RN170_DANRE
ID RN170_DANRE Reviewed; 266 AA.
AC Q7SZN2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; ORFNames=zgc:65779;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays an essential role in
CC stimulus-induced inositol 1,4,5-trisphosphate receptor (ITPR)
CC ubiquitination and degradation via the endoplasmic reticulum-associated
CC degradation (ERAD) pathway. Also involved in ITPR turnover in resting
CC cells. {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 -!- 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; BC056330; AAH56330.1; -; mRNA.
DR EMBL; BC069061; AAH69061.1; -; mRNA.
DR RefSeq; NP_999915.1; NM_214750.1.
DR AlphaFoldDB; Q7SZN2; -.
DR STRING; 7955.ENSDARP00000038867; -.
DR PaxDb; Q7SZN2; -.
DR GeneID; 406612; -.
DR KEGG; dre:406612; -.
DR CTD; 81790; -.
DR ZFIN; ZDB-GENE-040426-2572; rnf170.
DR eggNOG; KOG2164; Eukaryota.
DR InParanoid; Q7SZN2; -.
DR OrthoDB; 1563172at2759; -.
DR PhylomeDB; Q7SZN2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7SZN2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0043009; P:chordate embryonic development; IMP:ZFIN.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010652; DUF1232.
DR InterPro; IPR038896; RNF170.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22894; PTHR22894; 1.
DR PANTHER; PTHR22894:SF1; PTHR22894:SF1; 1.
DR Pfam; PF06803; DUF1232; 1.
DR Pfam; PF00097; zf-C3HC4; 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 pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..266
FT /note="E3 ubiquitin-protein ligase RNF170"
FT /id="PRO_0000280702"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..266
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 266 AA; 29628 MW; DE96CEFAA32CB987 CRC64;
MEGSVCVDGA AAPAPDEASL IEGVSNAVLL VLVLSVTLLA GLTTLLCRSE QQRIHPESQE
RVRVVREQLQ AEQVSSESRH QFYSDMSCPV CLQQAVLPVE TNCGHLFCGS CIIAYWRYGT
WLGAISCPIC RQMVTLLFPL FQDSEQSAVA ADSPVEPTLI LTDISDYNRR FSGQPRSLLD
RLRDVPTLLR HAFREMFSVG GLFWMFRVRI LLCVCGALAY LVSPLDFLPE GVLGLLGFLD
DFFVILLLFI YISIMYREVV TQRLAG