ZNRF2_MOUSE
ID ZNRF2_MOUSE Reviewed; 238 AA.
AC Q71FD5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=E3 ubiquitin-protein ligase ZNRF2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ZNRF2;
DE AltName: Full=Zinc/RING finger protein 2;
GN Name=Znrf2;
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], AND TISSUE SPECIFICITY.
RX PubMed=14561866; DOI=10.1523/jneurosci.23-28-09385.2003;
RA Araki T., Milbrandt J.;
RT "ZNRF proteins constitute a family of presynaptic E3 ubiquitin ligases.";
RL J. Neurosci. 23:9385-9394(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-24; SER-75; SER-107;
RP SER-110 AND SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in the establishment and maintenance of
CC neuronal transmission and plasticity via its ubiquitin ligase activity.
CC E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating
CC enzyme in the form of a thioester and then directly transfer the
CC ubiquitin to targeted substrates. {ECO:0000250}.
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: Interacts with UBE2N. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q8NHG8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NHG8}. Lysosome
CC membrane {ECO:0000250|UniProtKB:Q8NHG8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NHG8}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8NHG8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NHG8}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in the nervous system.
CC Expression is more intense in the granular cell layer of hippocampus,
CC Purkinje cell layer of the cerebellum and the granular cell layer of
CC the olfactory bulb. Detected in sensory neurons but not expressed in
CC sympatic or enteric neurons. Expressed in testis, adipose tissue,
CC columnar epithelial cells of the gut. {ECO:0000269|PubMed:14561866}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
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DR EMBL; AF513708; AAQ08116.1; -; mRNA.
DR CCDS; CCDS20159.1; -.
DR RefSeq; NP_954594.1; NM_199143.2.
DR AlphaFoldDB; Q71FD5; -.
DR SMR; Q71FD5; -.
DR STRING; 10090.ENSMUSP00000078795; -.
DR iPTMnet; Q71FD5; -.
DR PhosphoSitePlus; Q71FD5; -.
DR EPD; Q71FD5; -.
DR jPOST; Q71FD5; -.
DR MaxQB; Q71FD5; -.
DR PaxDb; Q71FD5; -.
DR PeptideAtlas; Q71FD5; -.
DR PRIDE; Q71FD5; -.
DR ProteomicsDB; 275043; -.
DR Antibodypedia; 35132; 121 antibodies from 25 providers.
DR DNASU; 387524; -.
DR Ensembl; ENSMUST00000079869; ENSMUSP00000078795; ENSMUSG00000058446.
DR GeneID; 387524; -.
DR KEGG; mmu:387524; -.
DR UCSC; uc009cae.2; mouse.
DR CTD; 223082; -.
DR MGI; MGI:1196246; Znrf2.
DR VEuPathDB; HostDB:ENSMUSG00000058446; -.
DR eggNOG; KOG0801; Eukaryota.
DR GeneTree; ENSGT00940000159017; -.
DR HOGENOM; CLU_062700_2_0_1; -.
DR InParanoid; Q71FD5; -.
DR OMA; SEEMDLH; -.
DR OrthoDB; 1256682at2759; -.
DR PhylomeDB; Q71FD5; -.
DR TreeFam; TF317681; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 387524; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Znrf2; mouse.
DR PRO; PR:Q71FD5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q71FD5; protein.
DR Bgee; ENSMUSG00000058446; Expressed in cortical plate and 256 other tissues.
DR ExpressionAtlas; Q71FD5; baseline and differential.
DR Genevisible; Q71FD5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Endosome; Lipoprotein; Lysosome; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; Reference proteome; Synapse;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..238
FT /note="E3 ubiquitin-protein ligase ZNRF2"
FT /id="PRO_0000277804"
FT ZN_FING 195..236
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHG8"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHG8"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHG8"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 238 AA; 23705 MW; 40422C7ECCC173CC CRC64;
MGAKQSGPAA NGRTRAYSGS DLPSGTGSGG GGADGARAAR FAAPVSGAQQ PSASAGAAAA
AAAAASAPAA PRSRSLGGAV GSASGGRAAQ SAFSIPSAGG GGGPYGSQDS VHSSPEDSVG
ARDRDRPAGG GPGGPRLVIG SLPAHLSPHL FGGFKCPVCS KFVPSDEMDL HLVMCLTKPR
ITYNEDVLSK DTGECAICLE ELQQGDTIAR LPCLCIYHKG CIDEWFEVNR SCPEHPSD
