ID A0A8C6IEQ7_MUSSI Unreviewed; 484 AA.
AC A0A8C6IEQ7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=E3 ubiquitin-protein ligase ARIH1 {ECO:0000256|ARBA:ARBA00070156};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=E3 ubiquitin-protein ligase arih1 {ECO:0000256|ARBA:ARBA00070790};
DE AltName: Full=Protein ariadne-1 homolog {ECO:0000256|ARBA:ARBA00083021};
DE AltName: Full=UbcH7-binding protein {ECO:0000256|ARBA:ARBA00075923};
DE AltName: Full=Ubiquitin-conjugating enzyme E2-binding protein 1 {ECO:0000256|ARBA:ARBA00075721};
OS Mus spicilegus (Steppe mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10103 {ECO:0000313|Ensembl:ENSMSIP00000035297.1, ECO:0000313|Proteomes:UP000694415};
RN [1] {ECO:0000313|Ensembl:ENSMSIP00000035297.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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 CUL1, CUL2 and CUL3. Interacts with neddylated CUL1. Interacts with
CC neddylated CUL2. Interacts with neddylated CUL3. Interacts with
CC neddylated CUL4A. {ECO:0000256|ARBA:ARBA00064699}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR Ensembl; ENSMSIT00000044471.1; ENSMSIP00000035297.1; ENSMSIG00000029370.1.
DR GeneTree; ENSGT00940000155744; -.
DR Proteomes; UP000694415; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
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; 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 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:UP000694415};
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 110..320
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 114..161
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..90
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 55639 MW; F97C2B49C1E5AB52 CRC64;
MDSDEGYNYE FDEDEECSEE DSGAEEEEDD DEDEPDDDNL DLGEVELVEP GLGVGGERDG
LLCGETGGGG GSALGPGGGG GGGGGGGGPG HEQEEDYRYE VLTAEQILQH MVECIREVNE
VIQYFTGLEC GHKFCMQCWS EYLTTKIMEE GMGQTISCPA HGCDILVDDN TVMRLITDSK
VKLKYQHLIT NSFVECNRLL KWCPAPDCHH VVKVQYPDAK PVRCKCGRQF CFNCGENWHD
PVKCKWLKKW IKKCDDDSET SNWIAANTKE CPKCHVTIEK DGGCNHMVCR NQNCKAEFCW
VCLGPWEPHG SAWYNCNRYN EDDAKAARDA QERSRAALQR YLFYCNRYMN HMQSLRFEHK
LYAQVKQKME EMQQHNMSWI EVQFLKKAVD VLCQCRATLM YTYVFAFYLK KNNQSIIFEN
NQADLENATE VLSGYLERDI SQDSLQDIKQ KVQDKYRYCE SRRRVLLQHV HEGYEKDLWE
YIED
//
