ID   RN128_XENLA             Reviewed;         404 AA.
AC   Q8AWW4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF128;
DE            EC=2.3.2.27;
DE   AltName: Full=Goliath-related E3 ubiquitin-protein ligase 1;
DE   AltName: Full=RING finger protein 128;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF128 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=rnf128; Synonyms=greul1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
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).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that catalyzes polyubiquitin
CC       chains (By similarity). Converts epidermis into cement gland and neural
CC       tissue in whole embryos. {ECO:0000250, ECO:0000269|PubMed:12435366}.
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: Endomembrane system {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}. Cytoplasm, perinuclear region
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the cement gland, cranial placodes,
CC       and the pronephros. {ECO:0000269|PubMed:12435366}.
CC   -!- DEVELOPMENTAL STAGE: Present as a maternal transcript. Early expression
CC       is confined to tissues of ectodermal origin. At stage 16, the
CC       predominant area of expression is within the developing cement gland.
CC       At stage 27, expression is detected in the anterodorsal lateral line
CC       placode, the olfactory placode, and the otic vesicle and pronephros.
CC       {ECO:0000269|PubMed:12435366}.
CC   -!- PTM: Auto-ubiquitinated.
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DR   EMBL; DQ911466; AAM51875.2; -; mRNA.
DR   RefSeq; NP_001090201.1; NM_001096732.1.
DR   AlphaFoldDB; Q8AWW4; -.
DR   SMR; Q8AWW4; -.
DR   GeneID; 779098; -.
DR   KEGG; xla:779098; -.
DR   CTD; 779098; -.
DR   Xenbase; XB-GENE-6253090; rnf128.L.
DR   OMA; AQSRKQX; -.
DR   OrthoDB; 1487241at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 779098; Expressed in stomach and 17 other tissues.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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   Cytoplasm; Membrane; Metal-binding; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..404
FT                   /note="E3 ubiquitin-protein ligase RNF128"
FT                   /id="PRO_0000261415"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          62..166
FT                   /note="PA"
FT   ZN_FING         260..301
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          336..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  44862 MW;  E7560CEA36325F9D CRC64;
     MGALKMRCQC FPLPYLSLLA LLLLNLSLTR AETLWTANVN YSYVYDNKTY GEEGEIGVFG
     QDSPIERAAG LVVLPKSEKL YTACKDNVNF SVPSGWTGPW IALIQRGGGC TFTEKINRAA
     ERGARAVVVY NNGIDNEVFE MSHPGTKDTV AIMIGNLKGN EIVDLIKGGM QVTMVIEVGR
     KHGSWINHYS IFFVSVSFFI VTAATVGYFI FYSARRWRLT RAQNKKQKRL KAEAKKAIGK
     LQLRTIKQGD KVLGPDGDSC AVCIEPYKPS DVVRILTCNH FFHKNCIDPW LLEHRTCPMC
     KCDILKSLGI AEDEEEGTSV AIPSVSSELQ RSTVQITEEE NHSETASSGY ASVRGGDEQV
     DEGQHIYENT ELVHEASATS IEVLPHMDNP GFESEDVHVH EMKS