ID   RN170_XENLA             Reviewed;         257 AA.
AC   Q5PPX5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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; BC087450; AAH87450.1; -; mRNA.
DR   RefSeq; NP_001088785.1; NM_001095316.1.
DR   RefSeq; XP_018104407.1; XM_018248918.1.
DR   RefSeq; XP_018104416.1; XM_018248927.1.
DR   RefSeq; XP_018104426.1; XM_018248937.1.
DR   AlphaFoldDB; Q5PPX5; -.
DR   MaxQB; Q5PPX5; -.
DR   DNASU; 496050; -.
DR   GeneID; 496050; -.
DR   KEGG; xla:496050; -.
DR   CTD; 496050; -.
DR   Xenbase; XB-GENE-5789603; rnf170.L.
DR   OMA; CRQEEQN; -.
DR   OrthoDB; 1563172at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 496050; Expressed in zone of skin and 19 other tissues.
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   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..257
FT                   /note="E3 ubiquitin-protein ligase RNF170"
FT                   /id="PRO_0000280703"
FT   TOPO_DOM        1..24
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         87..130
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   257 AA;  29484 MW;  4877E885BD2F3A09 CRC64;
     MADNQEERPH FPLDEGSIIE GVSDQVIVVV LLSFVAVGSL IYLLLRNDEQ NIHPENQDRV
     RAVREQLQNE QETPAPPRPQ FYSDMTCPVC LQQATFPVET NCGHLFCGSC IIAYWRYGTW
     LGAINCPICR QTVTLLFPLF GATDQEDAQN ILQEATGYNR RFSGQPRSLM DRIMDLPTLL
     RHAFREMFSV GGLFWMFRIR IVLCLLGALL YLVSPLDIIP EALFGILGFL DDLFVLFLLL
     IYISIMYREV VTQRLYR