ID A0A2U4ABG2_TURTR Unreviewed; 1894 AA.
AC A0A2U4ABG2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_019778310.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019778310.1};
RN [1] {ECO:0000313|RefSeq:XP_019778310.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019778310.1};
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 RefSeq; XP_019778310.1; XM_019922751.2.
DR GeneID; 101334978; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000245320; Chromosome 7.
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; IPR044046; E3_ligase_UBR-like_C.
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; PF18995; PRT6_C; 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:UP000245320};
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 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 339..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1894 AA; 213359 MW; 75825208E035F19C CRC64;
MAAAAAAAAV GGPQPPQAEM PAPGLALDKA ATAAHLKAAL SRPDNRAGAE ELQALLERVL
SAERPLAAAA DGEEAAAAGG GGGPGAAEEE ALEWCKCLLA GGGGYDEFCA AVRAYDPAAL
CGLVWTANFV AYRCRTCGIS PCMSLCAECF HQGDHTGHDF NMFRSQAGGA CDCGDSNVMR
ESGFCKRHQI KSSSNIPCVP KDLLMMSEFV LPRFIFCLIQ YLREGYNEPA ADVPSEKDLN
KVLQLLEPQI SFLEDLTKMG GAMRSVLTQV LTNQQSYKDL TSGLGENAYA RKSHEKYLIA
LKSSGLTYPE DKLVYGIQEP SAGTSTLAVQ GFAGATGTLG QLDSSDEEDQ DGSQGLGKRK
RVKLSSNTKD QSIMDVLKHK SFLEELLFWT IKYEFPQKMV TFLLNMLPDQ EYKVAFTKTF
VQHYAFIMKT LKKSHESDTM SNRIVHISVQ LFSNEELARQ VTEECQLLDI MVTVLLYMME
SCLIKSELQD EENSLHVVVN CGEALLKNNT YWPLVSDFIN ILSHQSVAKR FLEDHGLLVT
WMNFVSFFQG MNLNKRELNE HVEFESQTYY AAFAAELEAC AQPMWGLLSH CKVRETQEYT
RNVVRYCLEA LQDWFDAINF VDEPAPNQVT FHLPLHRYYA MFLSKAVKCQ ELDLDSVLPD
QEMLMKLMIH PLQIQASLAE IHSNMWVRNG LQIKGQAMTY VQSHFCNSMI DPDIYLLQVC
ASRLDPDYFI SSVFERFKVV DLLTMASQHQ NTVLDAEHER SMLEGALTFL VILLSLRLHL
GMSDDEILRA EMVAQLCMND RTHSSLLDLI PENPNPKSGI IPGSYSFESV LSAVADFKAP
VFEPGGSMQQ GMYTPKAEVW DHEFDPVMVI LRTVYRRDVQ SAMDRYTAFL KQSGKFPGNP
WPPYKKRTPL HPSYKGLMRL LHCKTLHIVL FTLLYKILMD HQNLSEHVLC MVLYLIELGL
ENSAEEESDE EASVGGPERC HDSWFPGSNL VSNMRHFINY VRVRVPETAP EVKRDSPAST
SSDSLGSLQN SGTAQVFSLV AERRKKFQEI INRNSSEANQ VVRPKTSNKW SAPGSAPQLT
TAILEIKESI LSLLIKLHHK LSGKQNSYYP PWLDDIEILI QPDIPKYSHG DGITAVERIL
LKAALQSRMN KRIIEEICRK VTPPVPPKKI TAAEKKTLDK EERRQKARER QQKLLAEFAS
RQKSFMETAM DVDSPESDIP MEITTAEPQV SEAVYDCVIC GQSGPSSEDR PTGLVVLLQA
SSVLGQCRDN IEPKKLPITE EEQIYPWDTC AAVHDVRLSL LQRYFKDSSC LLAVSIGWEG
GVYVQTCGHT LHIDCHKSYM ESLRNDQVLQ GFSVDKGEFT CPLCRQFANS VLPCYPGSNV
ENNLWQRPSN KSIQDLIKEV EELQGRPGAF PVSISSETNL SKEMESVMKD IKNTTQKKYR
DYSKTPGSPD NDFLFMYSVA RTNLELELIH RGGNLCSGGA STAGKRSCLN QLFHVLALHM
RLYSIDSEYN PWRKLTQLLE EMNSQLGNEE QQPEVPILYH DVTSLLLIQI LMMPQPLRKD
HFTCIVKVLF TLLYTQGLVA LSVKCNEDDR SAWKHTGALK KNTCDAEKSY EVLLSFVIRE
LSKGKLYHEE GTQECATISP IAWSPESTEK YLQDFCLHFL RITSLLQHHL FGEDLPSCQE
EEEFSVLSSC LGLLPTFYQT EHPFISASCL DWPVPAFDII SQWCFEINSF TERHAEQGKA
LLIQESRWKL PHLLQLPENY NTIFQYYHRK TCSVCTKVPK DPAVCLVCGT FVCLKGLCCK
QQSYCECVLH SQNCGAGTGI FLLINASVII IIRGHRFCLW GSVYLDAHGE EDRDLRRGKP
LYICKERYKV LEQQWISHTF DHINKRWGPH YNGL
//
