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E3 ubiquitin-protein ligase TM129 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TM129)

 TM129_MOUSE             Reviewed;         362 AA.
Q8K304; Q3TA74; Q9DCF3;
12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
12-SEP-2018, entry version 103.
RecName: Full=E3 ubiquitin-protein ligase TM129;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase TM129 {ECO:0000305};
Name=Tmem129;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: E3 ubiquitin-protein ligase involved in ER-associated
protein degradation, preferentially associates with the E2 enzyme
UBE2J2. Exploited by viral US11 proteins to mediate HLA class I
proteins degradation. {ECO:0000250|UniProtKB:A0AVI4}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Integral component of ER-resident dislocation complexes.
{ECO:0000250|UniProtKB:A0AVI4}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:A0AVI4}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:A0AVI4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8K304-1; Sequence=Displayed;
Name=2;
IsoId=Q8K304-2; Sequence=VSP_026159;
-!- DOMAIN: The RING-type zinc finger domain is responsible for E3
ubiquitin ligase activity. {ECO:0000250|UniProtKB:A0AVI4}.
-!- SIMILARITY: Belongs to the TMEM129 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK002836; BAB22394.1; -; mRNA.
EMBL; AK172044; BAE42795.1; -; mRNA.
EMBL; BC029088; AAH29088.1; -; mRNA.
EMBL; BC094042; AAH94042.1; -; mRNA.
CCDS; CCDS19206.1; -. [Q8K304-1]
RefSeq; NP_080974.2; NM_026698.2. [Q8K304-1]
RefSeq; XP_006504143.1; XM_006504080.1.
RefSeq; XP_006504144.1; XM_006504081.1.
UniGene; Mm.491151; -.
ProteinModelPortal; Q8K304; -.
STRING; 10090.ENSMUSP00000019439; -.
iPTMnet; Q8K304; -.
PhosphoSitePlus; Q8K304; -.
PaxDb; Q8K304; -.
PeptideAtlas; Q8K304; -.
PRIDE; Q8K304; -.
Ensembl; ENSMUST00000019439; ENSMUSP00000019439; ENSMUSG00000019295. [Q8K304-1]
GeneID; 68366; -.
KEGG; mmu:68366; -.
UCSC; uc008xay.1; mouse. [Q8K304-1]
CTD; 92305; -.
MGI; MGI:1915616; Tmem129.
eggNOG; KOG3899; Eukaryota.
eggNOG; ENOG410XT2B; LUCA.
GeneTree; ENSGT00390000013284; -.
HOGENOM; HOG000006582; -.
HOVERGEN; HBG097695; -.
InParanoid; Q8K304; -.
KO; K22380; -.
OMA; CIGCMQT; -.
OrthoDB; EOG091G0AYM; -.
PhylomeDB; Q8K304; -.
TreeFam; TF314487; -.
UniPathway; UPA00143; -.
PRO; PR:Q8K304; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000019295; Expressed in 286 organ(s), highest expression level in cerebral cortex.
CleanEx; MM_TMEM129; -.
ExpressionAtlas; Q8K304; baseline and differential.
Genevisible; Q8K304; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
InterPro; IPR018801; TM129.
PANTHER; PTHR31322; PTHR31322; 1.
Pfam; PF10272; Tmpp129; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Membrane; Metal-binding; Reference proteome; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Unfolded protein response; Zinc; Zinc-finger.
CHAIN 1 362 E3 ubiquitin-protein ligase TM129.
/FTId=PRO_0000291042.
TOPO_DOM 1 6 Lumenal. {ECO:0000255}.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TOPO_DOM 28 56 Cytoplasmic. {ECO:0000255}.
TRANSMEM 57 77 Helical. {ECO:0000255}.
TOPO_DOM 78 94 Lumenal. {ECO:0000255}.
TRANSMEM 95 115 Helical. {ECO:0000255}.
TOPO_DOM 116 362 Cytoplasmic. {ECO:0000255}.
ZN_FING 285 350 RING-type; degenerate.
VAR_SEQ 1 71 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_026159.
CONFLICT 69 69 G -> A (in Ref. 1; BAB22394).
{ECO:0000305}.
CONFLICT 322 322 C -> R (in Ref. 1; BAE42795).
{ECO:0000305}.
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


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