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RN170_BOVIN
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   03-AUG-2022, entry version 59.
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. {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.ENSBTAP00000044412; -.
DR   PaxDb; F1MK05; -.
DR   PRIDE; F1MK05; -.
DR   eggNOG; KOG2164; Eukaryota.
DR   HOGENOM; CLU_072335_0_0_1; -.
DR   InParanoid; F1MK05; -.
DR   OrthoDB; 1563172at2759; -.
DR   TreeFam; TF328342; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; 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   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   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
 
 
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