TM129_MOUSE
ID TM129_MOUSE Reviewed; 362 AA.
AC Q8K304; Q3TA74; Q9DCF3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K304-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K304-2; Sequence=VSP_026159;
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; AK002836; BAB22394.1; -; mRNA.
DR EMBL; AK172044; BAE42795.1; -; mRNA.
DR EMBL; BC029088; AAH29088.1; -; mRNA.
DR EMBL; BC094042; AAH94042.1; -; mRNA.
DR CCDS; CCDS19206.1; -. [Q8K304-1]
DR RefSeq; NP_080974.2; NM_026698.2. [Q8K304-1]
DR RefSeq; XP_006504143.1; XM_006504080.1.
DR RefSeq; XP_006504144.1; XM_006504081.1.
DR AlphaFoldDB; Q8K304; -.
DR STRING; 10090.ENSMUSP00000019439; -.
DR iPTMnet; Q8K304; -.
DR PhosphoSitePlus; Q8K304; -.
DR EPD; Q8K304; -.
DR MaxQB; Q8K304; -.
DR PaxDb; Q8K304; -.
DR PeptideAtlas; Q8K304; -.
DR PRIDE; Q8K304; -.
DR ProteomicsDB; 260673; -. [Q8K304-1]
DR ProteomicsDB; 260674; -. [Q8K304-2]
DR Antibodypedia; 64956; 4 antibodies from 3 providers.
DR Ensembl; ENSMUST00000019439; ENSMUSP00000019439; ENSMUSG00000019295. [Q8K304-1]
DR GeneID; 68366; -.
DR KEGG; mmu:68366; -.
DR UCSC; uc008xay.1; mouse. [Q8K304-1]
DR CTD; 92305; -.
DR MGI; MGI:1915616; Tmem129.
DR VEuPathDB; HostDB:ENSMUSG00000019295; -.
DR eggNOG; KOG3899; Eukaryota.
DR GeneTree; ENSGT00390000013284; -.
DR HOGENOM; CLU_048119_1_0_1; -.
DR InParanoid; Q8K304; -.
DR OMA; AEYGELC; -.
DR OrthoDB; 647242at2759; -.
DR PhylomeDB; Q8K304; -.
DR TreeFam; TF314487; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 68366; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem129; mouse.
DR PRO; PR:Q8K304; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K304; protein.
DR Bgee; ENSMUSG00000019295; Expressed in spermatocyte and 264 other tissues.
DR ExpressionAtlas; Q8K304; baseline and differential.
DR Genevisible; Q8K304; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR InterPro; IPR018801; TM129.
DR PANTHER; PTHR31322; PTHR31322; 1.
DR Pfam; PF10272; Tmpp129; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Unfolded protein response; Zinc; Zinc-finger.
FT CHAIN 1..362
FT /note="E3 ubiquitin-protein ligase TM129"
FT /id="PRO_0000291042"
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"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026159"
FT CONFLICT 69
FT /note="G -> A (in Ref. 1; BAB22394)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="C -> R (in Ref. 1; BAE42795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40628 MW; BF0E6A9429FD5178 CRC64;
MDSPEVTFTL AYLVFAVCFV FTPNEFYSAG LTVQNLLSGW LGSEDAAFVP YHLRRTSATL
LCHSLLPLGY YMGMCFAASE KQLYSPGQAP EAWQLFLLLA VTLPLLSCTL IYYWSWDRWT
RHPLAQTLAL YALPQSGWQA VASSINTEFR RIDKFATGAP GARVIVTDTW VMKVTTYRVH
VAQQQDVHLT VTESRQHDLS PDSNLPVQLL TIRVASTSPG TQPFDIRLNS SEYGELCEKL
HAPIRSAANV VIRQSLGDLF LETFASHVEV NPAYSVPSNQ ELEPCIGCMQ TRASVKLVKT
CQEPAVGECQ QCYCRPMWCL TCMGKWFASR QDPQRPDTWL ASRVPCPTCR ARFCILDVCC
VR
