ID A0A2Y9N8Y9_DELLE Unreviewed; 1534 AA.
AC A0A2Y9N8Y9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=UBR3 {ECO:0000313|RefSeq:XP_022425718.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022425718.1};
RN [1] {ECO:0000313|RefSeq:XP_022425718.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022425718.1};
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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
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 RefSeq; XP_022425718.1; XM_022570010.2.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248483; Unplaced.
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; cd16483; RING-H2_UBR3; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000248483};
KW Transferase {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 119..190
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 119..190
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1534 AA; 172334 MW; 69B0ED4A8C507522 CRC64;
MAAAAAAAAV GGPQPPQAEM PAPGLALDKA ATAAHLKAAL SRPDNRAGAE ELQALLERVL
SAERPLAAAA DGEEAAAAGG GGGPGAAEEE ALEWCKCLLA GGGGYDEFCA AVRAYDPAAL
CGLVWTANFV AYRCRTCGIS PCMSLCAECF HQGDHTGHDF NMFRSQAGGA CDCGDSNVMR
ESGYTNQRKK TTENSFVGRD HKAYRNCINN CMLPLMFCKR HQIKSSSNIP CVPKDLLMMS
EFVLPRFIFC LIQYLREGYN EPAADVPSEK DLNKVLQLLE PQISFLEDLT KMGGAMRSVL
TQVLTNQQSY KDLTSGLGEN AYARKSHEKY LIALKSSGLT YPEDKLVYGI QEPSAGTSTL
AVQGFAGATG TLGQLDSSDE EDQDGSQGLG KRKRVKLSSN TKDQSIMDVL KHKSFLEELL
FWTIKYEFPQ KMVTFLLNML PDQEYKVAFT KTFVQHYAFI MKTLKKSHES DTMSNRIVHI
SVQLFSNEEL ARQVTEECQL LDIMVTVLLY MMESCLIKSE LQDEENSLHV VVNCGEALLK
NNTYWPLVSD FINILSHQSV AKRFLEDHGL LVTWMNFVSF FQGMNLNKRE LNEHVEFESQ
TYYAAFAAEL EACAQPMWGL LSHCKVRETQ EYTRNVVRYC LEALQDWFDA INFVDEPAPN
QVTFHLPLHR YYAMFLSKAV KCQELDLDSV LPDQEMLMKL MIHPLQIQAS LAEIHSNMWV
RNGLQIKGQA MTYVQSHFCN SMIDPDIYLL QVCASRLDPD YFISSVFERF KVVDLLTMAS
QHQNTVLDAE HERSMLEGAL TFLVILLSLR LHLGMSDDEI LRAEMVAQLC MNDRTHSSLL
DLIPENPNPK SGIIPGSYSF ESVLSAVADF KAPVFEPGGS MQQGMYTPKA EVWDHEFDPV
MVILRTVYRR DVQSAMDRYT AFLKQSGKFP GNPWPPYKKR TPLHPSYKGL MRLLHCKTLH
IVLFTLLYKI LMDHQNLSEH VLCMVLYLIE LGLENSAEEE SDEEASVGGP ERCHDSWFPG
SNLVSNMRHF INYVRVRVPE TAPEVKRDSP ASTSSDSLGS LQNSGTAQVF SLVAERRKKF
QEIINRNSSE ANQVVRPKTS NKWSAPGSAP QLTTAILEIK ESILSLLIKL HHKLSGKQNS
YYPPWLDDIE ILIQPDIPKY SHGDGITAVE RILLKAALQS RMNKRIIEEI CRKVTPPVPP
KKITAAEKKT LDKEERRQKA RERQQKLLAE FASRQKSFME TAMDVDSPES DIPMEITTAE
PQVSEAVYDC VICGQSGPSS EDRPTGLVVL LQASSVLGQC RDNIEPKKLP ITEEEQIYPW
DTCAAVHDVR LSLLQRYFKD SSCLLAVSIG WEGGVYVQTC GHTLHIDCHK SYMESLRNDQ
VLQGFSVDKG EFTCPLCRQF ANSVLPCYPG SNVENNLWQR PSNKSIQDLI KEVEELQGRP
GAFPSETNLS KEMESVMKDI KNTTQKKYRD YSKTPGSPDN DFLFMYSVAR LGNRRFVKTK
CIDLIYIPLM KEHMLVSARF LSTNMKSLSL LPCW
//
