GOLI_MOUSE
ID GOLI_MOUSE Reviewed; 419 AA.
AC Q8VEM1; Q80VL7; Q9QZQ6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=E3 ubiquitin-protein ligase RNF130;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86XS8};
DE AltName: Full=G1-related zinc finger protein;
DE AltName: Full=Goliath homolog;
DE AltName: Full=RING finger protein 130;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF130 {ECO:0000305};
DE Flags: Precursor;
GN Name=Rnf130 {ECO:0000312|EMBL:AAH18199.1};
GN Synonyms=G1rp {ECO:0000312|EMBL:AAF05310.1};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10806348; DOI=10.1016/s0378-1119(00)00109-8;
RA Baker S.J., Reddy E.P.;
RT "Cloning of murine G1RP, a novel gene related to Drosophila melanogaster
RT g1.";
RL Gene 248:33-40(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH18199.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH18199.1}, and
RC Olfactory epithelium {ECO:0000312|EMBL:AAH48901.2};
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: Acts as an E3 ubiquitin-protein ligase (By similarity). May
CC have a role during the programmed cell death of hematopoietic cells.
CC {ECO:0000250, ECO:0000269|PubMed:10806348}.
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; Evidence={ECO:0000250|UniProtKB:Q86XS8};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q86XS8}.
CC -!- TISSUE SPECIFICITY: Expression is highest in liver, with lesser amounts
CC in the lung, spleen, brain, heart, kidney and testis.
CC {ECO:0000269|PubMed:10806348}.
CC -!- INDUCTION: Up-regulated in response to interleukin-3 (IL-3) withdrawal-
CC induced apoptosis of 32Dcl3 cells (derived from bone marrow).
CC {ECO:0000269|PubMed:10806348}.
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DR EMBL; AF171875; AAF05310.1; -; mRNA.
DR EMBL; AL627187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018199; AAH18199.1; -; mRNA.
DR EMBL; BC048901; AAH48901.2; -; mRNA.
DR CCDS; CCDS24626.1; -.
DR RefSeq; NP_001277678.1; NM_001290749.1.
DR RefSeq; NP_001277679.1; NM_001290750.1.
DR RefSeq; NP_067515.2; NM_021540.4.
DR AlphaFoldDB; Q8VEM1; -.
DR SMR; Q8VEM1; -.
DR BioGRID; 208508; 2.
DR STRING; 10090.ENSMUSP00000099837; -.
DR GlyConnect; 2271; 4 N-Linked glycans (1 site).
DR GlyGen; Q8VEM1; 6 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q8VEM1; -.
DR PhosphoSitePlus; Q8VEM1; -.
DR EPD; Q8VEM1; -.
DR MaxQB; Q8VEM1; -.
DR PaxDb; Q8VEM1; -.
DR PRIDE; Q8VEM1; -.
DR ProteomicsDB; 271029; -.
DR Antibodypedia; 2993; 114 antibodies from 24 providers.
DR DNASU; 59044; -.
DR Ensembl; ENSMUST00000102776; ENSMUSP00000099837; ENSMUSG00000020376.
DR GeneID; 59044; -.
DR KEGG; mmu:59044; -.
DR UCSC; uc007irl.2; mouse.
DR CTD; 55819; -.
DR MGI; MGI:1891717; Rnf130.
DR VEuPathDB; HostDB:ENSMUSG00000020376; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000157465; -.
DR InParanoid; Q8VEM1; -.
DR OMA; NADEAEW; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q8VEM1; -.
DR TreeFam; TF317486; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 59044; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Rnf130; mouse.
DR PRO; PR:Q8VEM1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VEM1; protein.
DR Bgee; ENSMUSG00000020376; Expressed in granulocyte and 261 other tissues.
DR ExpressionAtlas; Q8VEM1; baseline and differential.
DR Genevisible; Q8VEM1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0012501; P:programmed cell death; IMP: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 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..419
FT /note="E3 ubiquitin-protein ligase RNF130"
FT /id="PRO_0000030719"
FT TOPO_DOM 28..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 105..176
FT /note="PA"
FT ZN_FING 264..305
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 310
FT /note="K -> R (in Ref. 1; AAF05310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46376 MW; 4E699A66D658CBF2 CRC64;
MSGAARAGPA RLAALALLTC SLWPTRADNA SQEYYTALIN VTVQEPGRGT PLTFRIDRGR
YGLDSPKAEV RGQVLAPLPI HGVADHLGCD PQTRFFVPPN IKQWIALLQR GNCTFKEKIS
RAAFHNAVAV VIYNNKSKEE PVTMTHPGTG DIIAVMITEL RGKDILSYLE KNISVQMTIA
VGTRMPPKNF SRGSLVFVSI SFIVLMIISS AWLIFYFIQK IRYTNARDRN QRRLGDAAKK
AISKLTTRTV KKGDKETDPD FDHCAVCIES YKQNDVVRVL PCKHVFHKSC VDPWLSEHCT
CPMCKLNILK ALGIVPNLPC TDNVAFDMER LTRTQAVNRR AALGDLAGDS SLGLEPLRTS
GISPLPQDGE LTPRTGEINI AVTKEWFIIA SFGLLSALTL CYMIIRATAS LNANEVEWF
