ID   SAE1_BOVIN              Reviewed;         346 AA.
AC   A2VE14;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 105.
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;
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=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; BC133519; AAI33520.1; -; mRNA.
DR   RefSeq; NP_001075180.1; NM_001081711.1.
DR   AlphaFoldDB; A2VE14; -.
DR   SMR; A2VE14; -.
DR   STRING; 9913.ENSBTAP00000003467; -.
DR   PaxDb; A2VE14; -.
DR   PeptideAtlas; A2VE14; -.
DR   PRIDE; A2VE14; -.
DR   Ensembl; ENSBTAT00000003467; ENSBTAP00000003467; ENSBTAG00000002676.
DR   GeneID; 505512; -.
DR   KEGG; bta:505512; -.
DR   CTD; 10055; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002676; -.
DR   VGNC; VGNC:34261; SAE1.
DR   eggNOG; KOG2014; Eukaryota.
DR   GeneTree; ENSGT00550000075007; -.
DR   HOGENOM; CLU_002556_4_0_1; -.
DR   InParanoid; A2VE14; -.
DR   OMA; TDVWGTF; -.
DR   OrthoDB; 1180926at2759; -.
DR   TreeFam; TF315037; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000002676; Expressed in spermatocyte and 105 other tissues.
DR   ExpressionAtlas; A2VE14; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IBA:GO_Central.
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..346
FT                   /note="SUMO-activating enzyme subunit 1"
FT                   /id="PRO_0000423289"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   CHAIN           2..346
FT                   /note="SUMO-activating enzyme subunit 1, N-terminally
FT                   processed"
FT                   /id="PRO_0000328137"
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         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBE0"
FT   MOD_RES         198
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1T2"
SQ   SEQUENCE   346 AA;  38306 MW;  04CE3BE656FA8EC6 CRC64;
     MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASQVL LVGMKGLGAE IAKNLILAGV
     KGLTMLDHEQ VSPEDPGAQF LIRTGSVGRN RAEASLERAQ NLNPMVDVKV DTENIEKKPE
     SFFTQFDAVC LTCCSRDVIV KVDQICHKNS IKFFTGDVFG YHGYTFANLG EHEFVEEKTK
     VAKVSQGVED GPDTKRAKLD SSETTMVKKK VVFCSVKEAL EVDWSSDKAK AALKRTTPDY
     FLLQVLLKFR TDKGRDPSSD TFGEDSELLL QIRNDVLDAL GVNPDLLPED FVRYCFSEMA
     PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPN