE LLLQIRNDVF DSLGVSPDLL PDDFVRYCFS
     EMAPVCAVVG GILAQEIVKA LSQRDPPHNN FFFFDGMKGS GIVECLGPQ