ID M3YF17_MUSPF Unreviewed; 1753 AA.
AC M3YF17;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=UBR1 {ECO:0000313|Ensembl:ENSMPUP00000009924.1,
GN ECO:0000313|RefSeq:XP_004751275.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009924.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000009924.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004751275.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004751275.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; AEYP01028357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004751275.1; XM_004751218.3.
DR STRING; 9669.ENSMPUP00000009924; -.
DR Ensembl; ENSMPUT00000010084.1; ENSMPUP00000009924.1; ENSMPUG00000009999.1.
DR GeneID; 101682186; -.
DR KEGG; mpuf:101682186; -.
DR CTD; 197131; -.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_001801_2_0_1; -.
DR OMA; TWMKLLA; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0000502; C:proteasome complex; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0070728; F:leucine binding; IEA:Ensembl.
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:0071233; P:cellular response to leucine; IEA:Ensembl.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IEA:Ensembl.
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 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; 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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
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|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"
FT COMPBIAS 842..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1753 AA; 200409 MW; FC4B347E1ACD19F8 CRC64;
MADEEAGGAE RMEVSTELPQ TPQLLASWWD QQVDFYTTFL HYLAQLVPEI YSAEMDPDLE
KQEESIQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG KVFKSGETTY SCRDCAIDPT
CVLCMDCFQN SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVSHEPGR AGTTKENLRC
PLNEEVIAQA RKIFPSVVKY 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
YILISKPTAW TERLRMQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM
QLKNILLMFQ EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTVVQLCG HALETKSYRV
SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVPFEDF QVEVLVEYPL RCLVLVAQVV
AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS LMDPNKFLLL VLQRYELADA
FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTKEEVTMR EIIHLLCIEP
MPHSAIAKNL PENENNETGL ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK
TQHSKAEHMQ KKRRKQENKD EALPPPPPPE FCPAFSKVVN LLNCDIMMYI LRTIFERAID
TDSNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVTFD FYHKASRLGS SSMNAQNIQM
LLEKLKGIPQ LEGQKDMITW ILQMFDTVKR LREKSCLIVA TTSGSESIKN DEVTHDKEKA
ERKRKAEAAR LHRQKIMAQM SALQKNFIET HKLMYDSTSE MSGKEDSIME EESTPAVSDY
SRIALGPKRG PTVTEKEVLT CILCQEEQEV KIENNAMVLS ACVQKSTALT QNRGKPIELS
GEIVDPLFMD PDLAYGTYTG SCGHVMHAVC WQKYFEAVQL SSQQRIHVDL FDLESGEYLC
PLCKSLCNTV IPIIPLQPQR ISSENTEAVG QLLTLEQWIQ TVLARISGYN MKHARGENPT
IPVLFDQGMG DSTFEFHSIL NFGVQSSIKY SNSIKEMVIL FATTIYRIGL KVPPDETDPR
IPMMTWSTCA FTIQAIENLL GDEGKPLFGA LQNRQHNGLK ALMQFAIAQK ITCPQVLIQK
HLIRLLSVVL PNLKSEDTPC LLSIDLFHVL VGAVLAFPSL YWEDTVDLQP SSISSSYTHL
YLFHLITMAH MLQILLTIDT ELPLAQVQEE SEEARSASSF LAEVSQYTNG CIGCGVPGWY
LWASLKNGIT PYLRCAALFF HYLLGITPPE ELLTNSAEGE YGALCSYLSL PTNLFLLFQE
YWDTVRPLLQ RWCADPALLN CLKQKSTVVR YPRKRNSLIE LPDDYSCLLN QASHFRCPRS
ADDERKHPVL CLFCGAILCS QNICCQEIVN GEEVGACIFH ALHCGAGVCI FLKIRECRVV
LVEGKARGCA YPAPYLDEYG ETDPGLKRGN PLHLSRERYR KLHLVWQQHC IIEEIARSQE
TNQMLFGFNW QLL
//
