ID A0A2Y9KUC2_ENHLU Unreviewed; 1745 AA.
AC A0A2Y9KUC2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=LOC111158765 {ECO:0000313|RefSeq:XP_022376743.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022376743.1};
RN [1] {ECO:0000313|RefSeq:XP_022376743.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022376743.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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 ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SUBUNIT: Interacts with RECQL4. {ECO:0000256|ARBA:ARBA00062088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, ECO:0000256|RuleBase:RU366018}.
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DR RefSeq; XP_022376743.1; XM_022521035.1.
DR GeneID; 111158765; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd19678; UBR-box_UBR1; 1.
DR FunFam; 3.30.1390.10:FF:000005; E3 ubiquitin-protein ligase UBR1 isoform X2; 1.
DR FunFam; 2.10.110.30:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform 1; 1.
DR FunFam; 1.10.10.2670:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform X1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR047507; UBR-box_UBR1.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR055194; UBR1-like_WH.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF27; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF22960; WHD_UBR1; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 842..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1745 AA; 199497 MW; 23DC439A2DA3D863 CRC64;
MADEEAGGAE RMEVSTELPQ TPQLLASWWD QQVDFYTTFL HYLAQLVPEI YSAEMDPDLE
KQEESIQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG KVFKSGETTY SCRDCAIDPT
CVLCMDCFQN SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVSHEPGR AGTTKENLRC
PLNEEVIAQA RKIFPSVIKY IVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH
VIYSLQRALD CELAEAQLHT TAIDKEGRRA VKAGAFAACQ EAKEDIKSHS ENVSQHPLHV
EVLHSEVMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL REEPGSENPC LISRLMLWDA
KLYKGARKIL HELIFSSFFM EMEYKKFFAM EFVKYYKQLQ KEYISDDHDR SISVTALSVQ
MFTVPTLARH LIEEQNVISV ITETLLEVLP EYLDRNNKFN FQGYSQDKLG RVYAVICDLK
YILISKPTTW TERLRMQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM
QLKNILLMFQ EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTVVQLCG HTLETKSYRV
SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVPFEDF QVEVLVEYPL RCLVLVAQVV
AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS SMDPNKFLLL VLQRYELADA
FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTKEEVTMR EIIHLLCIEP
MPHSAIAKNL PENENNETGL ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK
TQHSKAEHMQ KKRRKQENKD EALPPPPPPE FCPAFSKVVN LLNCDIMMYI LRTIFERAID
TDSNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVTFD FYHKASRLGS SAMNAQNIQM
LLEKLKGIPQ LEGQKDMITW ILQMFDTVKR LREKSCLIVA TTSGSESIKN DEITHDKEKA
ERKRKAEAAR LHRQKIMAQM SALQKNFIET HKLMYDSTSE MSGKEDSIME EESTPAVSDY
SRIALGPKRG PTVTEKEVLT CILCQEEQEV KIENNAMVLS ACVQKSTALT QNRGKPIELS
GEIVDPLFMD PDLAYGTYTG SCGHVMHAVC WQKYFEAVQL SSQQRIHVDL FDLESGEYLC
PLCKSLCNTV IPIIPLQPQR ISSENTEAVG QLLTLEQWIQ TVLARISGEN PTIPVLFDQG
MGDSTFEFHS ILNFGVQSSI KYSNSIKEMV ILFATTIYRI GLKVPPDETD PRIPMMTWST
CAFTIQAIEN LLGDEGKPLF GALQNRQHNG LKALMQFAIA QKITCPQVLI QKHLIRLLSV
VLPNLKSEDT PCLLSIDLFH VLVGAVLAFP SLYWEDTVDL QPSSISSSYT HLYLFHLITM
AHMLQILLTI DTELPLAQVQ EESEEARSAS SFLAEVSQYT NGCIGSGVPG WYLWASLKNG
ITPYLRCAAL FFHYLLGITP PEELLTNSAE GEYGALCSYL SLPTNLFLLF QEYWDTVRPL
LQRWCADPAL LNCLKQKSTV VRYPRKRNSL IELPDDYSCL LNQASHFRCP RSSDDERKHP
VLCLFCGAIL CSQNICCQEI VNGEEVGACI FHALHCGAGV CIFLKIRECR VVLVEGKARG
CAYPAPYLDE YGETDPGLKR GNPLHLSRER YRKLHLVWQQ HCIIEEIARS QETNQMLFGF
NWQLL
//
