ID   RN133_MACFA             Reviewed;         376 AA.
AC   Q95K04; Q95JW9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF133;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 133;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF133 {ECO:0000305};
GN   Name=RNF133; ORFNames=QtsA-11567, QtsA-13332;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RA   Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA   Sugano S.;
RT   "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT   libraries.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
CC   -!- FUNCTION: Has E3 ubiquitin-protein ligase activity.
CC       {ECO:0000250|UniProtKB:Q14B02}.
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: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q14B02}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q14B02}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q14B02}.
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DR   EMBL; AB070058; BAB63003.1; -; mRNA.
DR   EMBL; AB070023; BAB62968.1; -; mRNA.
DR   RefSeq; NP_001306501.1; NM_001319572.1.
DR   AlphaFoldDB; Q95K04; -.
DR   SMR; Q95K04; -.
DR   STRING; 9541.XP_005550690.1; -.
DR   GeneID; 102146898; -.
DR   CTD; 168433; -.
DR   eggNOG; KOG4628; Eukaryota.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003137; PA_domain.
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   Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..376
FT                   /note="E3 ubiquitin-protein ligase RNF133"
FT                   /id="PRO_0000247838"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          65..167
FT                   /note="PA"
FT   ZN_FING         256..297
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          328..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        262
FT                   /note="H -> L (in Ref. 1; BAB63003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="I -> F (in Ref. 1; BAB63003)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  42239 MW;  D44585F36F4E0C6E CRC64;
     MHLLKVGTWR NNTAFSWLIM FGVLWLVSQN CCRASVVWTA YMNISFHVGN HVLSELGETG
     VFGRSSTLKR VAGVIVPPEG KIQNACNPNT IFSRSKYSET WLALIERGGC TFTQKIKVAA
     EKGASGVIIY NFPGTGNQVF PMFHQAFEDV VVVMIGNLKG TEIFHLIKKG VLITAMVEVG
     RKHIIWMNHY LVSFVIVTTA TLAYFIFYHI HRLCLARIQN RRWQRLTTDL QNAFGQLQLR
     VVKEGDEEIN PNGDSCVICF EHYKPNDIVR ILTCKHFFHK NCIDPWILSH GTCPICKCDI
     LKVLGIQVDV ENGTEPLQVL MSSELCETLS PSEEETNNEV SPAGTSDKVI HVEENPTSQN
     NDSQPHSVVE DVHPSP