ARI1_BOVIN
ID ARI1_BOVIN Reviewed; 555 AA.
AC A2VEA3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=E3 ubiquitin-protein ligase ARIH1;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5};
DE AltName: Full=Protein ariadne-1 homolog;
DE Short=ARI-1;
DE AltName: Full=RING-type E3 ubiquitin transferase ARIH1 {ECO:0000305};
GN Name=ARIH1;
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 MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination
CC of target proteins together with ubiquitin-conjugating enzyme E2
CC UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working
CC together with cullin-RING ubiquitin ligase (CRL) complexes and
CC initiating ubiquitination of CRL substrates: associates with CRL
CC complexes and specifically mediates addition of the first ubiquitin on
CC CRLs targets. The initial ubiquitin is then elongated by CDC34/UBE2R1
CC and UBE2R2. E3 ubiquitin-protein ligase activity is activated upon
CC binding to neddylated cullin-RING ubiquitin ligase complexes. Plays a
CC role in protein translation in response to DNA damage by mediating
CC ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are
CC however unclear. According to a report, EIF4E2 ubiquitination leads to
CC promote EIF4E2 cap-binding and protein translation arrest. According to
CC another report EIF4E2 ubiquitination leads to its subsequent
CC degradation. Acts as the ligase involved in ISGylation of EIF4E2. In
CC vitro, controls the degradation of the LINC (LInker of Nucleoskeleton
CC and Cytoskeleton) complex member SUN2 and may therefore have a role in
CC the formation and localization of the LINC complex, and as a
CC consequence, may act in nuclear subcellular localization and nuclear
CC morphology. {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5};
CC -!- ACTIVITY REGULATION: Autoinhibited by the ariadne domain, which masks
CC the second RING-type zinc finger that contains the active site and
CC inhibits the E3 activity. Inhibition is relieved upon binding to
CC neddylated cullin-RING ubiquitin ligase complexes, which activate the
CC E3 ligase activity of ARIH1. {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via the first RING-type zinc finger) with UBE2L3.
CC Associates with cullin-RING ubiquitin ligase (CRL) complexes containing
CC CUL1, CUL2 and CUL3. Interacts with neddylated CUL1. Interacts with
CC neddylated CUL2. Interacts with neddylated CUL3. Interacts with
CC neddylated CUL4A. {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q9Y4X5}. Note=Mainly cytoplasmic. Present in
CC Lewy body. {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING-type zinc finger, but
CC require an obligate trans-thiolation step during the ubiquitin
CC transfer, requiring a conserved active site Cys residue in the second
CC RING-type zinc finger. The active site probably forms a thioester
CC intermediate with ubiquitin taken from the active-site cysteine of the
CC E2 before ultimately transferring it to a Lys residue on the substrate.
CC {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- DOMAIN: The Ariadne domain inhibits activity by masking the second
CC RING-type zinc finger that contains the active site.
CC {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000305}.
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DR EMBL; BC133645; AAI33646.1; -; mRNA.
DR RefSeq; NP_001075183.1; NM_001081714.2.
DR AlphaFoldDB; A2VEA3; -.
DR BMRB; A2VEA3; -.
DR SMR; A2VEA3; -.
DR STRING; 9913.ENSBTAP00000008822; -.
DR PaxDb; A2VEA3; -.
DR PRIDE; A2VEA3; -.
DR Ensembl; ENSBTAT00000008822; ENSBTAP00000008822; ENSBTAG00000006708.
DR GeneID; 508410; -.
DR KEGG; bta:508410; -.
DR CTD; 25820; -.
DR VEuPathDB; HostDB:ENSBTAG00000006708; -.
DR VGNC; VGNC:26133; ARIH1.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000155744; -.
DR HOGENOM; CLU_009823_4_2_1; -.
DR InParanoid; A2VEA3; -.
DR OMA; CAAHACD; -.
DR OrthoDB; 469819at2759; -.
DR TreeFam; TF300805; -.
DR Reactome; R-BTA-1169408; ISG15 antiviral mechanism.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000006708; Expressed in spermatid and 106 other tissues.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097413; C:Lewy body; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..555
FT /note="E3 ubiquitin-protein ligase ARIH1"
FT /id="PRO_0000330477"
FT ZN_FING 184..234
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 254..315
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 342..373
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..151
FT /note="UBA-like"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4X5"
FT REGION 180..391
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 406..555
FT /note="Ariadne domain"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4X5"
FT COMPBIAS 1..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1K5"
SQ SEQUENCE 555 AA; 64017 MW; 0A52A06862EEEDA5 CRC64;
MDSDEGYNYE FDEDEECSEE DSGAEEEEDE DDDEPDDDNL DLGEVELVEP GLGVGGERDG
LLCGETGGGG GSALGPGGGG GGGGGGGGPG HEQEEDYRYE VLTAEQILQH MVECIREVNE
VIQNPATITR ILLSHFNWDK EKLMERYFDG NLEKLFAECH VINPSKKSRT RQMNTRSSAQ
DMPCQICYLN YPNSYFTGLE CGHKFCMQCW SEYLTTKIME EGMGQTISCP AHGCDILVDD
NTVMRLITDS KVKLKYQHLI TNSFVECNRL LKWCPAPDCH HVVKVQYPDA KPVRCKCGRQ
FCFNCGENWH DPVKCKWLKK WIKKCDDDSE TSNWIAANTK ECPKCHVTIE KDGGCNHMVC
RNQNCKAEFC WVCLGPWEPH GSAWYNCNRY NEDDAKAARD AQERSRAALQ RYLFYCNRYM
NHMQSLRFEH KLYAQVKQKM EEMQQHNMSW IEVQFLKKAV DVLCQCRATL MYTYVFAFYL
KKNNQSIIFE NNQADLENAT EVLSGYLERD ISQDSLQDIK QKVQDKYRYC ESRRRVLLQH
VHEGYEKDLW EYIED
