RN128_BOVIN
ID RN128_BOVIN Reviewed; 431 AA.
AC Q29RU0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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}.
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DR EMBL; BC114021; AAI14022.1; -; mRNA.
DR RefSeq; NP_001069539.1; NM_001076071.2.
DR AlphaFoldDB; Q29RU0; -.
DR SMR; Q29RU0; -.
DR STRING; 9913.ENSBTAP00000031108; -.
DR PaxDb; Q29RU0; -.
DR PRIDE; Q29RU0; -.
DR GeneID; 535869; -.
DR KEGG; bta:535869; -.
DR CTD; 79589; -.
DR eggNOG; KOG4628; Eukaryota.
DR InParanoid; Q29RU0; -.
DR OrthoDB; 1487241at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; 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..431
FT /note="E3 ubiquitin-protein ligase RNF128"
FT /id="PRO_0000261411"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 75..186
FT /note="PA"
FT ZN_FING 280..321
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 345..431
FT /note="Disordered"
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 431 AA; 46881 MW; 4B963786A00119BE CRC64;
MGQLPGAGVF CRGGCGFSRL LAWCFLLVLS PQTPGSRGAE AVWTAYLNVS WRVPHTGVNR
TVWELSEEGV YGQDSPLEPV AGVLVPPDGP GALNACNPHT NFTVPTVPGD WGSSVQVSWL
ALIQRGGGCT FADKIHLAYE RGASGAVIFN FPGTRNEVIP MSHPGAGDIV AIMIGNLKGT
KILQSIQRGI QVTMVIEVGK KHGPWVNHYS IFFVSVSFFI ITAATVGYFI FYSARRLRNA
RAQSRKQRQL KADAKKAIGR LQLRTQKQGD KEIGPDGDSC AVCIELYKPN DLVRILTCNH
VFHKTCVDPW LLEHRTCPMC KCDILKALGI EVDVEDGSVS LQVPVSNETS SNASPHEEDN
RSETASSGYA SVQGADEPPL EEHAHSANEN LQLVNHEANS MAVDVVPHVD NPTFEEDESP
DQETTVREIK S
