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   03-AUG-2022, entry version 83.
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}.
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DR   EMBL; BC070590; AAH70590.1; -; mRNA.
DR   RefSeq; NP_001084782.1; NM_001091313.1.
DR   AlphaFoldDB; Q6NRX0; -.
DR   SMR; Q6NRX0; -.
DR   DNASU; 431819; -.
DR   GeneID; 431819; -.
DR   KEGG; xla:431819; -.
DR   CTD; 431819; -.
DR   Xenbase; XB-GENE-972107; rnf149.L.
DR   OMA; NEEHYGN; -.
DR   OrthoDB; 1487241at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 431819; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; cd16804; RING-H2_RNF149; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR042712; RNF149_RING-H2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 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