ID   GID8_BOVIN              Reviewed;         228 AA.
AC   Q32L52;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Glucose-induced degradation protein 8 homolog;
GN   Name=GID8;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC       complex that selectively accepts ubiquitin from UBE2H and mediates
CC       ubiquitination and subsequent proteasomal degradation of the
CC       transcription factor HBP1. Acts as a positive regulator of Wnt
CC       signaling pathway by promoting beta-catenin (CTNNB1) nuclear
CC       accumulation. {ECO:0000250|UniProtKB:Q9NWU2}.
CC   -!- SUBUNIT: Homodimer; may also form higher oligomers (By similarity).
CC       Identified in the CTLH complex that contains GID4, RANBP9 and/or
CC       RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B),
CC       GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or
CC       alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or
CC       RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5
CC       have ancillary roles. Interacts with RANBP9. Part of a complex
CC       consisting of RANBP9, MKLN1 and GID8. Interacts with CTNNB1, AXIN1 and
CC       GSK3B (By similarity). {ECO:0000250|UniProtKB:Q9D7M1,
CC       ECO:0000250|UniProtKB:Q9NWU2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NWU2}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9NWU2}. Note=Localizes in the cytoplasm in the
CC       absence of Wnt stimulation and in the nucleus in the presence of Wnt
CC       stimulation. {ECO:0000250|UniProtKB:Q9NWU2}.
CC   -!- PTM: Polyubiquitinated through 'Lys-48'-polyubiquitin chains, leading
CC       to proteasomal degradation in the absence of Wnt stimulation.
CC       {ECO:0000250|UniProtKB:Q9NWU2}.
CC   -!- SIMILARITY: Belongs to the GID8 family. {ECO:0000305}.
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DR   EMBL; BC109762; AAI09763.1; -; mRNA.
DR   RefSeq; NP_001032676.1; NM_001037587.2.
DR   RefSeq; XP_005214613.1; XM_005214556.2.
DR   RefSeq; XP_015329616.1; XM_015474130.1.
DR   AlphaFoldDB; Q32L52; -.
DR   SMR; Q32L52; -.
DR   BioGRID; 162217; 1.
DR   STRING; 9913.ENSBTAP00000002387; -.
DR   PaxDb; Q32L52; -.
DR   PRIDE; Q32L52; -.
DR   Ensembl; ENSBTAT00000002387; ENSBTAP00000002387; ENSBTAG00000001827.
DR   GeneID; 505570; -.
DR   KEGG; bta:505570; -.
DR   CTD; 54994; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001827; -.
DR   VGNC; VGNC:29353; GID8.
DR   eggNOG; KOG2659; Eukaryota.
DR   GeneTree; ENSGT00390000015162; -.
DR   HOGENOM; CLU_073203_1_0_1; -.
DR   InParanoid; Q32L52; -.
DR   OMA; QNGRIQE; -.
DR   OrthoDB; 1365635at2759; -.
DR   TreeFam; TF300176; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000001827; Expressed in esophagus and 104 other tissues.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013144; CRA_dom.
DR   InterPro; IPR024964; CTLH/CRA.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR006594; LisH.
DR   Pfam; PF10607; CLTH; 1.
DR   Pfam; PF08513; LisH; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; Ubl conjugation;
KW   Wnt signaling pathway.
FT   CHAIN           1..228
FT                   /note="Glucose-induced degradation protein 8 homolog"
FT                   /id="PRO_0000328503"
FT   DOMAIN          25..57
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          63..120
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REGION          116..212
FT                   /note="Interaction with CTNNB1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWU2"
SQ   SEQUENCE   228 AA;  26799 MW;  6D1F2223D8E58808 CRC64;
     MSYTEKPDEI TKDEWMEKLN NLHVQRADMN RLIMNYLVTE GFKEAAEKFR MESGIEPSVD
     LETLDERIKI REMILKGQIQ EAIALINSLH PELLDTNRYL YFHLQQQHLI ELIRQRETEA
     ALEFAQTQLA EQGEESRECL TEMERTLALL AFDNPEDSPF GDLLNMMQRQ KVWSEVNQAV
     LDYENRESTP KLAKLLKLLL WAQNELDQKK VKYPKMTDLS KGVIEEPK