ID A4FV12_BOVIN Unreviewed; 640 AA. AC A4FV12; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 22-FEB-2023, entry version 124. DE RecName: Full=SUMO-activating enzyme subunit 2 {ECO:0000256|PIRNR:PIRNR039133}; DE EC=2.3.2.- {ECO:0000256|PIRNR:PIRNR039133}; GN Name=UBA2 {ECO:0000313|EMBL:AAI23591.1, GN ECO:0000313|Ensembl:ENSBTAP00000003333.4, GN ECO:0000313|VGNC:VGNC:36562}; GN Synonyms=SAE2 {ECO:0000313|EMBL:AAI23591.1}; 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 {ECO:0000313|EMBL:AAI23591.1}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000003333.4, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000003333.4, RC ECO:0000313|Proteomes:UP000009136}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAI23591.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hereford {ECO:0000313|EMBL:AAI23591.1}; RC TISSUE=Fetal lung {ECO:0000313|EMBL:AAI23591.1}; RA Quirk P.G., Krulwich T.A.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSBTAP00000003333.4} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000003333.4}; RG Ensembl; RL Submitted (OCT-2022) to UniProtKB. 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. CC {ECO:0000256|PIRNR:PIRNR039133}. CC -!- PATHWAY: Protein modification; protein sumoylation. CC {ECO:0000256|ARBA:ARBA00004718, ECO:0000256|PIRNR:PIRNR039133}. 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. CC {ECO:0000256|ARBA:ARBA00026003}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|PIRNR:PIRNR039133}. CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|PIRNR:PIRNR039133}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC123590; AAI23591.1; -; mRNA. DR RefSeq; NP_001076850.1; NM_001083381.1. DR STRING; 9913.ENSBTAP00000003333; -. DR Ensembl; ENSBTAT00000003333.5; ENSBTAP00000003333.4; ENSBTAG00000002573.5. DR GeneID; 507005; -. DR KEGG; bta:507005; -. DR CTD; 10054; -. DR VEuPathDB; HostDB:ENSBTAG00000002573; -. DR VGNC; VGNC:36562; UBA2. DR eggNOG; KOG2013; Eukaryota. DR GeneTree; ENSGT00550000074924; -. DR HOGENOM; CLU_013325_7_4_1; -. DR OMA; VQWDTLL; -. DR OrthoDB; 20494at2759; -. DR TreeFam; TF300765; -. DR Reactome; R-BTA-3065676; SUMO is conjugated to E1 (UBA2:SAE1). DR Reactome; R-BTA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9). DR UniPathway; UPA00886; -. DR Proteomes; UP000009136; Chromosome 18. DR Bgee; ENSBTAG00000002573; Expressed in spermatocyte and 111 other tissues. 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; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0044388; F:small protein activating enzyme binding; IEA:Ensembl. DR GO; GO:0019948; F:SUMO activating enzyme activity; IBA:GO_Central. DR GO; GO:0032183; F:SUMO binding; IEA:Ensembl. DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IEA:Ensembl. DR GO; GO:0033235; P:positive regulation of protein sumoylation; IEA:Ensembl. DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central. DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central. DR CDD; cd01489; Uba2_SUMO; 1. DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1. DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1. DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1. DR InterPro; IPR045886; ThiF/MoeB/HesA. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR InterPro; IPR028077; UAE_UbL_dom. DR InterPro; IPR042449; Ub-E1_IAD_1. DR InterPro; IPR023318; Ub_act_enz_dom_a_sf. DR InterPro; IPR030661; Uba2. DR InterPro; IPR032426; UBA2_C. DR InterPro; IPR035985; Ubiquitin-activating_enz. DR InterPro; IPR018074; UBQ-activ_enz_E1_CS. DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS. DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1. DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1. DR Pfam; PF00899; ThiF; 1. DR Pfam; PF14732; UAE_UbL; 1. DR Pfam; PF16195; UBA2_C; 1. DR PIRSF; PIRSF039133; SUMO_E1B; 1. DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1. DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|PIRNR:PIRNR039133, ECO:0000256|PIRSR:PIRSR039133- KW 2}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR039133, KW ECO:0000256|PIRSR:PIRSR039133-3}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR039133, KW ECO:0000256|PIRSR:PIRSR039133-2}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR039133}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A4FV12}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Ubl conjugation {ECO:0000256|PIRNR:PIRNR039133}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PIRNR:PIRNR039133}; KW Zinc {ECO:0000256|PIRNR:PIRNR039133, ECO:0000256|PIRSR:PIRSR039133-3}. FT DOMAIN 9..442 FT /note="THIF-type NAD/FAD binding fold" FT /evidence="ECO:0000259|Pfam:PF00899" FT DOMAIN 452..537 FT /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like" FT /evidence="ECO:0000259|Pfam:PF14732" FT DOMAIN 549..630 FT /note="SUMO-activating enzyme subunit 2 C-terminal" FT /evidence="ECO:0000259|Pfam:PF16195" FT REGION 202..233 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 287..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 551..628 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..233 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 288..306 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 563..586 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 601..628 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 173 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1, FT ECO:0000256|PROSITE-ProRule:PRU10132" FT BINDING 24..29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2" FT BINDING 56..59 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2" FT BINDING 72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2" FT BINDING 95..96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2" FT BINDING 117..122 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2" FT BINDING 158 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3" FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3" FT BINDING 441 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3" FT BINDING 444 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-4" FT CROSSLNK 190 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-4" FT CROSSLNK 236 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-4" FT CROSSLNK 257 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-4" FT CROSSLNK 420 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-4" FT CROSSLNK 623 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000256|PIRSR:PIRSR039133-4" SQ SEQUENCE 640 AA; 71031 MW; 4B1946642E4AE5DA CRC64; MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD YNVEFFRQFI LVMNALDNRA ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEASWEPM EAEARARASN EDGDIKRVST KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETSASDQQ NEPQLGLKDQ QVLDVKSYAC LFSKSIETLR VHLAEKGDGA ELIWDKDDPS AMDFVTSAAN LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL EGLKILSGKI DQCRTIFLNK QPNPRKKLLV PCALDAPNPN CYVCASKPEV TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV QIEDGKGTIL ISSEEGETEA NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK DVEFEVVGDA PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEGPSNN ADISEEERSR KRKLDEKESV SAKRSRIEQA EELDEVIALD //