ID RN149_XENLA Reviewed; 397 AA.
AC Q6NRX0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=E3 ubiquitin-protein ligase RNF149;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 149;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF149 {ECO:0000305};
DE Flags: Precursor;
GN Name=rnf149;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its
CC proteasomal degradation. {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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC070590; AAH70590.1; -; mRNA.
DR RefSeq; NP_001084782.1; NM_001091313.1.
DR AlphaFoldDB; Q6NRX0; -.
DR SMR; Q6NRX0; -.
DR GlyCosmos; Q6NRX0; 3 sites, No reported glycans.
DR DNASU; 431819; -.
DR GeneID; 431819; -.
DR KEGG; xla:431819; -.
DR AGR; Xenbase:XB-GENE-972107; -.
DR CTD; 431819; -.
DR Xenbase; XB-GENE-972107; rnf149.L.
DR OMA; GPDSEWT; -.
DR OrthoDB; 5474929at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 431819; Expressed in zone of skin and 19 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd02122; PA_GRAIL_like; 1.
DR CDD; cd16804; RING-H2_RNF149; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR042712; RNF149_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF30; RING FINGER PROTEIN 149; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..397
FT /note="E3 ubiquitin-protein ligase RNF149"
FT /id="PRO_0000261613"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 83..170
FT /note="PA"
FT ZN_FING 264..305
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 39..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 43471 MW; 818B8CAC2D6D3800 CRC64;
MLRWLCLYSA LCALTHGSSA RSLEWFTALV RTEYTEPLTN SSVTGSTESG RYGDSSPKES
VKGFVGYPRD PWQLEGCHPD TQYIVPGTSA AAAAGPDSEW TQPWIALVAR GGCTFKEKVF
NAANRGASAV VIYNEAKSGN ATVSMSHLGT GNTVVIMVSY PKGMEIMEPL RRDIPVKMVI
TVGTRHVQEF ISGQSVVFVA IAFITMMIIS LAWLIFYYIQ RFLYTGAQCG NQSNRKETKK
AISQLQLHRV KKGEKGIDID AENCAVCIEN YKTKDLVRIL PCKHIFHRLC IDPWLIEHRT
CPMCKLDVIK ALGFWVEPEE TLDIHVPDSI AGSSLSIGTV SITQEESRSE GNNLPSSSTG
SSLQQSNSVK DDAGETTALL DDPGNDNAAA THTQDSH
//
