UBL4A_RAT
ID UBL4A_RAT Reviewed; 157 AA.
AC B2GV38;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ubiquitin-like protein 4A;
GN Name=Ubl4a; Synonyms=Ubl4;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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: As part of a cytosolic protein quality control complex, the
CC BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-
CC containing proteins in a soluble state and participates in their proper
CC delivery to the endoplasmic reticulum or alternatively can promote
CC their sorting to the proteasome where they undergo degradation. The
CC BAG6/BAT3 complex is involved in the post-translational delivery of
CC tail-anchored/type II transmembrane proteins to the endoplasmic
CC reticulum membrane. Recruited to ribosomes, it interacts with the
CC transmembrane region of newly synthesized tail-anchored proteins and
CC together with SGTA and ASNA1 mediates their delivery to the endoplasmic
CC reticulum. Client proteins that cannot be properly delivered to the
CC endoplasmic reticulum are ubiquitinated and sorted to the proteasome.
CC Similarly, the BAG6/BAT3 complex also functions as a sorting platform
CC for proteins of the secretory pathway that are mislocalized to the
CC cytosol either delivering them to the proteasome for degradation or to
CC the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in
CC the endoplasmic reticulum-associated degradation (ERAD), a quality
CC control mechanism that eliminates unwanted proteins of the endoplasmic
CC reticulum through their retrotranslocation to the cytosol and their
CC targeting to the proteasome. It maintains these retrotranslocated
CC proteins in an unfolded yet soluble state condition in the cytosol to
CC ensure their proper delivery to the proteasome.
CC {ECO:0000250|UniProtKB:P11441}.
CC -!- SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of BAG6,
CC UBL4A and GET4/TRC35. Interacts with BAG6; the interaction is direct
CC and required for UBL4A protein stability. Interacts with USP13; may be
CC indirect via BAG6. {ECO:0000250|UniProtKB:P11441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P11441}. Nucleus {ECO:0000250|UniProtKB:P11441}.
CC -!- PTM: Polyubiquitinated. Ubiquitination by AMFR and deubiquitination by
CC USP13 may regulate the interaction between the BAG6/BAT complex and
CC SGTA and therefore may regulate client proteins fate.
CC {ECO:0000250|UniProtKB:P11441}.
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DR EMBL; CH474099; EDL84970.1; -; Genomic_DNA.
DR EMBL; BC166513; AAI66513.1; -; mRNA.
DR RefSeq; NP_001099816.1; NM_001106346.2.
DR AlphaFoldDB; B2GV38; -.
DR SMR; B2GV38; -.
DR BioGRID; 254493; 3.
DR STRING; 10116.ENSRNOP00000053153; -.
DR iPTMnet; B2GV38; -.
DR PhosphoSitePlus; B2GV38; -.
DR jPOST; B2GV38; -.
DR PaxDb; B2GV38; -.
DR PeptideAtlas; B2GV38; -.
DR PRIDE; B2GV38; -.
DR GeneID; 293864; -.
DR KEGG; rno:293864; -.
DR CTD; 8266; -.
DR RGD; 1563983; Ubl4a.
DR VEuPathDB; HostDB:ENSRNOG00000053061; -.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_119809_0_0_1; -.
DR InParanoid; B2GV38; -.
DR OMA; SMDTSYM; -.
DR OrthoDB; 1586605at2759; -.
DR PhylomeDB; B2GV38; -.
DR TreeFam; TF354228; -.
DR PRO; PR:B2GV38; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000053061; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; B2GV38; RN.
DR GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR CDD; cd01807; Ubl_UBL4A_like; 1.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR InterPro; IPR041421; Ubl4_C_TUGS.
DR InterPro; IPR044724; Ubl_UBL4A-like.
DR Pfam; PF17840; Tugs; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..157
FT /note="Ubiquitin-like protein 4A"
FT /id="PRO_0000403739"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 96..138
FT /note="Required and sufficient for interaction with BAG6"
FT /evidence="ECO:0000250|UniProtKB:P11441"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11441"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P11441"
SQ SEQUENCE 157 AA; 17791 MW; E8F80221F03606A9 CRC64;
MQLTVKALQG RECSLQVAED ELVSTLKHLV SDKLNVPVRQ QRLLFKGKAL ADEKRLSDYN
IGPNSKLNLV VKPLEKVLLE EGSAHRLVDS SATPIWQLIS KVLARHFSIG DASRVLEQLQ
RDYDRSLSRL TLDDIERLAS RFLHPEVTEA MEKGFCK
