RN133_MOUSE
ID RN133_MOUSE Reviewed; 382 AA.
AC Q14B02; Q8C1F1; Q8CGR0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, 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=Goliath-related E3 ubiquitin-protein ligase 2;
DE AltName: Full=RING finger protein 133;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF133 {ECO:0000305};
GN Name=Rnf133; Synonyms=Greul2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-381 (ISOFORM 1).
RC STRAIN=CD-1;
RX PubMed=12435366; DOI=10.1006/dbio.2002.0814;
RA Borchers A.G.M., Hufton A.L., Eldridge A.G., Jackson P.K., Harland R.M.,
RA Baker J.C.;
RT "The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus
RT development.";
RL Dev. Biol. 251:395-408(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=18574499; DOI=10.1038/cr.2008.73;
RA Nian H., Zhang W., Shi H., Zhao Q., Xie Q., Liao S., Zhang Y., Zhang Z.,
RA Wang C., Han C.;
RT "Mouse RING finger protein Rnf133 is a testis-specific endoplasmic
RT reticulum-associated E3 ubiquitin ligase.";
RL Cell Res. 18:800-802(2008).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity.
CC {ECO:0000269|PubMed:18574499}.
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:0000305|PubMed:18574499}; Single-pass membrane protein
CC {ECO:0000305|PubMed:18574499}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14B02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14B02-2; Sequence=VSP_037829;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:18574499}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the testis at day 21 and
CC increases dramatically from day 28 and thereafter.
CC {ECO:0000269|PubMed:18574499}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18574499}.
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DR EMBL; AK028082; BAC25740.1; -; mRNA.
DR EMBL; CH466533; EDL13834.1; -; Genomic_DNA.
DR EMBL; BC116423; AAI16424.1; -; mRNA.
DR EMBL; BC116424; AAI16425.1; -; mRNA.
DR EMBL; AY155441; AAN75222.1; -; mRNA.
DR CCDS; CCDS19938.1; -. [Q14B02-2]
DR RefSeq; NP_937894.1; NM_198251.2. [Q14B02-2]
DR AlphaFoldDB; Q14B02; -.
DR SMR; Q14B02; -.
DR iPTMnet; Q14B02; -.
DR PhosphoSitePlus; Q14B02; -.
DR PRIDE; Q14B02; -.
DR ProteomicsDB; 300535; -. [Q14B02-1]
DR ProteomicsDB; 300536; -. [Q14B02-2]
DR Antibodypedia; 2716; 201 antibodies from 24 providers.
DR DNASU; 386611; -.
DR Ensembl; ENSMUST00000063548; ENSMUSP00000066906; ENSMUSG00000051956. [Q14B02-2]
DR Ensembl; ENSMUST00000115354; ENSMUSP00000111011; ENSMUSG00000051956. [Q14B02-1]
DR GeneID; 386611; -.
DR KEGG; mmu:386611; -.
DR UCSC; uc009bbk.1; mouse. [Q14B02-2]
DR UCSC; uc029vtq.1; mouse. [Q14B02-1]
DR CTD; 168433; -.
DR MGI; MGI:2677436; Rnf133.
DR VEuPathDB; HostDB:ENSMUSG00000051956; -.
DR GeneTree; ENSGT00940000163928; -.
DR HOGENOM; CLU_049885_1_2_1; -.
DR InParanoid; Q14B02; -.
DR OMA; IIWMNHY; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q14B02; -.
DR TreeFam; TF317486; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 386611; 2 hits in 57 CRISPR screens.
DR PRO; PR:Q14B02; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q14B02; protein.
DR Bgee; ENSMUSG00000051956; Expressed in seminiferous tubule of testis and 4 other tissues.
DR Genevisible; Q14B02; MM.
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; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..382
FT /note="E3 ubiquitin-protein ligase RNF133"
FT /id="PRO_0000380751"
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..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 160..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037829"
FT CONFLICT 182
FT /note="K -> E (in Ref. 4; AAN75222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 43102 MW; 3EC4A20E7B5CF4D0 CRC64;
MNPLQTSTWQ NQAPSFWLLR FSFIWLVSQK CCTASAVWTA YMNISFHVGN RMLSELGETG
VFGRSSILKR VAGVVVPPEG KIQNACDPNT TFILPRNKEP WIALIERGGC AFTQKIKVAS
EHGARGVIIY NFPGTGNQVF PMSHQAFEDI VVVMIGNIKG MEILHLIRKG VHVTVMVEVG
RKHVIWLNHY FVSFMIVTTA TLAYFTFYHI RRLWVARIEN RRWKRLTREL KKAFGQLQVR
VLKEGDEEVN PNADSCVICF EAYKPNEIVR ILTCKHFFHK NCIDPWILAH GTCPMCKCDI
LKALGIQMDI EDGTDSLQVL MSNELPGTLS PVEEETNYEL PPARTSSKVT HVQEHPTSSA
NAGSQPPEAE ETSHPSHGQQ VL
