ID   TM129_BOVIN             Reviewed;         362 AA.
AC   Q08DK0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=E3 ubiquitin-protein ligase TM129;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase TM129 {ECO:0000305};
GN   Name=TMEM129;
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=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase involved in ER-associated protein
CC       degradation, preferentially associates with the E2 enzyme UBE2J2.
CC       Exploited by viral US11 proteins to mediate HLA class I proteins
CC       degradation. {ECO:0000250|UniProtKB:A0AVI4}.
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   -!- SUBUNIT: Integral component of ER-resident dislocation complexes.
CC       {ECO:0000250|UniProtKB:A0AVI4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:A0AVI4}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:A0AVI4}.
CC   -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC       ubiquitin ligase activity. {ECO:0000250|UniProtKB:A0AVI4}.
CC   -!- SIMILARITY: Belongs to the TMEM129 family. {ECO:0000305}.
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DR   EMBL; BC123709; AAI23710.1; -; mRNA.
DR   RefSeq; NP_001070332.1; NM_001076864.1.
DR   AlphaFoldDB; Q08DK0; -.
DR   STRING; 9913.ENSBTAP00000014663; -.
DR   PaxDb; Q08DK0; -.
DR   PRIDE; Q08DK0; -.
DR   Ensembl; ENSBTAT00000014663; ENSBTAP00000014663; ENSBTAG00000011042.
DR   GeneID; 518991; -.
DR   KEGG; bta:518991; -.
DR   CTD; 92305; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011042; -.
DR   VGNC; VGNC:35962; TMEM129.
DR   eggNOG; KOG3899; Eukaryota.
DR   GeneTree; ENSGT00390000013284; -.
DR   InParanoid; Q08DK0; -.
DR   OMA; AEYGELC; -.
DR   OrthoDB; 647242at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000011042; Expressed in ileocecal valve and 104 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR   InterPro; IPR018801; TM129.
DR   PANTHER; PTHR31322; PTHR31322; 1.
DR   Pfam; PF10272; Tmpp129; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Unfolded protein response; Zinc; Zinc-finger.
FT   CHAIN           1..362
FT                   /note="E3 ubiquitin-protein ligase TM129"
FT                   /id="PRO_0000291040"
FT   TOPO_DOM        1..6
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..94
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         285..350
FT                   /note="RING-type; degenerate"
SQ   SEQUENCE   362 AA;  40454 MW;  630E3E6E3B3E0FC3 CRC64;
     MDSPEVTFTL AYLVFAVCFV FTPTEFHSAG LTVQNLLSGW LGSEDAAFVP YHLRRTAATL
     LCHSLLPLGY YVGMCFAASE KQLYYPSQTP ETWRAFLLLA LMLPAIACTL IYYWSRDHWA
     CHPLARTLAL YALPRSGWQA VASSVNTEFR RIDKFATGVP GARVIVTDTW VMKVTTYRVH
     VAQQQDVRLT VTEAQQHELS PDSHLPVQLL TIRVASANPA VPAFHIRLNS TEYGELCEKL
     RAPIRSAANV VIHQSLGDLF LETFASLVEV NPAYSVPSSQ DLEACIGCMQ TQASVKLVKT
     CQEVAVGECQ QCYCRPMWCL TCMGKWFASR QDPQRPDTWL ASRVPCPTCR ARFCVLDVCA
     VR