ZNRF1_BOVIN
ID ZNRF1_BOVIN Reviewed; 227 AA.
AC F1MM41;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=E3 ubiquitin-protein ligase ZNRF1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ZNRF1;
DE AltName: Full=Zinc/RING finger protein 1;
GN Name=ZNRF1;
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 that mediates the ubiquitination
CC of AKT1 and GLUL, thereby playing a role in neuron cells
CC differentiation. Plays a role in the establishment and maintenance of
CC neuronal transmission and plasticity. Regulates Schwann cells
CC differentiation by mediating ubiquitination of GLUL. Promotes
CC degeneration by mediating 'Lys-48'-linked polyubiquitination and
CC subsequent degradation of AKT1 in axons: degradation of AKT1 prevents
CC AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and
CC phosphorylation of DPYSL2/CRMP2 followed by destabilization of
CC microtubule assembly in axons (By similarity). {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 AKT1, GLUL and TUBB2A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}. Lysosome {ECO:0000250}.
CC Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC Note=Associated with synaptic vesicle membranes in neurons.
CC {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
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DR EMBL; DAAA02045987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179139.1; NM_001192210.1.
DR RefSeq; XP_005218391.1; XM_005218334.3.
DR RefSeq; XP_005218392.1; XM_005218335.3.
DR RefSeq; XP_005218393.1; XM_005218336.3.
DR RefSeq; XP_005218394.1; XM_005218337.2.
DR AlphaFoldDB; F1MM41; -.
DR SMR; F1MM41; -.
DR STRING; 9913.ENSBTAP00000046062; -.
DR PaxDb; F1MM41; -.
DR PRIDE; F1MM41; -.
DR Ensembl; ENSBTAT00000086698; ENSBTAP00000064184; ENSBTAG00000034689.
DR GeneID; 509076; -.
DR KEGG; bta:509076; -.
DR CTD; 84937; -.
DR VEuPathDB; HostDB:ENSBTAG00000034689; -.
DR VGNC; VGNC:37363; ZNRF1.
DR eggNOG; KOG0801; Eukaryota.
DR GeneTree; ENSGT00940000159278; -.
DR HOGENOM; CLU_062700_0_1_1; -.
DR InParanoid; F1MM41; -.
DR OMA; YNVRTQR; -.
DR OrthoDB; 1256682at2759; -.
DR TreeFam; TF317681; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000034689; Expressed in thymus and 105 other tissues.
DR ExpressionAtlas; F1MM41; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cytoplasmic vesicle; 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..227
FT /note="E3 ubiquitin-protein ligase ZNRF1"
FT /id="PRO_0000415578"
FT ZN_FING 184..225
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..10
FT /note="Required for endosomal and lysosomal localization
FT and myristoylation"
FT /evidence="ECO:0000250"
FT REGION 77..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND25"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND25"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND25"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 227 AA; 23712 MW; 827D7B79485A015B CRC64;
MGGKQSTAAR SRGPFPGVST DDSAVPPPGG APHFGHYRAG GGAMGLRSRS VSSVAGMGMD
PSSAGGVSFG LYTPASRGAG DAERAPGSGG SASDSTYAHG NGYQETGGGH HRDGMLYLGS
RASLADALPL HIAPRWFSSH SGFKCPICSK SVASDEMEMH FIMCLSKPRL SYNDDVLTKD
AGECVICLEE LLQGDTIARL PCLCIYHKSC IDSWFEVNRS CPEHPAD
