ID RN170_BOVIN Reviewed; 259 AA.
AC F1MK05;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=E3 ubiquitin-protein ligase RNF170;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 170;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF170 {ECO:0000305};
GN Name=RNF170;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Plays an essential role in
CC stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1)
CC ubiquitination and degradation via the endoplasmic reticulum-associated
CC degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting
CC cells. Selectively inhibits the TLR3-triggered innate immune response
CC by promoting the 'Lys-48'-linked polyubiquitination and degradation of
CC TLR3. {ECO:0000250|UniProtKB:Q96K19}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Constitutively associated with the ERLIN1/ERLIN 2 complex.
CC Interacts with activated ITPR1. {ECO:0000250|UniProtKB:Q96K19}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96K19}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96K19}.
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DR EMBL; DAAA02060959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1MK05; -.
DR SMR; F1MK05; -.
DR STRING; 9913.ENSBTAP00000072624; -.
DR PaxDb; 9913-ENSBTAP00000044412; -.
DR eggNOG; KOG2164; Eukaryota.
DR HOGENOM; CLU_072335_0_0_1; -.
DR InParanoid; F1MK05; -.
DR TreeFam; TF328342; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16553; RING-HC_RNF170; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010652; DUF1232.
DR InterPro; IPR038896; RNF170.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22894:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF170; 1.
DR PANTHER; PTHR22894; UNCHARACTERIZED; 1.
DR Pfam; PF06803; DUF1232; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..259
FT /note="E3 ubiquitin-protein ligase RNF170"
FT /id="PRO_0000418624"
FT TOPO_DOM 1..25
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 88..131
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 259 AA; 29690 MW; BF61BD6DEDE3B603 CRC64;
MAKYQGEVQS LKLDDDSVIE GVSDQVLVAV VVSLALIATL VYALFSRNAH QNIHPENQEL
VRVLREQLQT EQDAPAAARQ QFYTDMYCPI CLHQASLPVE TNCGHLFCGT CIVAYWRYGS
WLGAISCPIC RQTVTLLLPV FGENDQSQDV VSLHQDISDY NRRFSGQPRS IMERIMDLPT
LLRHAFREMF SVGGLFWMFR IRIILCLMGA FFYLISPLDF VPEALFGILG FLDDFFVIFL
LLIYISIMYR EVITQRLNR
//
