ID   TM129_DANRE             Reviewed;         361 AA.
AC   Q6PD82;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
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; ORFNames=zgc:63798;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2003) 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; BC058876; AAH58876.1; -; mRNA.
DR   RefSeq; NP_998612.1; NM_213447.1.
DR   AlphaFoldDB; Q6PD82; -.
DR   SMR; Q6PD82; -.
DR   STRING; 7955.ENSDARP00000101988; -.
DR   PaxDb; Q6PD82; -.
DR   GeneID; 406756; -.
DR   KEGG; dre:406756; -.
DR   CTD; 92305; -.
DR   ZFIN; ZDB-GENE-040426-2796; tmem129.
DR   eggNOG; KOG3899; Eukaryota.
DR   InParanoid; Q6PD82; -.
DR   OrthoDB; 647242at2759; -.
DR   PhylomeDB; Q6PD82; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6PD82; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..361
FT                   /note="E3 ubiquitin-protein ligase TM129"
FT                   /id="PRO_0000291044"
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..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         285..349
FT                   /note="RING-type; degenerate"
SQ   SEQUENCE   361 AA;  41146 MW;  B2BE96F2443E8FAA CRC64;
     MDRPDATFTL AYVVFALCFV FTPNEFRSAG FTVQHMFSEW LGSEDISFIQ HHIRRTTLTV
     LFHSFLPLGY YIGMCFAAPE QNLMYVHHAS QGWQMYFGLS LVIQLLSCAL AFYWSRRGWA
     NHPICKALSV HALPQSSWRA VASSINTEFR RIDKFASGSP SARVIVTDTW VMKVTTYSLH
     VALHQDCHLT VTDSKHHSLS PDLNTPVQIV TITVGSINPR VKSFDIRLKS TEYAELQEKL
     HAPIRNAANV VIHLTMSELF LETFKSYVRM NVVYKCPSGQ ELEPCIGCMQ VNANVKLLCL
     CQSDEGECQQ CYCRPMWCLT CMGKWFASRQ DQQQPETWLS SRVPCPTCRA KFCILDVCPI
     E