ID A0A1L8GTD7_XENLA Unreviewed; 572 AA.
AC A0A1L8GTD7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=arih1.S {ECO:0000313|RefSeq:XP_018111094.1,
GN ECO:0000313|RefSeq:XP_018111095.1,
GN ECO:0000313|Xenbase:XB-GENE-17344895};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018111094.1};
RN [1] {ECO:0000313|RefSeq:XP_018111094.1, ECO:0000313|RefSeq:XP_018111095.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|Proteomes:UP000186698,
RC ECO:0000313|RefSeq:XP_018111094.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018111094.1,
RC ECO:0000313|RefSeq:XP_018111095.1};
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
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. E3 ubiquitin-
CC protein ligase activity is activated upon binding to neddylated cullin-
CC RING ubiquitin ligase complexes. {ECO:0000256|ARBA:ARBA00060357}.
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:0000256|ARBA:ARBA00001798};
CC -!- SUBUNIT: Interacts (via the first RING-type zinc finger) with ube2l3.
CC Associates with cullin-RING ubiquitin ligase (CRL) complexes containing
CC neddylated cullin. {ECO:0000256|ARBA:ARBA00063741}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR RefSeq; XP_018111094.1; XM_018255605.2.
DR RefSeq; XP_018111095.1; XM_018255606.2.
DR STRING; 8355.A0A1L8GTD7; -.
DR PaxDb; 8355-A0A1L8GTD7; -.
DR GeneID; 108712991; -.
DR KEGG; xla:108712991; -.
DR AGR; Xenbase:XB-GENE-17344895; -.
DR CTD; 108712991; -.
DR Xenbase; XB-GENE-17344895; arih1.S.
DR OMA; HRFCMIC; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 108712991; Expressed in testis and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16626; RING-HC_RBR_HHARI; 1.
DR FunFam; 1.20.120.1750:FF:000002; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
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; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 197..408
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 201..249
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 90..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..107
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 66626 MW; 5A29D3B000055062 CRC64;
MTYFSPVENS TSKLHINIQF FLNCHLGKPL LNQEPLSGLF CQLNMDSDEG YNYEFDDEEE
CSEDSGADEH EDELDLGEVE LVEAGLSGSE RAGLCGDGGG SALGPGPGEE DEDYRYEVLT
AEQILQHMVE CIREVNEVIQ NPATITRILL SHFNWDKEKL MERYFDGNLE KLFSECHVIN
PSKKSRTRQM NTRSSAQDMS CQICYLNYPN AYFTGLECGH KFCMQCWGEY LTTKIIEEGM
GQTISCPAHG CDILVDDNTV MRLITDSKVK LKYQHLITNS FVECNRLLKW CPAPDCHHVV
KVQYPDAKPV RCKCGRQFCF NCGENWHDPI KCKWLRKWIK KCDDDSETSN WIAANTKECP
KCHVTIEKDG GCNHMVCRNQ NCKAEFCWVC LGPWEPHGSA WYNCNRYNED DAKAARDAQE
RSRAALQRYL FYCNRYMNHM QSLRFEHKLY AQVKQKMEEM QQHNMSWIEV QFLKKAVDVL
CQCRSTLMYT YVFAFYLKKN NQSIIFENNQ ADLENATEVL SGYLERDISQ DSLQDIKQKV
QDKYRYCESR RRVLLLHVHE GYEKDLWEYI ED
//
