ID   TM129_XENTR             Reviewed;         362 AA.
AC   Q0IJ33;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-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       {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; BC121210; AAI21211.1; -; mRNA.
DR   RefSeq; NP_001016117.2; NM_001016117.3.
DR   AlphaFoldDB; Q0IJ33; -.
DR   PaxDb; Q0IJ33; -.
DR   DNASU; 548871; -.
DR   Ensembl; ENSXETT00000008404; ENSXETP00000008404; ENSXETG00000003875.
DR   GeneID; 548871; -.
DR   KEGG; xtr:548871; -.
DR   CTD; 92305; -.
DR   Xenbase; XB-GENE-5934178; tmem129.
DR   eggNOG; KOG3899; Eukaryota.
DR   HOGENOM; CLU_048119_1_0_1; -.
DR   InParanoid; Q0IJ33; -.
DR   OMA; DEHPISH; -.
DR   OrthoDB; 647242at2759; -.
DR   PhylomeDB; Q0IJ33; -.
DR   TreeFam; TF314487; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000003875; Expressed in egg cell and 14 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: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_0000291046"
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;  41137 MW;  E9335A54CA163339 CRC64;
     MESPEVTFTL AYVVFSVCFV FTPNEFHSAG ITVQNLLSGW LGSEDVAFVH YHIRRSTATL
     LTHSLLPMGY FIGMCFAAPE KELYNVYKAA DGWKVFVLIT VLLPVTTSIL AFYWSQKRWG
     NHPLAKTLAH HALPQSSWRA VASSINTEFR RIDKFATGAP SARVIVTDTW VMKVTTYRVD
     VAQQQDIHLT VTDSRQHELS PDSNTPVQFI TIRVASVNPR VKPFDIRLNS TEYGELREKL
     HAPIRNAANV VIHQTLSDMF LETFKSLVEA NQVYELSSNQ ELEPCIGCMQ TNANIKLVKY
     CQEANEGECQ QCYCRPMWCL TCMGKWFASR QDQQHPETWL SSHVPCPTCR AKFCIVDVCI
     VR