ID B7TJ08_PIG Unreviewed; 502 AA.
AC B7TJ08; A0A4X1V2L4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000256|ARBA:ARBA00031783};
GN Name=RAD18 {ECO:0000313|EMBL:ACJ53929.1,
GN ECO:0000313|Ensembl:ENSSSCP00000049022.1,
GN ECO:0000313|VGNC:VGNC:92053};
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|EMBL:ACJ53929.1};
RN [1] {ECO:0000313|EMBL:ACJ53929.1}
RP NUCLEOTIDE SEQUENCE.
RA Liu G.Y.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000049022.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000049022.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HDB72815.1}
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 [4] {ECO:0000313|Ensembl:ENSSSCP00005040738.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RAD18 family.
CC {ECO:0000256|ARBA:ARBA00009506}.
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DR EMBL; FJ236699; ACJ53929.1; -; mRNA.
DR EMBL; DQIR01217338; HDB72815.1; -; Transcribed_RNA.
DR EMBL; DQIR01231513; HDB86990.1; -; Transcribed_RNA.
DR EMBL; DQIR01232024; HDB87501.1; -; Transcribed_RNA.
DR RefSeq; NP_001136305.1; NM_001142833.1.
DR Ensembl; ENSSSCT00000065083.3; ENSSSCP00000049022.1; ENSSSCG00000026158.4.
DR Ensembl; ENSSSCT00005065829.1; ENSSSCP00005040738.1; ENSSSCG00005040752.1.
DR GeneID; 100217383; -.
DR KEGG; ssc:100217383; -.
DR VGNC; VGNC:92053; RAD18.
DR GeneTree; ENSGT00390000011230; -.
DR OMA; IPNTGPR; -.
DR OrthoDB; 6177at2759; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; RAD18; pig.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000026158; Expressed in oocyte and 46 other cell types or tissues.
DR Genevisible; B7TJ08; SS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0000403; F:Y-form DNA binding; IEA:Ensembl.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR CDD; cd16529; RING-HC_RAD18; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 25..63
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 202..229
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT DOMAIN 249..283
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 161..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 431..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 56727 MW; 606F431F8028F2B4 CRC64;
MDSLVEQRWP PGLAVMKPVD DLLRCGICFE YFNIAMMIPQ CSHNYCSLCI RKFLSYKTQC
PTCCVTVTEP DLKNNRVLDE LVKSLNFARN HLLQFALESP PVSPASSSSK NHAVKVQSTP
VGFRHSLKKG SRLMENFLIR ETGGSMSELL IKENESKFSP LKELSSSAKT GGPPSVEKSA
PGSSEAIVPE TPSTSALKQV TKVDCPVCGV NIPENHINKH LDSCLSREEK KESLRSSVQK
RKLLPKTVYN LLSDRDLKKK LKQHGLSVQG NKQQLIKRHQ EFVHMYNAQC DALHPKSAAE
IVQEIENMEK TRMRLEASKL NESIMVFTKD QTEKEIDEIH RKYRKKHQNE FQLLVDQAKK
GYEKAVGMSK KKVTKKDDES TKDLLSVCVG PEDNKMKLSD TPLVTKHLPQ LMLDSPGKLE
PDRPDDSSSC TDFQEEALSS SESDSCNSSS SDIIRDLLEE EEAWEASHKN DLQDTEISPR
QNRRTRSAES VDLEPRNKRN RN
//
