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Identification and preliminary characterization of mouse Adam33.

Gunn TM, Azarani A, Kim PH, Hyman RW, Davis RW, Barsh GS - BMC Genet. (2002)

Bottom Line: The metalloprotease-disintegrin family, or ADAM, proteins, are implicated in cell-cell interactions, cell fusion, and cell signaling, and are widely distributed among metazoan phyla.Orthologous relationships have been defined for a few ADAM proteins including ADAM10 (Kuzbanian), and ADAM17 (TACE), but evolutionary relationships are not clear for the majority of family members.Adam33 is expressed in the mouse adult brain and could play a role in complex processes that require cell-cell communication.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Pediatrics, and the Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA, USA.

ABSTRACT

Background: The metalloprotease-disintegrin family, or ADAM, proteins, are implicated in cell-cell interactions, cell fusion, and cell signaling, and are widely distributed among metazoan phyla. Orthologous relationships have been defined for a few ADAM proteins including ADAM10 (Kuzbanian), and ADAM17 (TACE), but evolutionary relationships are not clear for the majority of family members. Human ADAM33 refers to a testis cDNA clone that does not contain a complete open reading frame, but portions of the predicted protein are similar to Xenopus laevis ADAM13.

Results: In a 48 kb region of mouse DNA adjacent to the Attractin gene on mouse chromosome 2, we identified sequences very similar to human ADAM33. A full-length mouse cDNA was identified by a combination of gene prediction programs and RT-PCR, and the probable full-length human cDNA was identified by comparison to human genomic sequence in the homologous region on chromosome 20p13. Mouse ADAM33 is 44% identical to Xenopus laevis ADAM13, however a phylogenetic alignment and consideration of functional domains suggests that the two genes are not orthologous. Mouse Adam33 is widely expressed, most highly in the adult brain, heart, kidney, lung and testis.

Conclusions: While mouse ADAM33 is similar to Xenopus ADAM13 in sequence, further examination of its embryonic expression pattern, catalytic activity and protein interactions will be required to assess the functional relationship between these two proteins. Adam33 is expressed in the mouse adult brain and could play a role in complex processes that require cell-cell communication.

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Amino acid similarity among mouse (m) and human (h) ADAM33 proteins, and Xenopus laevis (X) ADAM13. Residues identical to the mouse protein are indicated in bold. Putative signal sequence cleavage sites (SS) are indicated by arrow. The metalloprotease site (MP), disintegrin loop (DL) and transmembrane domain (TM) are boxed and cysteine residues are highlighted by black boxes. The metalloprotease (MPD), disintegrin-like (DD), cysteine-rich (CRD), and EGF-like (EGF) domains are indicated.
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Figure 2: Amino acid similarity among mouse (m) and human (h) ADAM33 proteins, and Xenopus laevis (X) ADAM13. Residues identical to the mouse protein are indicated in bold. Putative signal sequence cleavage sites (SS) are indicated by arrow. The metalloprotease site (MP), disintegrin loop (DL) and transmembrane domain (TM) are boxed and cysteine residues are highlighted by black boxes. The metalloprotease (MPD), disintegrin-like (DD), cysteine-rich (CRD), and EGF-like (EGF) domains are indicated.

Mentions: The full-length Adam33 cDNA sequence was predicted using Genscan, GRAIL, and sequence data from EST clones, to identify exons within a ~48 kb contig of genomic DNA (Genbank AF155960). The predicted cDNA sequence was confirmed by sequencing RT-PCR products amplified from adult brain RNA. Adam33 lies centromere-distal to Atrn and Gfra4 and centromere-proximal to Sn and Cdc25b (Figure 1A). Beginning with the putative translational initiation site, the Adam33 cDNA consists of 22 exons spanning 12671 bp of genomic DNA and corresponds to a 2771 bp cDNA of which 2391 bp are protein-coding (Figure 1B, 2). The predicted 797 amino acid protein is most closely related to Xenopus laevis X-ADAM13 (44% identity, 58% similarity) and X-MDC13 (43% identity, 57% similarity), and to mouse ADAM12 (38% identity, 51% similarity) and ADAM19 (39 % identity, 53% similarity).


Identification and preliminary characterization of mouse Adam33.

Gunn TM, Azarani A, Kim PH, Hyman RW, Davis RW, Barsh GS - BMC Genet. (2002)

Amino acid similarity among mouse (m) and human (h) ADAM33 proteins, and Xenopus laevis (X) ADAM13. Residues identical to the mouse protein are indicated in bold. Putative signal sequence cleavage sites (SS) are indicated by arrow. The metalloprotease site (MP), disintegrin loop (DL) and transmembrane domain (TM) are boxed and cysteine residues are highlighted by black boxes. The metalloprotease (MPD), disintegrin-like (DD), cysteine-rich (CRD), and EGF-like (EGF) domains are indicated.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC88886&req=5

Figure 2: Amino acid similarity among mouse (m) and human (h) ADAM33 proteins, and Xenopus laevis (X) ADAM13. Residues identical to the mouse protein are indicated in bold. Putative signal sequence cleavage sites (SS) are indicated by arrow. The metalloprotease site (MP), disintegrin loop (DL) and transmembrane domain (TM) are boxed and cysteine residues are highlighted by black boxes. The metalloprotease (MPD), disintegrin-like (DD), cysteine-rich (CRD), and EGF-like (EGF) domains are indicated.
Mentions: The full-length Adam33 cDNA sequence was predicted using Genscan, GRAIL, and sequence data from EST clones, to identify exons within a ~48 kb contig of genomic DNA (Genbank AF155960). The predicted cDNA sequence was confirmed by sequencing RT-PCR products amplified from adult brain RNA. Adam33 lies centromere-distal to Atrn and Gfra4 and centromere-proximal to Sn and Cdc25b (Figure 1A). Beginning with the putative translational initiation site, the Adam33 cDNA consists of 22 exons spanning 12671 bp of genomic DNA and corresponds to a 2771 bp cDNA of which 2391 bp are protein-coding (Figure 1B, 2). The predicted 797 amino acid protein is most closely related to Xenopus laevis X-ADAM13 (44% identity, 58% similarity) and X-MDC13 (43% identity, 57% similarity), and to mouse ADAM12 (38% identity, 51% similarity) and ADAM19 (39 % identity, 53% similarity).

Bottom Line: The metalloprotease-disintegrin family, or ADAM, proteins, are implicated in cell-cell interactions, cell fusion, and cell signaling, and are widely distributed among metazoan phyla.Orthologous relationships have been defined for a few ADAM proteins including ADAM10 (Kuzbanian), and ADAM17 (TACE), but evolutionary relationships are not clear for the majority of family members.Adam33 is expressed in the mouse adult brain and could play a role in complex processes that require cell-cell communication.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Pediatrics, and the Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA, USA.

ABSTRACT

Background: The metalloprotease-disintegrin family, or ADAM, proteins, are implicated in cell-cell interactions, cell fusion, and cell signaling, and are widely distributed among metazoan phyla. Orthologous relationships have been defined for a few ADAM proteins including ADAM10 (Kuzbanian), and ADAM17 (TACE), but evolutionary relationships are not clear for the majority of family members. Human ADAM33 refers to a testis cDNA clone that does not contain a complete open reading frame, but portions of the predicted protein are similar to Xenopus laevis ADAM13.

Results: In a 48 kb region of mouse DNA adjacent to the Attractin gene on mouse chromosome 2, we identified sequences very similar to human ADAM33. A full-length mouse cDNA was identified by a combination of gene prediction programs and RT-PCR, and the probable full-length human cDNA was identified by comparison to human genomic sequence in the homologous region on chromosome 20p13. Mouse ADAM33 is 44% identical to Xenopus laevis ADAM13, however a phylogenetic alignment and consideration of functional domains suggests that the two genes are not orthologous. Mouse Adam33 is widely expressed, most highly in the adult brain, heart, kidney, lung and testis.

Conclusions: While mouse ADAM33 is similar to Xenopus ADAM13 in sequence, further examination of its embryonic expression pattern, catalytic activity and protein interactions will be required to assess the functional relationship between these two proteins. Adam33 is expressed in the mouse adult brain and could play a role in complex processes that require cell-cell communication.

Show MeSH
Related in: MedlinePlus