SMART: Cadherin_pro domain annotation

Cadherin_pro Cadherin prodomain like

SMART accession number:	SM01055
Description:	Cadherins are a family of proteins that mediate calcium dependent cell-cell adhesion. They are activated through cleavage of a prosequence in the late Golgi. This domain corresponds to the folded region of the prosequence, and is termed the prodomain. The prodomain shows structural resemblance to the cadherin domain, but lacks all the features known to be important for cadherin-cadherin interactions (PUBMED:15130472).
Interpro abstract (IPR014868):	Cadherins are a group of proteins that mediate calcium dependent cell-cell adhesion. They are activated through cleavage of a prosequence in the late Golgi. The folded part of the prosequence (termed the prodomain) shows structural resemblance to cadherin adhesive domains, but lacks all the features known to be important for cadherin-cadherin interactions [(PUBMED:15130472)]. This entry represents the caderin prodomain.
Family alignment:	View or

There are 183 Cadherin_pro domains in 183 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Cadherin_pro domain is also avaliable.

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Go to specific node: Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: interaction
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Koch AW, Farooq A, Shan W, Zeng L, Colman DR, Zhou MM
- Structure of the neural (N-) cadherin prodomain reveals a cadherinextracellular domain-like fold without adhesive characteristics.
- Structure. 2004; 12: 793-805
- Display abstract
- Classical cadherins mediate cell-cell adhesion through calcium-dependenthomophilic interactions and are activated through cleavage of aprosequence in the late Golgi. We present here the first three-dimensionalstructure of a classical cadherin prosequence, solved by NMR. Theprototypic prosequence of N-cadherin consists of an Ig-like domain and anunstructured C-terminal region. The folded part of the prosequence-termedprodomain-has a striking structural resemblance to cadherin "adhesive"domains that could not have been predicted from the amino acid sequencedue to low sequence similarities. Our detailed structural and evolutionaryanalysis revealed that prodomains are distant relatives of cadherin"adhesive" domains but lack all the features known to be important forcadherin-cadherin interactions. The presence of an additional"nonadhesive" domain seems to make it impossible to engage homophilicinteractions between cadherins that are necessary to activate adhesion,thus explaining the inactive state of prodomain-bearing cadherins.
Structure (3D structures containing this domain)

Links (links to other resources describing this domain)
PFAM Cadherin_pro
INTERPRO IPR014868

PDB code	Main view	Title
1op4		Solution structure of neural cadherin prodomain
1q55		W-shaped trans interactions of cadherins model based on fitting c-cadherin (1l3w) to 3d map of desmosomes obtained by electron tomography
1q5a		S-shaped trans interactions of cadherins model based on fitting c-cadherin (1l3w) to 3d map of desmosomes obtained by electron tomography
1q5b		Lambda-shaped trans and cis interactions of cadherins model based on fitting c-cadherin (1l3w) to 3d map of desmosomes obtained by electron tomography
1q5c		S-s-lambda-shaped trans and cis interactions of cadherins model based on fitting c-cadherin (1l3w) to 3d map of desmosomes obtained by electron tomography

PFAM	Cadherin_pro
INTERPRO	IPR014868

Cadherin_pro

3D Structures of Cadherin_pro domains in PDB