SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00020381 
UniProt Accession
Theoretical PI
5.82  
Molecular Weight
60449 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Tcp1 
Gene Synonyms/Alias
Cct1, Ccta 
Protein Name
T-complex protein 1 subunit alpha 
Protein Synonyms/Alias
TCP-1-alpha CCT-alpha; Tailless complex polypeptide 1A;TCP-1-A Tailless complex polypeptide 1B;TCP-1-B 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:17;13108567-13117933;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.95811523 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. The mouse t haplotypes show defects in spermatogenesis attributed to multiple loci on chromosome 17. We have cloned the gene for an abundant testicular germ cell protein, t complex polypeptide 1, which has a variant form in t haplotypes, TCP-1A. A cDNA clone, pB1.4, which hybridizes to a 19S mRNA that is abundant in haploid cells during mouse spermatogenesis, derives from the 3' end of the mRNA encoding TCP-1B. The Tcp-1 gene appears to be a member of a novel gene family and shows multiple changes between the predicted amino acid sequences of TCP-1B and TCP-1A. An additional Taq1 site is created by a T to C transition in the predicted open reading frame of the Tcp-1a gene. The resultant RFLP has allowed typing of the Tcp-1 gene cluster in 54 complete and partial t haplotype chromosomes. DNA sequence comparison of the Tcp-1 genes suggests that the t haplotype chromosome arose within the genus Mus more than one million years ago. PMID: [3753900] 


3. We have isolated complete cDNA clones encoding the mouse t-complex polypeptides 1A and 1B (TCP-1A and TCP-1B) from t-haplotype and wild-type (wt) mice, respectively. The complete nucleotide (nt) sequence of the Tcp-1a cDNA was determined. The Tcp-1a cDNA has an open reading frame (ORF) encoding a 60-kDa protein of 556 amino acids (aa). A comparison of nt sequences between the Tcp-1a and Tcp-1b cDNAs revealed that the 1786-bp regions upstream from their polyadenylation signals differed by 17 substitutions and that Tcp-1a had different polyadenylation sites from Tcp-1b. In these ORFs, 15 bp were substituted between the two alleles, occurring in 14 codons and resulting in eleven single-aa substitutions. Among these 15 substitutions, twelve were nonsynonymous (aa change) and three were synonymous (no aa change). The aa substitution in TCP-1 has occurred at least 20 times faster between t-haplotype and wt than between mouse and human or mouse and Drosophila. PMID: [1937024] 

4. The nucleotide (nt) sequence of the structural gene (Tcp-1) encoding mouse t-complex polypeptide 1 (TCP-1) has been determined. The nt sequence extending to 10,043 bp shows that the Tcp-1 gene is divided into 12 exons, 11 introns and 5'- and 3'-flanking regions. The Tcp-1 gene has a tight cluster of major transcription start points (tsp). Two GC boxes, one CCAAT box and some other possible regulatory elements are located in the region upstream from the tsp, but no TATA box was found. Extending from the 5'-flanking region to the first intron, a CpG dinucleotide-rich cluster is located. In addition, Tcp-1 gene transcripts in mouse organs, embryos and cultured cells were analyzed by Northern blotting. The Tcp-1 mRNA is enriched not only in testes, but also in early post-implantation embryos and some cultured cell lines, as compared with mouse organs other than the testis. The amount of Tcp-1 mRNA in embryos decreases during development. These results suggest that the expression of the Tcp-1 gene may be regulated spatially and temporally in embryonic and adult mice by transcriptional control or by mRNA stability. PMID: [1383093] 

5. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

6. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

7. Kinases play a prominent role in tumor development, pointing to the presence of specific phosphorylation patterns in tumor tissues. Here, we investigate whether recently developed high resolution mass spectrometric (MS) methods for proteome and phosphoproteome analysis can also be applied to solid tumors. As tumor model, we used TG3 mutant mice carrying skin melanomas. At total of 100 microg of solid tumor lysate yielded a melanoma proteome of 4443 identified proteins, including at least 88 putative melanoma markers previously found by cDNA microarray technology. Analysis of 2 mg of lysate from dissected melanoma with titansphere chromatography and 8 mg with strong cation exchange together resulted in the identification of more than 5600 phosphorylation sites on 2250 proteins. The phosphoproteome included many hits from pathways important in melanoma. One-month storage at -80 degrees C did not significantly decrease the number of identified phosphorylation sites. Thus, solid tumor can be analyzed by MS-based proteomics with similar efficiency as cell culture models and in amounts compatible with biopsies. PMID: [19367708] 

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Function
Molecular chaperone; assists the folding of proteinsupon ATP hydrolysis. As part of the BBS/CCT complex may play arole in the assembly of BBSome, a complex involved in ciliogenesisregulating transports vesicles to the cilia. Known to play a role,in vitro, in the folding of actin and tubulin (By similarity). 
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Subcellular Location
Cytoplasm. Cytoplasm, cytoskeleton,centrosome (By similarity). 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0030054 C:cell junction IEA:Compara.
GO:0005832 C:chaperonin-containing T-complex IDA:MGI.
GO:0005794 C:Golgi apparatus IEA:Compara.
GO:0005874 C:microtubule IEA:Compara.
GO:0005720 C:nuclear heterochromatin IDA:MGI.
GO:0000242 C:pericentriolar material IDA:MGI.
GO:0005886 C:plasma membrane IEA:Compara.
GO:0005524 F:ATP binding IEA:UniProtKB-KW.
GO:0006457 P:protein folding IEA:InterPro.
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Interpro
IPR012715;    Chap_CCT_alpha.
IPR017998;    Chaperone_TCP-1.
IPR002194;    Chaperonin_TCP-1_CS.
IPR002423;    Cpn60/TCP-1.
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Pfam
PF00118;    Cpn60_TCP1;    1.
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SMART
PROSITE
PS00750;    TCP1_1;    1.
PS00751;    TCP1_2;    1.
PS00995;    TCP1_3;    1.
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PRINTS
PR00304;    TCOMPLEXTCP1.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    556       T-complex protein 1 subunit alpha.
                             /FTId=PRO_0000128305.
MOD_RES       1      1       N-acetylmethionine.
MOD_RES     544    544       Phosphoserine.
MOD_RES     551    551       Phosphoserine.
VAR_SEQ       1     49       Missing (in isoform 2).
                             /FTId=VSP_024734.
VAR_SEQ      50     50       G -> M (in isoform 2).
                             /FTId=VSP_024735.
CONFLICT     17     17       V -> I (in Ref. 1; AAA40337, 3; BAA14356
                             and 5; BAE30084).
CONFLICT     36     36       F -> L (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    140    140       T -> A (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    149    151       INA -> TNT (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    151    151       A -> T (in Ref. 1; AAA40338).
CONFLICT    177    177       L -> H (in Ref. 5; BAE31381).
CONFLICT    192    192       V -> I (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    217    217       N -> D (in Ref. 5; BAE39599).
CONFLICT    259    259       K -> E (in Ref. 5; BAE31381).
CONFLICT    296    296       Y -> C (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    318    318       H -> C (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    326    326       S -> T (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    378    378       R -> Q (in Ref. 5; BAE30084).
CONFLICT    402    402       V -> I (in Ref. 5; BAE30407/BAE31988).
CONFLICT    405    405       L -> S (in Ref. 1; AAA40337 and 3;
                             BAA14356).
CONFLICT    429    429       S -> N (in Ref. 1; AAA40338).
CONFLICT    439    439       A -> V (in Ref. 5; BAE31381).
CONFLICT    454    454       V -> M (in Ref. 5; BAE39052).
CONFLICT    494    494       K -> N (in Ref. 5; BAE30407).
CONFLICT    537    537       S -> C (in Ref. 1; AAA40337 and 3;
                             BAA14356).
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Nucleotide Sequence
Length: 863 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 556 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data
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