ID A0A288CFV1_PIG Unreviewed; 148 AA.
AC A0A288CFV1; A0A4X1UN61;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ubiquitin conjugating enzyme E2 D3 {ECO:0000313|Ensembl:ENSSSCP00000057683.2};
DE SubName: Full=Ubiquitin-conjugating enzyme E2 D3 isoform 2 {ECO:0000313|EMBL:HDB48417.1};
GN Name=UBE2D3 {ECO:0000313|Ensembl:ENSSSCP00000057683.2};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000057683.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000057683.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000057683.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB48417.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000057683.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000256|ARBA:ARBA00000485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000256|ARBA:ARBA00035845};
CC -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000256|RuleBase:RU362109}.
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DR EMBL; DQIR01192940; HDB48417.1; -; Transcribed_RNA.
DR RefSeq; XP_005656607.1; XM_005656550.2.
DR RefSeq; XP_013844838.1; XM_013989384.1.
DR RefSeq; XP_013844840.1; XM_013989386.1.
DR RefSeq; XP_013844841.1; XM_013989387.1.
DR RefSeq; XP_013844842.1; XM_013989388.1.
DR Ensembl; ENSSSCT00000065206.3; ENSSSCP00000057683.2; ENSSSCG00000035622.3.
DR Ensembl; ENSSSCT00005062741.1; ENSSSCP00005038780.1; ENSSSCG00005039203.1.
DR Ensembl; ENSSSCT00005062792.1; ENSSSCP00005038810.1; ENSSSCG00005039203.1.
DR GeneTree; ENSGT00940000153169; -.
DR OMA; RNCKEIL; -.
DR Reactome; R-SSC-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-SSC-201451; Signaling by BMP.
DR Reactome; R-SSC-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-SSC-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-SSC-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SSC-8951664; Neddylation.
DR Reactome; R-SSC-9033241; Peroxisomal protein import.
DR Reactome; R-SSC-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-SSC-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000035622; Expressed in oocyte and 41 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR PANTHER; PTHR24068:SF415; UBIQUITIN-CONJUGATING ENZYME E2 D3; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362109};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 148 AA; 16785 MW; E73DC194DB6D4EFE CRC64;
MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD RDKYNRLARE WTEKYAML
//
