RNF26_MOUSE
ID RNF26_MOUSE Reviewed; 424 AA.
AC Q8BUH7; F6SS41; Q5PR90; Q8BZY8; Q99KC1;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=E3 ubiquitin-protein ligase RNF26 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9BY78};
DE AltName: Full=RING finger protein 26 {ECO:0000305};
GN Name=Rnf26 {ECO:0000312|MGI:MGI:2388131};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Lung, Testis, 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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Eye, and Mammary tumor;
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays a key role in endosome
CC organization by retaining vesicles in the perinuclear cloud. Acts as a
CC platform for perinuclear positioning of the endosomal system by
CC mediating ubiquitination of SQSTM1 through interaction with the
CC ubiquitin conjugating enzyme UBE2J1. Ubiquitinated SQSTM1 attracts
CC specific vesicle-associated adapters, forming a molecular bridge that
CC restrains cognate vesicles in the perinuclear region and organizes the
CC endosomal pathway for efficient cargo transport. Also acts as a
CC regulator of type I interferon production in response to viral
CC infection by mediating the formation of 'Lys-11'-linked polyubiquitin
CC chains on TMEM173/STING, leading to stabilize TMEM173/STING. Also
CC required to limit type I interferon response by promoting autophagic
CC degradation of IRF3. {ECO:0000250|UniProtKB:Q9BY78}.
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; Evidence={ECO:0000250|UniProtKB:Q9BY78};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BY78}.
CC -!- SUBUNIT: Interacts with INCA1. Interacts with TMEM43, ENDOD1, TMEM33
CC and TMED1 to form a complex capable of modulating innate immune
CC signaling through the cGAS-STING pathway. Interacts with UBE2J1; this
CC interaction is important for SQSTM1 ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BY78}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BY78}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BUH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BUH7-2; Sequence=VSP_042390, VSP_042391;
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DR EMBL; AK033164; BAC28179.1; -; mRNA.
DR EMBL; AK085078; BAC39357.1; -; mRNA.
DR EMBL; AK157821; BAE34211.1; -; mRNA.
DR EMBL; AK169538; BAE41218.1; -; mRNA.
DR EMBL; AC148328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004739; AAH04739.1; -; mRNA.
DR EMBL; BC063251; AAH63251.1; -; mRNA.
DR EMBL; BC086757; AAH86757.1; -; mRNA.
DR CCDS; CCDS23096.1; -. [Q8BUH7-1]
DR RefSeq; NP_717095.2; NM_153762.3. [Q8BUH7-1]
DR AlphaFoldDB; Q8BUH7; -.
DR STRING; 10090.ENSMUSP00000110478; -.
DR iPTMnet; Q8BUH7; -.
DR PhosphoSitePlus; Q8BUH7; -.
DR PaxDb; Q8BUH7; -.
DR PRIDE; Q8BUH7; -.
DR ProteomicsDB; 301622; -. [Q8BUH7-1]
DR DNASU; 213211; -.
DR Ensembl; ENSMUST00000056328; ENSMUSP00000110478; ENSMUSG00000053128. [Q8BUH7-1]
DR Ensembl; ENSMUST00000065379; ENSMUSP00000070060; ENSMUSG00000053128. [Q8BUH7-1]
DR Ensembl; ENSMUST00000162126; ENSMUSP00000123938; ENSMUSG00000111409. [Q8BUH7-1]
DR Ensembl; ENSMUST00000185479; ENSMUSP00000140405; ENSMUSG00000111409. [Q8BUH7-1]
DR GeneID; 213211; -.
DR KEGG; mmu:213211; -.
DR UCSC; uc009pbu.2; mouse. [Q8BUH7-1]
DR CTD; 79102; -.
DR MGI; MGI:2388131; Rnf26.
DR VEuPathDB; HostDB:ENSMUSG00000053128; -.
DR VEuPathDB; HostDB:ENSMUSG00000111409; -.
DR eggNOG; KOG4265; Eukaryota.
DR GeneTree; ENSGT00390000016584; -.
DR HOGENOM; CLU_057705_0_0_1; -.
DR InParanoid; Q8BUH7; -.
DR OMA; WTPCQLL; -.
DR OrthoDB; 670633at2759; -.
DR PhylomeDB; Q8BUH7; -.
DR TreeFam; TF331813; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 213211; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Rnf26; mouse.
DR PRO; PR:Q8BUH7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BUH7; protein.
DR Bgee; ENSMUSG00000053128; Expressed in tracheobronchial tree and 110 other tissues.
DR ExpressionAtlas; Q8BUH7; baseline and differential.
DR Genevisible; Q8BUH7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0032479; P:regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16788; mRING-HC-C3HC5_RNF26; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040089; RNF26_mRING-HC-C3HC5.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript 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..424
FT /note="E3 ubiquitin-protein ligase RNF26"
FT /id="PRO_0000415816"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 371..413
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 144..181
FT /note="VAYVINSLVNICLISTQNFFSLVLALWDAVTGPLWRMT -> EPQPTTGQLA
FT KSGRSTRSPPRWPQEGVLSQDPATGHSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042390"
FT VAR_SEQ 182..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042391"
FT CONFLICT 86
FT /note="L -> V (in Ref. 3; AAH04739)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="S -> G (in Ref. 3; AAH04739)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="P -> H (in Ref. 1; BAC28179)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="T -> A (in Ref. 3; AAH04739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46914 MW; 919A8F83E1B515B9 CRC64;
MEAVYLVVNG VGLVLDLLTL MLDLNFLLVS SLLATLAWLL AFIYNLPHTV LTSLLHLGRG
FLLSLLALVE AVVRFTFGGL QALGTLLYSC YSGLESLKLL GHLASHGALR SREFLNRGIL
NMVSNGHALL RQACDICAIA MSLVAYVINS LVNICLISTQ NFFSLVLALW DAVTGPLWRM
TDVVAAFLAH ISSSAVAMAI LLWTPCQLAL ELLASAARLL ASCVVFHLTG LVLLACVLAV
ILIVLHPEQT LRLATQALSQ LHARPSYHRL WEDIVRLTRL PLGLEAWRRV WSRSLQLASW
PNRGGAPGAP QGGPRRVFSA RIQPQDTPPE AEEEVIRTAP ARGREQLNED EPAAGQDPWK
LLKEQEERKK CVICQDQSKT VLLLPCRHLC LCQACTEILM RHPVYHRNCP LCRRSILQTL
NVYL
