RN170_MOUSE
ID RN170_MOUSE Reviewed; 286 AA.
AC Q8CBG9; A6H618; Q3U796; Q78QX6; Q8C8S1; Q8C9I0; Q8K0H6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Brain cortex, Cerebellum, Retina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH ERLIN1/ERLIN2 COMPLEX AND ITPR1, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF CYS-130 AND HIS-132.
RX PubMed=21610068; DOI=10.1074/jbc.m111.251983;
RA Lu J.P., Wang Y., Sliter D.A., Pearce M.M., Wojcikiewicz R.J.;
RT "RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase,
RT mediates inositol 1,4,5-trisphosphate receptor ubiquitination and
RT degradation.";
RL J. Biol. Chem. 286:24426-24433(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that 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:0000269|PubMed:21610068}.
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:0000269|PubMed:21610068}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21610068}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21610068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CBG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CBG9-2; Sequence=VSP_023858;
CC Name=3;
CC IsoId=Q8CBG9-3; Sequence=VSP_023861, VSP_023864;
CC Name=4;
CC IsoId=Q8CBG9-4; Sequence=VSP_023859, VSP_023863;
CC Name=5;
CC IsoId=Q8CBG9-5; Sequence=VSP_023860, VSP_023862;
CC -!- CAUTION: It is uncertain whether Met-1 or Met-30 is the initiator.
CC Initiation at Met-30 is supported by sequence similarity with mammalian
CC orthologs and by a Kozak context more favorable compared to that at
CC Met-1. {ECO:0000305}.
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DR EMBL; AK036051; BAC29287.1; -; mRNA.
DR EMBL; AK042063; BAC31147.1; -; mRNA.
DR EMBL; AK044579; BAC31988.1; -; mRNA.
DR EMBL; AK080591; BAC37951.1; -; mRNA.
DR EMBL; AK152760; BAE31474.1; -; mRNA.
DR EMBL; CH466580; EDL32805.1; -; Genomic_DNA.
DR EMBL; BC031383; AAH31383.1; -; mRNA.
DR EMBL; BC114210; AAI14211.1; -; mRNA.
DR EMBL; BC138930; AAI38931.1; -; mRNA.
DR EMBL; BC145718; AAI45719.1; -; mRNA.
DR CCDS; CCDS90380.1; -. [Q8CBG9-2]
DR RefSeq; NP_084241.1; NM_029965.2.
DR RefSeq; XP_006509278.1; XM_006509215.3.
DR RefSeq; XP_006509279.1; XM_006509216.3.
DR RefSeq; XP_006509280.1; XM_006509217.3.
DR RefSeq; XP_006509281.1; XM_006509218.3.
DR AlphaFoldDB; Q8CBG9; -.
DR BioGRID; 218881; 4.
DR STRING; 10090.ENSMUSP00000014022; -.
DR PhosphoSitePlus; Q8CBG9; -.
DR SwissPalm; Q8CBG9; -.
DR MaxQB; Q8CBG9; -.
DR PaxDb; Q8CBG9; -.
DR PeptideAtlas; Q8CBG9; -.
DR PRIDE; Q8CBG9; -.
DR ProteomicsDB; 300445; -. [Q8CBG9-1]
DR ProteomicsDB; 300446; -. [Q8CBG9-2]
DR ProteomicsDB; 300447; -. [Q8CBG9-3]
DR ProteomicsDB; 300448; -. [Q8CBG9-4]
DR DNASU; 77733; -.
DR Ensembl; ENSMUST00000014022; ENSMUSP00000014022; ENSMUSG00000013878. [Q8CBG9-1]
DR Ensembl; ENSMUST00000110575; ENSMUSP00000106204; ENSMUSG00000013878. [Q8CBG9-3]
DR Ensembl; ENSMUST00000110579; ENSMUSP00000106208; ENSMUSG00000013878. [Q8CBG9-5]
DR Ensembl; ENSMUST00000153528; ENSMUSP00000118689; ENSMUSG00000013878. [Q8CBG9-2]
DR Ensembl; ENSMUST00000209300; ENSMUSP00000147842; ENSMUSG00000013878. [Q8CBG9-4]
DR GeneID; 77733; -.
DR KEGG; mmu:77733; -.
DR UCSC; uc009lhl.1; mouse. [Q8CBG9-3]
DR UCSC; uc009lhm.1; mouse. [Q8CBG9-1]
DR UCSC; uc009lhp.1; mouse. [Q8CBG9-2]
DR CTD; 81790; -.
DR MGI; MGI:1924983; Rnf170.
DR VEuPathDB; HostDB:ENSMUSG00000013878; -.
DR eggNOG; KOG2164; Eukaryota.
DR GeneTree; ENSGT00390000017123; -.
DR HOGENOM; CLU_072335_0_0_1; -.
DR InParanoid; Q8CBG9; -.
DR OMA; CRQEEQN; -.
DR OrthoDB; 1563172at2759; -.
DR PhylomeDB; Q8CBG9; -.
DR TreeFam; TF328342; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 77733; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf170; mouse.
DR PRO; PR:Q8CBG9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CBG9; protein.
DR Bgee; ENSMUSG00000013878; Expressed in secondary oocyte and 226 other tissues.
DR ExpressionAtlas; Q8CBG9; baseline and differential.
DR Genevisible; Q8CBG9; MM.
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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..286
FT /note="E3 ubiquitin-protein ligase RNF170"
FT /id="PRO_0000280701"
FT TOPO_DOM 1..52
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 115..158
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 28..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023858"
FT VAR_SEQ 136..142
FT /note="GSCIIAY -> VLQLFPH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023859"
FT VAR_SEQ 136..140
FT /note="GSCII -> ENCGF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023860"
FT VAR_SEQ 137..216
FT /note="SCIIAYWRYGSWLGAISCPICRQTVTLLLTVFGEDDQSQDVIRLRQDVNDYN
FT RRFSGQPRSIMERIMDLPTLLRHAFREV -> EQIMSDLVRVTSLRPLWIGSGLDCSFS
FT FYHIYVLRRVDCFTSPALVATQIIAYCLVYSILRSEDIAQLVECLAIMQKPWA (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023861"
FT VAR_SEQ 141..286
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023862"
FT VAR_SEQ 143..286
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023863"
FT VAR_SEQ 217..286
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023864"
FT MUTAGEN 130
FT /note="C->S: Loss of E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:21610068"
FT MUTAGEN 132
FT /note="H->S: Loss of E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:21610068"
FT CONFLICT 105
FT /note="A -> V (in Ref. 1; BAC31147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 33414 MW; 17294042B9C5CD49 CRC64;
MQRYWRFQDN KIQDICFGVL GESWIQRPVM ARYYSEGQSL QQDDSFIEGV SDQVLVAVVV
SLALTATLLY ALLRNVQQNI HPENQELVRV LREQFQTEQD VPAPARQQFY TEMYCPICLH
QASFPVETNC GHLFCGSCII AYWRYGSWLG AISCPICRQT VTLLLTVFGE DDQSQDVIRL
RQDVNDYNRR FSGQPRSIME RIMDLPTLLR HAFREVFSVG GLFWMFRIRI MLCLMGAFFY
LISPLDFVPE ALFGILGFLD DFFVIFLLLI YISIMYREVI TQRLTR
