Nicalin [Caenorhabditis elegans]
nicalin-like protein( domain architecture ID 10133856)
nicalin-like protein, similar to Human nicalin which regulates assembly and stability of the nicalin-nodal modulator (NOMO) membrane protein complex
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
M28_nicalin_like | cd03882 | M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ... |
121-424 | 1.01e-114 | |||||
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development. : Pssm-ID: 349878 Cd Length: 296 Bit Score: 342.42 E-value: 1.01e-114
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Name | Accession | Description | Interval | E-value | |||||
M28_nicalin_like | cd03882 | M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ... |
121-424 | 1.01e-114 | |||||
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development. Pssm-ID: 349878 Cd Length: 296 Bit Score: 342.42 E-value: 1.01e-114
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Iap | COG2234 | Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
195-417 | 8.64e-11 | |||||
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]; Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 62.46 E-value: 8.64e-11
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Nicastrin | pfam05450 | Nicastrin; Nicastrin and presenilin are two major components of the gamma-secretase complex, ... |
208-405 | 4.92e-08 | |||||
Nicastrin; Nicastrin and presenilin are two major components of the gamma-secretase complex, which executes the intramembrane proteolysis of type I integral membrane proteins such as the amyloid precursor protein (APP) and Notch. Nicastrin is synthesized in fibroblasts and neurons as an endoglycosidase-H-sensitive glycosylated precursor protein (immature nicastrin) and is then modified by complex glycosylation in the Golgi apparatus and by sialylation in the trans-Golgi network (mature nicastrin). A region featured in this family has a fold similar to human transferrin receptor (TfR) and a bacterial aminopeptidase. It is implicated in the pathogenesis of Alzheimer's disease. Pssm-ID: 310213 [Multi-domain] Cd Length: 227 Bit Score: 53.70 E-value: 4.92e-08
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Name | Accession | Description | Interval | E-value | |||||
M28_nicalin_like | cd03882 | M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ... |
121-424 | 1.01e-114 | |||||
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development. Pssm-ID: 349878 Cd Length: 296 Bit Score: 342.42 E-value: 1.01e-114
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M28 | cd02690 | M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
195-420 | 1.93e-21 | |||||
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases. Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 92.41 E-value: 1.93e-21
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Iap | COG2234 | Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
195-417 | 8.64e-11 | |||||
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]; Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 62.46 E-value: 8.64e-11
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Nicastrin | pfam05450 | Nicastrin; Nicastrin and presenilin are two major components of the gamma-secretase complex, ... |
208-405 | 4.92e-08 | |||||
Nicastrin; Nicastrin and presenilin are two major components of the gamma-secretase complex, which executes the intramembrane proteolysis of type I integral membrane proteins such as the amyloid precursor protein (APP) and Notch. Nicastrin is synthesized in fibroblasts and neurons as an endoglycosidase-H-sensitive glycosylated precursor protein (immature nicastrin) and is then modified by complex glycosylation in the Golgi apparatus and by sialylation in the trans-Golgi network (mature nicastrin). A region featured in this family has a fold similar to human transferrin receptor (TfR) and a bacterial aminopeptidase. It is implicated in the pathogenesis of Alzheimer's disease. Pssm-ID: 310213 [Multi-domain] Cd Length: 227 Bit Score: 53.70 E-value: 4.92e-08
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Peptidase_M28 | pfam04389 | Peptidase family M28; |
195-325 | 9.73e-05 | |||||
Peptidase family M28; Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 43.43 E-value: 9.73e-05
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M28_like | cd05643 | M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ... |
184-430 | 2.43e-04 | |||||
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion. Pssm-ID: 349895 [Multi-domain] Cd Length: 290 Bit Score: 43.16 E-value: 2.43e-04
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M28_Nicastrin | cd03881 | M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex; Peptidase M28 family, ... |
190-345 | 3.61e-04 | |||||
M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex; Peptidase M28 family, nicastrin subfamily. Nicastrin is a main component of the gamma-secretase complex, which also contains presenilin, Pen-2 and Aph-1. Its extracellular domain sequence resembles aminopeptidases, but certain catalytic residues are not conserved. It is mainly localized to the endoplasmic reticulum and Golgi. It is highly glycosylated (Mr 120 kDa) and is essential for substrate recognition of the N-terminus of gamma-secretase substrates derived from APP and Notch. Nicastrin facilitates substrate cleavage by the catalytic presenilin subunit in the gamma-secretase complex. One conserved glutamate is especially important, probably because this residue forms an ion pair with the amino terminus of the substrate. This substrate-binding domain is often called the DAP domain (named after DYIGS, the amino acid stretch that modulates amyloid precursor protein (APP) processing, and Peptidase homologous region). The sequence of the substrate N-terminus is apparently not critical for the interaction, but a free amino group is. Thus, nicastrin can be considered a kind of gatekeeper for the gamma-secretase complex: type I membrane proteins that have not shed their ectodomains cannot interact properly with nicastrin and do not gain access to the active site. Dysfunction of gamma-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1). Pssm-ID: 349877 [Multi-domain] Cd Length: 519 Bit Score: 43.18 E-value: 3.61e-04
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M28_like | cd05662 | M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ... |
191-376 | 3.71e-04 | |||||
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain. Pssm-ID: 349912 [Multi-domain] Cd Length: 268 Bit Score: 42.45 E-value: 3.71e-04
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M28_like | cd05640 | M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ... |
194-314 | 5.35e-04 | |||||
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349893 [Multi-domain] Cd Length: 281 Bit Score: 42.05 E-value: 5.35e-04
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M28_like | cd03877 | M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
195-267 | 2.89e-03 | |||||
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution. Pssm-ID: 349874 [Multi-domain] Cd Length: 206 Bit Score: 39.15 E-value: 2.89e-03
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M28_AAP | cd03879 | M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ... |
154-236 | 7.56e-03 | |||||
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position. Pssm-ID: 349875 [Multi-domain] Cd Length: 286 Bit Score: 38.38 E-value: 7.56e-03
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