RN186_BOVIN
ID RN186_BOVIN Reviewed; 226 AA.
AC Q3T0Y9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase RNF186 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9NXI6};
DE AltName: Full=RING finger protein 186 {ECO:0000250|UniProtKB:Q9NXI6};
GN Name=RNF186 {ECO:0000250|UniProtKB:Q9NXI6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin protein ligase that is part of an apoptotic
CC signaling pathway activated by endoplasmic reticulum stress. Stimulates
CC the expression of proteins specific of the unfolded protein response
CC (UPR), ubiquitinates BNIP1 and regulates its localization to the
CC mitochondrion and induces calcium release from the endoplasmic
CC reticulum that ultimately leads to cell apoptosis. Plays a role in the
CC maintenance of intestinal homeostasis and clearance of enteric
CC pathogens. Upon NOD2 stimulation, ubiquitinates the ER stress sensor
CC activating transcription factor 6/ATF6 and promotes the unfolded
CC protein response UPR. Participates in basal level of autophagy
CC maintenance by regulating the ubiquitination of EPHB2. Upon stimulation
CC by ligand EFNB1, ubiquitinates EPHB2 and further recruits MAP1LC3B for
CC autophagy induction. Controls nutrient sensing by ubiquitinating
CC Sestrin-2/SESN2, which is an intracellular sensor of cytosolic leucine
CC and inhibitor of mTORC1 activity. {ECO:0000250|UniProtKB:Q9NXI6}.
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:0000250|UniProtKB:Q9NXI6};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9NXI6}.
CC -!- SUBUNIT: Interacts with BNIP1. {ECO:0000250|UniProtKB:Q9NXI6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NXI6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The RING-type domain is required for ubiquitination.
CC {ECO:0000250|UniProtKB:Q9NXI6}.
CC -!- PTM: Polyubiquitinated. 'Lys-29' autoubiquitination leads to
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q9NXI6}.
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DR EMBL; BC102202; AAI02203.1; -; mRNA.
DR RefSeq; NP_001030388.1; NM_001035311.2.
DR AlphaFoldDB; Q3T0Y9; -.
DR SMR; Q3T0Y9; -.
DR STRING; 9913.ENSBTAP00000040482; -.
DR PaxDb; Q3T0Y9; -.
DR GeneID; 515529; -.
DR KEGG; bta:515529; -.
DR CTD; 54546; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q3T0Y9; -.
DR OrthoDB; 1446732at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0035519; P:protein K29-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038878; RNF186.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22791:SF21; PTHR22791:SF21; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..226
FT /note="E3 ubiquitin-protein ligase RNF186"
FT /id="PRO_0000261623"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 39..85
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 120..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 24378 MW; 621FBD33D6E2AC4B CRC64;
MACLEIPQQP QLVCQKATPS DPAGCDGGPG GPTEGDLECL VCREPYSGVR PPKLLGCQHA
FCAVCLKLLL CVQDDAWSIP CPLCRKVTAV PGGLVCTLRD QEKVLERLAR PGLEVPLRPQ
GLANPATLTA GQPREAGEEE QDAVTTNRAA ARRLAAHLLL LVLLIILILP FIYPGVIRWV
LSFLETLALL LALLFCSHPG QQDGCMPTPR TLFCRERKPS EIASIS
