ID   SAE1_PONAB              Reviewed;         346 AA.
AC   Q5NVN7; Q5R4J6; Q5R520; Q5R6W2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 94.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860370; CAH92498.1; -; mRNA.
DR   EMBL; CR861062; CAH93146.1; -; mRNA.
DR   EMBL; CR861251; CAH93320.1; -; mRNA.
DR   EMBL; CR925978; CAI29626.1; -; mRNA.
DR   RefSeq; NP_001126955.1; NM_001133483.1.
DR   AlphaFoldDB; Q5NVN7; -.
DR   SMR; Q5NVN7; -.
DR   STRING; 9601.ENSPPYP00000011372; -.
DR   GeneID; 100173973; -.
DR   KEGG; pon:100173973; -.
DR   CTD; 10055; -.
DR   eggNOG; KOG2014; Eukaryota.
DR   HOGENOM; CLU_002556_4_0_1; -.
DR   InParanoid; Q5NVN7; -.
DR   OrthoDB; 1180926at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000001595; Unplaced.
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:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
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_0000423292"
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_0000268867"
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"
FT   CONFLICT        115..116
FT                   /note="IE -> VG (in Ref. 1; CAH92498)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="F -> L (in Ref. 1; CAI29626)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="L -> P (in Ref. 1; CAH93320)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  38450 MW;  E2B10A69FF2ED746 CRC64;
     MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE IAKNLILAGV
     KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ NLNPMVDVKV DTEDIEKKPE
     SFFTQFDAVC LTCCSRDVIV KVDQICHKNS IKFFTGDVFG YHGYTFANLG EHEFVEEKTK
     VAKVSQGVED GPDTKRAKLD SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY
     FLLQVLLKFR TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA
     PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK