ID   TM129_XENLA             Reviewed;         362 AA.
AC   Q6IR55;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) 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       {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; BC071045; AAH71045.1; -; mRNA.
DR   RefSeq; NP_001085030.1; NM_001091561.1.
DR   AlphaFoldDB; Q6IR55; -.
DR   DNASU; 432097; -.
DR   GeneID; 432097; -.
DR   CTD; 432097; -.
DR   Xenbase; XB-GENE-6256270; tmem129.L.
DR   OrthoDB; 647242at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 432097; Expressed in egg cell and 19 other tissues.
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; IEA:InterPro.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
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_0000291045"
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;  40997 MW;  88C52D3E521F01FC CRC64;
     MESPAVTFTL AYVVFSVCFV FTPNEFHSAG ITVQNLLSGW LGSEDVAFVH YHIRRSSATL
     LAHSLLPMGY FIGMCFAAPE KELYNVHKAA DGWKVFVLMA VLLPIATSIL AFYWSQKRWS
     NHPLAKTLAH HALPQSSWRA VASSINTEFR RIDKFATGAP SARVIVTDTW VMKVTTYKVD
     VAQQQDIHLT VTDSRQHELS PDSNTPVQFI TIRVASINPR VKPFDIRLNS TEYGELREKL
     HAPIRNAANI VIHQTLGDMF LDTFRSLVEA NHTYEISSNQ ELEPCIGCMQ TNANIKLVKY
     CQEANEGECQ QCYCRPMWCL TCMGKWFASR QDQQHPETWL SSQVPCPTCR AKFCIVDVCI
     VR