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The image-based fine-grained identification of individual giant pandas (Ailuropoda melanoleuca) is an emerging technology, and it is extraordinarily challenging due to the extremely subtle visual differences between individual giant pandas and limited annotated training data. To address these challenges, we propose the Feature-Fusion Convolutional Neural Network with Patch Detector (FFCNN-PD) algorithm, which exploits the discriminative local patches and builds a hierarchical representation generated by fusing both global and local features. Specifically, an attentional cross-channel pooling is embedded in the FFCNN-PD to improve the class- specific patch detectors. In addition, we propose a new giant panda identification dataset (iPanda-30) to establish a benchmark. Experiments on the proposed iPanda-30 dataset and other fine-grained recognition datasets demonstrate the effectiveness of the FFCNN-PD algorithm against the existing state-of-the-arts.

Transposable elements are very common in genomes and play and important role in evolution. Recently, using the next generation sequencing technologies more and more non-traditional genomes such as the giant panda are being sequenced. Identifying transposable elements from such species is important for the population and conservation study of those species. In this paper we conducted a study to identify the genomie repetitive elements in the giant panda genome (Ailuropoda melanoleuca). We used two repetitive sequence identification methods and a short read mapping method to identify, compare and annotate giant panda transposable elements.

To explore the structure characteristic of rpL13 gene of Ailuropoda melanoleuca, RT-PCR and PCR strategy were employe d to isolate cDNA and genomic sequence of this gene from A. melanoleuca respectively, followed by sequencing and analyz ing preliminarily. The results indicated that the length of cDNA fragment cloned was 660 bp, containing an open reading frame of 636 bp, encoding 211 amino acids of deduced protein with an estimated molecular weight of 24.29 KD and PI of 12.17. The length of the genomic sequence is 1831 bp, with five exons and four introns. Alignment analysis indicate d that rpL13 is highly similarity with the reported species both at the level of DNA and protein. The predicted protein possessed 3 different patterns of functional sites. The results presented here will enrich the rpL13 gene database.

Ribosomal protein S9 is a component of the 40S ribosomal submit, encoded by the RPS9 gene in eucaryotic cell. It belongs to the S4P family of ribosomal proteins. To explore the structure characteristic of RPS9 gene of giant panda (Ailuropoda melanoleuca), primers were designed according to the known nucleotide sequence of RPS9 genes to clone the cDNA and genomic sequences of RPS9 gene of A. melanoleuca by RT-PCR and PCR strategy respectively, followed by sequencing and analyzing preliminarily. The results indicated that the cDNA fragment of RPS9 from giant panda was 637 bp in size, containing an open reading frame (ORF) of 585 bp, encoding 194 amino acids. The length of the genomic sequence was 6,193 bp, with four exons and three introns. The coding sequence shows a high degree of homology to those of Homo sapiens, Bos taurus, Canis lupus, Mus musculus and Rattus norvegicus by 92.65, 91.11, 92.48, 88.03, and 87.01%, respectively. The homology for the deduced amino acid sequences reached high up to 99.48%. Primary structure analysis revealed that the molecular weight of the putative RPS9 protein was 22.60 kDa, with a theoretical pI of 11.31. Based on topology prediction, there were four distinct types of functional sites in RPS9 protein of giant panda. The RPS9 gene was overexpressed in E. coli, and the N-terminally His-tagged protein was a 28 kDa polypeptide, in good agreement with the predicted molecular weight. The protein obtained could be purified for studying its function further.

40S ribosomal protein S10 is a protein encoded by the RPS10 gene in human, belonging to the S10E family of ribosomal proteins. To explore the structure characteristic of this gene of Ailuropoda melanoleuca, primers were designed based on the known nucleotide sequence of RPS10 gene. The RT-PCR and PCR strategy were employed to isolate cDNA and genome of RPS10 from A. melanoleuca respectively, followed by sequencing and analyz ing preliminarily. The results indicated that the length of cDNA fragment from giant panda is 549 bp in size, containing an open reading frame (ORF) of 498 bp, encoding 165 amino acids. The he genomic sequence is 5,862 bp in length, with five exons and four introns. The coding sequence shows a high degree of homology to those of Homo sapiens, Bos taurus, Mus musculus, Sus scrofa and Rattus norvegicus; the degree of homology was 92.37%, 94.38%, 89.76%, 92.77% and 89.16 %, respectively, while the homologies for amino acid sequences are 99.39%, 99.39%, 98.18 %, 98.79%, 98.18% and 98.30%, respectively. Primary structure analysis revealed that the molecular weight of the putative RPS10 protein is 18.86 kD, with a theoretical pI of 10.73. Based on topology prediction, there are four distinct types of functional sites in the RPS10 protein of giant panda.

Ribosomal protein L8 is a component of the 60S ribosomal subunit, encoded by the RPL8 gene in eucaryotic cell. The protein belongs to the L2P family of ribosomal proteins. To explore the structure characteristic of RPL8 gene of the Giant Panda, Ailuropoda melanoleuc), we have designed primers based on the known nucleotide sequence of RPL8 genes to clone the cDNA and genomic sequences of RPL8 gene of A. melanoleuca by RT-PCR and PCR strategy respectively, and then the cloned cDNA and genomic sequences were sequenced and analyzed preliminarily. The results indicated that the length of cDNA fragment of the RPL8 from the Giant Panda was 814 bp in size, containing an open reading frame (ORF) of 774 bp, encoding 257 amino acids. The length of the genomic sequence was 2,370 bp, with five exons and four introns. The coding sequence showed a high degree of homology to those of Homo sapiens, Bos taurus, Canis lupus, Mus musculus and Rattus norvegicus by 92.12, 90.11, 95.99, 86.46, and 88.50%, respectively. The homologies for the deduced amino acid sequences reached high up to 100%. Primary structure analysis revealed that the molecular weight of the putative RPL8 protein was 28.02 kD, with a theoretical pI of 11.65. Based on topology prediction, there were one cAMP- and cGMP-dependent protein kinase phosphorylation site, four protein kinase C phosphorylation site, two casein kinase II phosphorylation site, seven N-myristoylation sites, two Amidation site and one Ribosomal protein L2 signature in the RPL8 protein of the Giant Panda.

Interleukin-18 (IL-18) is a novel proinflammatory cytokine with potent interferon (IFN)-γ inducing activity that plays a crucial biological role in the enhancement of the activity of natural killer cells and cytotoxic T lymphocytes. In the present study, the cloning and sequence analysis of interleukin-18 (IL-18) from the giant panda (Ailuropoda melanoleuca) were described. The results showed that the cloned giant panda IL-18 gene was 582 bp in length, encoding a polypeptide of 192 amino acids. Homology analyses indicated that the identity levels of nucleotide and deduced that amino and acid sequences of IL-18 between the giant panda and other species of mammals ranges from 98.6% to 82.5% and from 96.4% to 73.2%, respectively. The functionally important domains and sites that have previously been recognized in other mammals were all observed in the IL-18 sequence of the giant panda. These result proves that the cDNA fragment cloned is indeed the IL-18 molecule with biological activity and can be used in immunological studies of the giant panda.

RPL18A is a component of the 60S large ribosomal subunit encoded by RPL18A gene, which plays an important role in ribosome. To explore the structure characteristic of ribosomal protein L18 (RPL18A) gene of the Giant Panda (Ailuropoda melanoleuca) and the differences with other species reported,we have designed primers which based on the already-known information of RPL18A gene. Then, the cDNA and the genomic sequence of RPL18A were cloned successfully from the Giant Panda using RT-PCR technology respectively, followed by sequencing and analyzing. The result indicated that the cDNA fragment of the RPL18A cloned from Giant Panda is 571 bp in size, containing an open reading frame of 531bp, and deduced protein was composed of 176 amino acids with an estimated molecular weight of 20.76 kD and PI of 11.42. The length of the genomic sequence is 1999bp, which was found to possess four exons and three introns. Alignment analysis indicated that the nucleotide sequence and the deduced amino acid sequence are highly conserved to other four mammals studied, including Homo sapiens, Mus musculus, Rattus norvegicus and Bos taurus. The homologies for nucleotide sequences of Giant Panda RPL18A with that of these species are 91.53%, 92.66%, 89.27% and 89.83%, respectively, while the homologies for amino acid sequences are 98.86%, 98.86%, 98.30% and 98.30%, respectively. Topology prediction showed there are 4 different patterns of functional sites in the RPL18A protein of the Giant Panda. The cDNA and the genomic sequence of RPL18A were cloned successfully from the Giant Panda in this research, which provided scientific material to enrich and improve the mammals RPL18A gene database.

Ribosomal protein L11 (rpL11) which is a component of the 60s large ribosomal subunit plays an important role in ribosome. To explore the structure characteristic of rpL11 gene of the Ailuropoda melanoleuca, we have designed primers based on the known nucleotide sequence of rpL11 gene. The RT-PCR and PCR strategy were employed to isolate cDNA and genome of rpL11 from the Ailuropoda melanoleuca respectively, sequenced, and analyzed preliminarily. The result indicated that the length of cDNA fragment cloned was 577bp; containing an open reading frame of 537bp. Deduced protein was composed of 178 amino acids with an estimated molecular weight of 20.25kD and PI of 9.97. The length of the genomic sequence is 3701bp, containing five exons and four introns. Alignment analysis indicates that RPL11 is highly similarity with the reported species both at the level of DNA and protein. Topology prediction shows that six different patterns were found in the RPL11 protein of the Ailuropoda melanoleuca. The rpL11 gene of the Ailuropoda melanoleuca was studied in this paper, which will enrich the rpL11 gene database.

fau gene is the cellular homolog of the fox sequence in the Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV). It encodes a fusion protein consisting of the ubiquitin-like protein FUBI at the N-terminus and ribosomal protein S30 at the C-terminus. Here we have cloned the cDNA and the genomic sequence of fau gene from the giant panda (Ailuropoda melanoleuca) using RT-PCR technology and Touchdown-PCR, respectively. The length of of cDNA fragment cloned contains an open reading frame of 414 bp encoding 133 amino acids which estimated molecular weight of the fau is 14.4277 kDa with an isoelectric point (pI) of 10.17 and the length of the genomic sequence is 1143 bp, containing four exons and three introns. Alignment analysis revealed that the nucleotide sequence and the deduced protein sequence are highly conserved to other five species studied, including Mus musculus, Rattus norvegicus, Bos taurus, Sus scrofa, and Homo sapiens. The homologies for nucleotide sequences of giant panda fau to that of these species are 89.80%, 89.55%, 91.29%, 92.79%, and 91.79%, respectively, and the homologies for amino acid sequences are 96.99%, 97.74%, 96.99%, 98.50%, and 96.99%, respectively. Topology prediction showed that there are one cAMP- and cGMP-dependent protein kinase phosphorylation site, two Protein kinase C phosphorylation sites, four Casein kinase II phosphorylation sites, and one Amidation site in the fau protein of the giant panda.