ID   A0A340X054_LIPVE        Unreviewed;       917 AA.
AC   A0A340X054;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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_007452694.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007452694.1};
RN   [1] {ECO:0000313|RefSeq:XP_007452694.1}
RP   IDENTIFICATION.
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}.
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DR   RefSeq; XP_007452694.1; XM_007452632.1.
DR   AlphaFoldDB; A0A340X054; -.
DR   STRING; 118797.A0A340X054; -.
DR   GeneID; 103082838; -.
DR   KEGG; lve:103082838; -.
DR   CTD; 130507; -.
DR   InParanoid; A0A340X054; -.
DR   OrthoDB; 51389at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000265300; 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; 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   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:UP000265300};
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          100..171
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         100..171
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          320..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         917
FT                   /evidence="ECO:0000313|RefSeq:XP_007452694.1"
SQ   SEQUENCE   917 AA;  102979 MW;  EA2A6CCF97665582 CRC64;
     MPAPGLALDK AATAAHLKAA LSRPDNRAGA EELQALLERV LSAERPLAAA ADGEEAAAAG
     GGGGSGAAEE EALEWCKCLL AGGGGYDEFC AAVRAYDPAA LCGLVWTANF VAYRCRTCGI
     SPCMSLCAEC FHQGDHTGHD FNMFRSQAGG ACDCGDSNVM RESGFCKRHQ IKSSSNIPCV
     PKDLLMMSEF VLPRFIFCLI QYLREGYNEP AADVPSEKDL NKVLQLLEPQ ISFLEDLTKM
     GGAMRSVLTQ VLTNQQSYKD LTSGLGENAY ARKSHEKYLI ALKSSGLTYP EDKLVYGIQE
     PSAGTSTLAV QGFAGATGTL GQLDSSDEED QDGSQGLGKR KRVKLSSNTK DQSIMDVLKH
     KSFLEELLFW TIKYEFPQKM VTFLLNMLPD QEYKVAFTKT FVQHYAFIMK TLKKSHESDT
     MSNRIVHISV QLFSNEELAR QVTEECQLLD IMVTVLLYMM ESCLIKSELQ DEENSLHVVV
     NCGEALLKNN TYWPLVSDFI NILSHQSVAK RFLEDHGLLV TWMNFVSFFQ GMNLNKRELN
     EHVEFESQTY YAAFAAELEA CAQPMWGLLS HCKVRETQEY TRNVVRYCLE ALQDWFDAIN
     FVDEPAPNQV TFHLPLHRYY AMFLSKAVKC QELDLDSVLP DQEMLMKLMI HPLQIQASLA
     EIHSNMWVRN GLQIKGQAMT YVQSHFCNSM IDPDIYLLQV CASRLDPDYF ISSVFERFKV
     VDLLTMASQH QNTVLDAEHE RSMLEGALTF LVILLSLRLH LGMSDDEILR AEMVAQLCMN
     DRTHSSLLDL IPENPNPKSG IIPGSYSFES VLSAVADFKA PVFEPGGSMQ QGMYTPKAEV
     WDHEFDPVMV ILRTVYRRDV QSAMDRYTAF LKQSGKFPGN PWPPYKKRTP LHPSYKGLMR
     LLHCKTLHIV LFTLLYK
//