ID GOLI_RAT Reviewed; 419 AA.
AC Q6Y290;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=E3 ubiquitin-protein ligase RNF130;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86XS8};
DE AltName: Full=Goliath homolog;
DE Short=R-goliath;
DE AltName: Full=RING finger protein 130;
DE Flags: Precursor;
GN Name=Rnf130 {ECO:0000250|UniProtKB:Q86XS8};
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] {ECO:0000305, ECO:0000312|EMBL:AAO31973.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAO31973.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAO31973.1};
RX PubMed=13679316; DOI=10.1095/biolreprod.103.018820;
RA Guais A., Solhonne B., Melaine N., Guellaeen G., Bulle F.;
RT "Goliath, a ring-H2 mitochondrial protein, regulated by luteinizing
RT hormone/human chorionic gonadotropin in rat Leydig cells.";
RL Biol. Reprod. 70:204-213(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}.
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}. Note=May be mitochondrial in the R2C
CC Leydig cell line. {ECO:0000269|PubMed:13679316}.
CC -!- TISSUE SPECIFICITY: In testis sections, expressed in interstitial
CC tissue and seminiferous tubules. In tubules, expression is mainly in
CC postmeiotic germ cells and to a much lesser extent in Sertoli cells (at
CC protein level). Expressed at high levels in liver, lung, stomach, heart
CC and thymus. {ECO:0000269|PubMed:13679316}.
CC -!- INDUCTION: Regulated by lutenising hormone (LH) in Leydig cells but not
CC in germ cells. {ECO:0000269|PubMed:13679316}.
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DR EMBL; AY190520; AAO31973.1; -; mRNA.
DR RefSeq; NP_001032747.1; NM_001037658.1.
DR AlphaFoldDB; Q6Y290; -.
DR SMR; Q6Y290; -.
DR STRING; 10116.ENSRNOP00000066033; -.
DR GlyCosmos; Q6Y290; 6 sites, No reported glycans.
DR GlyGen; Q6Y290; 6 sites.
DR PhosphoSitePlus; Q6Y290; -.
DR jPOST; Q6Y290; -.
DR GeneID; 652955; -.
DR KEGG; rno:652955; -.
DR AGR; RGD:1562041; -.
DR RGD; 1562041; Rnf130.
DR InParanoid; Q6Y290; -.
DR OrthoDB; 5474929at2759; -.
DR PhylomeDB; Q6Y290; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6Y290; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd02122; PA_GRAIL_like; 1.
DR CDD; cd16803; RING-H2_RNF130; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF27; RING FINGER PROTEIN 130; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; 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 /evidence="ECO:0000250"
FT /id="PRO_0000030720"
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 MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XS8"
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"
SQ SEQUENCE 419 AA; 46449 MW; C9FA8EE15B58DD32 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 SALGDLANDS SLGLEPLRTS
GISPLPQDGE LTPRTGEINI AVTKEWFIIA SFGLLSALTL CYMIIRATAS LNANEVEWF
//
