IED ID |
IndEnz0002012174 |
Enzyme Type ID |
protease012174 |
Protein Name |
Tudor domain-containing protein 6
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Gene Name |
Tdrd6 |
Organism |
Mus musculus (Mouse) |
Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Glires (Rodents and rabbits)
Rodentia
Myomorpha (mice and others)
Muroidea
Muridae
Murinae
Mus
Mus
Mus musculus (Mouse)
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Enzyme Sequence |
MSSTPGLPTPGASLALRVSFVDVHPEVIPVQLWGLVGQRREEYVRLSREIQEAAATRGPWALGGASASPGELCLVQVGLMWHRCRVVSRQAQDSRVFLLDEGRTITAGAGSLAPGRSEFFHLPSEVLGCVLAGLVPAGGGGTGGGEPQQWSPRAVDFLSNLQGKEVHGRVLDVLLLHRLVLLEVPVVSQQMEELGLARQVPDSLFCSLLKRYLTAAGQGSSGAPVLPRAAPKQEHPGLDYFYPQLQLGVTEPVVVTQVCHPHRIHCQLRSLSQEIHRLSESMAQVYRAPVGTDDEDSGSATWEEREESPDKPGSPCASCGLDGQWYRALLLETFRPQRCAQVLHVDYGRKELVSCSSLRYLLPEYFRMPVVTYPCALYGLWDCGRGWSRSQVGDLKALILGQAVNAKIEFYCSFEHMYYVTLYGEDGINLNSAFGVQSCCLADWFLQSQGIEEEEEEDEDEVEAAFQSQSPAEEMEAEVSLPSLRSIRLKMNTFYDAQVEFVKSPSEFWIRLRKHKNTFSKLTKRMCSFYSSASKLDGVILRPEPDDLCCVKWKENGYYRATVTRLDSKSVDVFLVDRGNSENVDWCDVRMLLPQFRQLPILALKCTLADIWPLGKTWSQEATSFFKKTVLHKELVVHVLDKQDHQYVIEILDESRMGEENISKVIAQAGFAKFQEFETKENIRLSAHSPGHVSGHFMAEPSKITSAKKAEGDQRAKKDNKTLSVSEALADTVSLSNLSTAQDTEKVTSDPSLLMLNFLKTKPDCCGKGELEVGSTVEVKVSHIENPGSFWCQLMRNAQGFRTLMCDIEDYCKSSEPSPYEGDTRVCLAKRTASGRWSRALISGAHSLEHVRVVFVDYGDRDVVSTKDILSVSDVFFQVRAQAFRCSLYNLIQPMGENPFVWDEKAVQAFSGFIDSARQNNLELKCTVFALASRHEEEWFNVVDLLTPFQSACRFLVEKRLARPVKHQKPLEPSVQLHSYYYSTHDLKIGSEELVYVTHADDPWTFYCQLARNINVLEQLSYNIMQLSKALLNLKASTLAPGTLCLARYTDGNWYRGIIIEKEPSKVFFVDFGNTYIAVDHLLPIPRDAHDVLLLPMQALKCSLSDIPHHIPEEVTAWFQETVLDKSLKALVVAKDPDGRLIIELYDDSVQINASINEKLGLLGYKNRTRRKEKENEIILHETKALEDKKESVKPSLADYLGKPGESKAHSIEIMGESCKPKMGPACKELRYLQGSAKANLVPPYQDSVGNKNDGGFPLTREKKEDIFASSPMSGTKLDSALPERRMGEPSGRDLPPKFCEFPQKTIAPGFKTSVYVSHINDLSDFYIQLIEDEAEINNLSERLNDVRTRPQYHTGPQWQSGDVICAVFPEDNLWYRALVMEQQPNGLLSVQFIDYGNMSVVHTNRTGRLGPVDAVLPALCLHCSLWGLSVPVCKEMVSYFSQRTDEAQIRCEFVKFQGTWEVILADEHGVIAEDMISRFPCNGNSQAGLTTQTMKGDCLKIANKPNTDTSVLLNWYNPKAKLIKAYATVIDGPEYFWCQFADSEKLQYLETEVQSAGKQLSDRRSCTQCPQIGDPCIVRYREDGHYYRALITNICDGELASVRLVDFGNAEDCVDAKELWSIPSELLLVPMQAFPCCLAGFSVSGGVCPQEGNDYFYDIVTEDVLDITILEIKRDVCNIPLAIVELRSKGENINEKMKKYAKTGVPKNDLSSEKRGPERKGSLASPDLGLKKPSHKIAQDKTFYGEARASELSERLEKDLNIETKTSKFYERSTRSIFNAFENSCKGKMGSERLEGSMDYHFVDRAKFDNNYLITGFNPILAHASEPKELLELSSLEVPLSADNDDECKEFLELESIELQHSPAGEEEKEELGLGSPMAPLSPGCQAGATLESFMMQLPLDCEAEKQLELKLPTPQLSLEDSISPLSAAVSQDIQGSRCSEDERKAGYMGSSDDDHSRSPLLQHGKGGNSPAHDGRNLSEEEFPQFESRDSAALLAPLFSEEEAREGRKCGSMVPAQLQSTYTLKGFSVGSKCVVWSSLRNTWSKCEILELAEEGTRVLNLSNGVEETVSPENVWNGIPKVDKRPSEAVFQTVGKDLPFMPSDDATTKGFSSVSEEEACGGDADSLSTAKLNI |
Enzyme Length |
2134 |
Uniprot Accession Number |
P61407 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
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EC Number |
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Enzyme Function |
FUNCTION: Tudor domain-containing protein involved in germ cell development, more specifically the formation of chromatoid body (during spermiogenesis), Balbiani body (during oogenesis), germ plasm (upon fertilization), and for proper miRNA expression and spliceosome maturation (PubMed:19345099, PubMed:27149095, PubMed:28263986) (By similarity). Essential for RNA-dependent helicase UPF1 localization to chromatoid body, for UPF1-UPF2 and UPF1-DDX4 interactions which are required for mRNA degradation, using the extended 3' UTR-triggered nonsense-mediated mRNA decay (NMD) pathway (PubMed:27149095). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through interaction with arginine N-methyltransferase PRMT5 and symmetrically arginine dimethylated SNRPB (small nuclear ribonucleoprotein-associated protein) (PubMed:28263986). {ECO:0000250|UniProtKB:F1R237, ECO:0000269|PubMed:19345099, ECO:0000269|PubMed:27149095, ECO:0000269|PubMed:28263986}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
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Features |
Chain (1); Compositional bias (3); Domain (6); Modified residue (7); Region (5) |
Keywords |
Cytoplasm;Developmental protein;Differentiation;Oogenesis;Phosphoprotein;Reference proteome;Repeat;Spermatogenesis |
Interact With |
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Induction |
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Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345099, ECO:0000269|PubMed:27149095, ECO:0000269|PubMed:28263986}. Note=Present in chromatoid body (CB) of spermatids, also named processing bodies (P-bodies) in somatic cells (PubMed:17141210, PubMed:19345099, PubMed:27149095). Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids (PubMed:17141210, PubMed:19345099). Colocalizes in CB with DDX4, PIWIL1, PIWIL2, TDRD1 and TDRD7 (PubMed:17141210, PubMed:19345099). {ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345099, ECO:0000269|PubMed:27149095}. |
Modified Residue |
MOD_RES 292; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1723; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1726; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1925; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1980; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2063; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2115; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
Post Translational Modification |
PTM: Undergoes proteolytic cleavage near the C-terminal by an unknown protease during the transition from meiosis I to meiosis II in primary spermatocytes. |
Signal Peptide |
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Structure 3D |
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Cross Reference PDB |
- |
Mapped Pubmed ID |
16093322;
17662146;
21267068;
21383078;
21670278;
25762440;
28444146;
34059773;
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Motif |
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Gene Encoded By |
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Mass |
237,914 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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