RN133_RAT
ID RN133_RAT Reviewed; 381 AA.
AC Q6AY01;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC079249; AAH79249.1; -; mRNA.
DR RefSeq; NP_001037743.1; NM_001044278.1.
DR RefSeq; XP_006236206.1; XM_006236144.3.
DR AlphaFoldDB; Q6AY01; -.
DR SMR; Q6AY01; -.
DR PhosphoSitePlus; Q6AY01; -.
DR Ensembl; ENSRNOT00000115813; ENSRNOP00000079460; ENSRNOG00000065130.
DR GeneID; 681395; -.
DR KEGG; rno:681395; -.
DR UCSC; RGD:1596695; rat.
DR CTD; 168433; -.
DR RGD; 1596695; Rnf133.
DR GeneTree; ENSGT00940000163928; -.
DR InParanoid; Q6AY01; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q6AY01; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6AY01; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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..381
FT /note="E3 ubiquitin-protein ligase RNF133"
FT /id="PRO_0000380753"
FT TRANSMEM 186..208
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 340..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 42872 MW; 181C4291A017657D CRC64;
MNPLQTGPWQ TSAPSFWLLK FSFIWLVSQN CCTASAVWTA YMNISFHVGN RMLSELGETG
VFGRSSILKR VAGVVVPPEG KIQNACDPNT SFILPRNKEP WIALIERGGC AFTQKIKVAS
ENGARGVIIY NFPGTGNQVF PMSHQAFEDI VVVMIGNVKG MEILHLIRKG VHVTVMVEVG
RKHVIWLNHY FVSFMIVTTA TLAYFTFYHI RRLWVARIED RRWKRLTREL KKAFGQLQVR
ILKEGDEEVS PNADSCVICF EAYKPNEIVR ILTCKHFFHK NCIDPWILAH GTCPMCKCDI
LKALGIQMDI EDGSDSLQVL MSNELPGTFS AMEEELNNEL PPARTSSKVT HVQEHPTSVN
VGSQPPEAEE TGHPSFGQHD L