RN128_PONAB
ID RN128_PONAB Reviewed; 428 AA.
AC Q5RF74;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=E3 ubiquitin-protein ligase RNF128;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 128;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF128 {ECO:0000305};
DE Flags: Precursor;
GN Name=RNF128;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains formation. Functions as an
CC inhibitor of cytokine gene transcription. Inhibits IL2 and IL4
CC transcription, thereby playing an important role in the induction of
CC the anergic phenotype, a long-term stable state of T-lymphocyte
CC unresponsiveness to antigenic stimulation associated with the blockade
CC of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages
CC and COR1A with 'Lys-63' linkages leading to their degradation, down-
CC regulation of these cytosleletal components results in impaired
CC lamellipodium formation and reduced accumulation of F-actin at the
CC immunological synapse. Functions in the patterning of the dorsal
CC ectoderm; sensitizes ectoderm to respond to neural-inducing signals.
CC {ECO:0000250|UniProtKB:Q8TEB7}.
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, cytoskeleton {ECO:0000250}.
CC Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an
CC asymmetric perinuclear punctate manner. Localizes to the internal pool
CC of the transferrin recycling endosomal pathway. Partially colocalized
CC with the endoplasmic reticulum resident HSPA5, with Golgi resident
CC STX5, and with the late endosomal GTPase RAB7A. {ECO:0000250}.
CC -!- DOMAIN: Binding to E2 ubiquitin-conjugating enzyme requires an intact
CC RING finger domain. {ECO:0000250|UniProtKB:Q8TEB7}.
CC -!- PTM: Auto-ubiquitinated. Controls the development of T-cell clonal
CC anergy by ubiquitination. {ECO:0000250|UniProtKB:Q8TEB7}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR857287; CAH89583.1; -; mRNA.
DR RefSeq; NP_001124698.1; NM_001131226.2.
DR AlphaFoldDB; Q5RF74; -.
DR SMR; Q5RF74; -.
DR STRING; 9601.ENSPPYP00000023062; -.
DR GeneID; 100171545; -.
DR KEGG; pon:100171545; -.
DR CTD; 79589; -.
DR eggNOG; KOG4628; Eukaryota.
DR HOGENOM; CLU_049885_0_0_1; -.
DR InParanoid; Q5RF74; -.
DR OMA; AQSRKQX; -.
DR OrthoDB; 1487241at2759; -.
DR TreeFam; TF317486; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
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:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
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; Cytoskeleton; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..428
FT /note="E3 ubiquitin-protein ligase RNF128"
FT /id="PRO_0000261414"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 75..183
FT /note="PA"
FT ZN_FING 277..318
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 346..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 428 AA; 46483 MW; FA2DBB5A88B81E8D CRC64;
MGPPLGAGVS CRGGCGSSRL LAWCFLLALS PQAPGSRGAE AVWTAYLNVS WRVPHTGVNR
TVWELSEEGV YGQDSPLEPV AGVLVPPDGP GALNACNPHT NFTVPTVWGS TVQVSWLALI
QRGGGCTFAD KIHLAYERGA SGAVIFNFPG TRNEVIPMSH PGAGDIVAIM IGNLKGTKIL
QSIQRGIQVT MVIEVGKKHG PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ
SRKQRQLKAD AKKAIGRLQL RTLKQGDREI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEISNSA SSHEEDNRSE
TASSGYASVQ GADEPPLEEH VQSTNENLQL VNHEANSVAV DVIPHVDNPT FEEDETPHQE
TAVREIKS
