RNF25_BOVIN
ID RNF25_BOVIN Reviewed; 458 AA.
AC Q5E9N3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=E3 ubiquitin-protein ligase RNF25;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 25;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF25 {ECO:0000305};
GN Name=RNF25;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of NKD2. Stimulates transcription
CC mediated by NF-kappa-B. {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 UBE2D2, and may also interact with UBE2E1 and
CC UBE2E3. Interacts with RELA and NKD2 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
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DR EMBL; BT020887; AAX08904.1; -; mRNA.
DR RefSeq; NP_001015575.1; NM_001015575.1.
DR AlphaFoldDB; Q5E9N3; -.
DR SMR; Q5E9N3; -.
DR STRING; 9913.ENSBTAP00000004972; -.
DR PaxDb; Q5E9N3; -.
DR PRIDE; Q5E9N3; -.
DR GeneID; 511571; -.
DR KEGG; bta:511571; -.
DR CTD; 64320; -.
DR eggNOG; KOG4445; Eukaryota.
DR InParanoid; Q5E9N3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
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:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039133; RNF25.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13198; PTHR13198; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..458
FT /note="E3 ubiquitin-protein ligase RNF25"
FT /id="PRO_0000056065"
FT DOMAIN 18..128
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT ZN_FING 135..201
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 267..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51236 MW; 377E65E6C6158A2D CRC64;
MAVSASVAAG DEDWVLPSEV EVLESIYLDE LQVVKGNGRS SPWEIYITLH PATAEDQDSQ
YVCFTLVLQV PTQYPHEVPQ ISIRNPRGLS DEQIHKISQA LSHVAEAGLG TAMLYELIEK
GKEILTDNNI PHGQCVICLY GFQEKEAFTK TPCYHYFRCH CLARYIQHME HELQAQGRER
EQERQHAAPE QAVGVQCPVC REPLVYDLAS LKAAPEPQQP MELYQPDAES LRQQEERKRL
YQRQQERGGI IDLEAERNRY FISLQQPPAP LEPESAIDVS RGSHQPSTLA TKPSTTSATH
TALSVSLPLA SQYTCEKTPG AGPHLPKLGE TQKAVLDPRR ASRGPWRQPE RRHLKGGECN
TLKGTSDTQK LQSPEGPLKE SMDLKPESHN QGGKGPPQDK GPGEWQGPPP RRTRDCAHWE
RAKNRTPASS YPRLPRGRGA YRPGPRREPV SLESEDGS
