NEUL3_MOUSE
ID NEUL3_MOUSE Reviewed; 254 AA.
AC Q8CJC5; Q8BS05;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=E3 ubiquitin-protein ligase NEURL3;
DE EC=2.3.2.27;
DE AltName: Full=Lung-inducible neuralized-related C3CH4 RING domain protein;
DE AltName: Full=Neuralized-like protein 3;
DE AltName: Full=RING-type E3 ubiquitin transferase NEURL3 {ECO:0000305};
GN Name=Neurl3; Synonyms=Lincr;
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 [MRNA] (ISOFORM 1), AND INDUCTION.
RC STRAIN=Swiss Webster;
RX PubMed=12169584; DOI=10.1152/ajplung.00496.2001;
RA Smith J.B., Nguyen T.T., Hughes H.J., Herschman H.R., Widney D.P.,
RA Bui K.C., Rovai L.E.;
RT "Glucocorticoid-attenuated response genes induced in the lung during
RT endotoxemia.";
RL Am. J. Physiol. 283:L636-L647(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Spleen, and Vein;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15936721; DOI=10.1016/j.bbrc.2005.05.102;
RA Hu Y., Nguyen T.T., Bui K.C., Demello D.E., Smith J.B.;
RT "A novel inflammation-induced ubiquitin E3 ligase in alveolar type II
RT cells.";
RL Biochem. Biophys. Res. Commun. 333:253-263(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Seems to utilize UBE2E1. In
CC vitro, generates polyubiquitin chains via non-canonical lysine residues
CC suggesting that it is not involved in tagging substrates for
CC proteasomal degradation. {ECO:0000269|PubMed:15936721}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CJC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CJC5-2; Sequence=VSP_032400, VSP_032401;
CC -!- TISSUE SPECIFICITY: Expressed in alveolar epithelial type II cells.
CC {ECO:0000269|PubMed:15936721}.
CC -!- INDUCTION: Induced in lung during endotoxemia. By LPS and inflammatory
CC cytokines in alveolar epithelial type II cells.
CC {ECO:0000269|PubMed:12169584, ECO:0000269|PubMed:15936721}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30757.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF321278; AAN16205.1; -; mRNA.
DR EMBL; AK040949; BAC30757.1; ALT_INIT; mRNA.
DR EMBL; AK156207; BAE33626.1; -; mRNA.
DR EMBL; BC056622; AAH56622.1; -; mRNA.
DR CCDS; CCDS14875.1; -. [Q8CJC5-1]
DR RefSeq; NP_700457.1; NM_153408.2. [Q8CJC5-1]
DR RefSeq; XP_006495911.1; XM_006495848.3. [Q8CJC5-1]
DR AlphaFoldDB; Q8CJC5; -.
DR SMR; Q8CJC5; -.
DR STRING; 10090.ENSMUSP00000055437; -.
DR iPTMnet; Q8CJC5; -.
DR PhosphoSitePlus; Q8CJC5; -.
DR MaxQB; Q8CJC5; -.
DR PaxDb; Q8CJC5; -.
DR PRIDE; Q8CJC5; -.
DR ProteomicsDB; 287384; -. [Q8CJC5-1]
DR ProteomicsDB; 287385; -. [Q8CJC5-2]
DR Antibodypedia; 74844; 27 antibodies from 8 providers.
DR DNASU; 214854; -.
DR Ensembl; ENSMUST00000056946; ENSMUSP00000055437; ENSMUSG00000047180. [Q8CJC5-1]
DR GeneID; 214854; -.
DR KEGG; mmu:214854; -.
DR UCSC; uc007aps.1; mouse. [Q8CJC5-1]
DR UCSC; uc007apt.1; mouse. [Q8CJC5-2]
DR CTD; 93082; -.
DR MGI; MGI:2429944; Neurl3.
DR VEuPathDB; HostDB:ENSMUSG00000047180; -.
DR eggNOG; KOG4625; Eukaryota.
DR GeneTree; ENSGT00940000162540; -.
DR HOGENOM; CLU_090535_0_0_1; -.
DR InParanoid; Q8CJC5; -.
DR OMA; PVCRWEI; -.
DR OrthoDB; 1384219at2759; -.
DR PhylomeDB; Q8CJC5; -.
DR TreeFam; TF314368; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 214854; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8CJC5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CJC5; protein.
DR Bgee; ENSMUSG00000047180; Expressed in granulocyte and 76 other tissues.
DR ExpressionAtlas; Q8CJC5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IGI:MGI.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR037962; Neuralized.
DR InterPro; IPR006573; NHR_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12429; PTHR12429; 1.
DR Pfam; PF07177; Neuralized; 1.
DR SMART; SM00588; NEUZ; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51065; NHR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..254
FT /note="E3 ubiquitin-protein ligase NEURL3"
FT /id="PRO_0000325772"
FT DOMAIN 17..174
FT /note="NHR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT ZN_FING 197..236
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 173..195
FT /note="DPKANAWIRSGEPVPESEVISGE -> GETPWGPDTECGMETKVQMTSC
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032400"
FT VAR_SEQ 196..254
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032401"
FT CONFLICT 148
FT /note="D -> N (in Ref. 2; BAC30757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 28040 MW; A24DE91AC3C0E77E CRC64;
MGSLLSPEAN AEVPREALSF HGNATGAQVH LDDQRSTARR RSTFHDGIVF SQRPVWPGER
VALRVLRHEE GWCGGLRVGF TRLDPAQVAA SCLPPFVCPD LEEQSPTWAA LLPEGFVRAG
NVVCFWVNRR GWLFAKVNAG RPLLLRKDVL VQGAPLWAVM DVYGTTKAIE LLDPKANAWI
RSGEPVPESE VISGEECVIC FHNTANTRLM PCGHSHFCGS CAWHIFKDTA RCPICRWQIE
EVAVVSSLKA EEGS
