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cocaine- and amphetamine-regulated transcript protein isoform X1 [Rattus norvegicus]
CART_CTD-like domain-containing protein( domain architecture ID 10533919)
CART_CTD-like domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||
CART | pfam06373 | Cocaine and amphetamine regulated transcript protein (CART); This family consists of several ... |
48-116 | 2.28e-42 | ||
Cocaine and amphetamine regulated transcript protein (CART); This family consists of several cocaine and amphetamine regulated transcript type I protein (CART) sequences. Cocaine and amphetamine regulated transcript (CART) peptide has been shown to be an anorectic peptide that inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. The C-terminal part containing the three disulfide bridges is the biologically active part of the molecule affecting food intake. The solution structure of the active part of CART has a fold equivalent to other functionally distinct small proteins. CART consists mainly of turns and loops spanned by a compact framework composed by a few small stretches of antiparallel beta-sheet common to cystine knots. : Pssm-ID: 461888 Cd Length: 70 Bit Score: 133.66 E-value: 2.28e-42
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Name | Accession | Description | Interval | E-value | ||
CART | pfam06373 | Cocaine and amphetamine regulated transcript protein (CART); This family consists of several ... |
48-116 | 2.28e-42 | ||
Cocaine and amphetamine regulated transcript protein (CART); This family consists of several cocaine and amphetamine regulated transcript type I protein (CART) sequences. Cocaine and amphetamine regulated transcript (CART) peptide has been shown to be an anorectic peptide that inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. The C-terminal part containing the three disulfide bridges is the biologically active part of the molecule affecting food intake. The solution structure of the active part of CART has a fold equivalent to other functionally distinct small proteins. CART consists mainly of turns and loops spanned by a compact framework composed by a few small stretches of antiparallel beta-sheet common to cystine knots. Pssm-ID: 461888 Cd Length: 70 Bit Score: 133.66 E-value: 2.28e-42
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CART_CTD-like | cd22741 | C-terminal domain of cocaine-and amphetamine-regulated transcript protein (CART) and similar ... |
76-116 | 1.06e-21 | ||
C-terminal domain of cocaine-and amphetamine-regulated transcript protein (CART) and similar proteins; Cocaine and amphetamine regulated transcript (CART) protein is a satiety factor closely associated with the actions of leptin and neuropeptide Y. It is an anorectic peptide that inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y. It is regulated by leptin in the hypothalamus. CART has been shown to promote neuronal development and survival in vitro. This model corresponds to the C-terminal domain (CTD) of CART, which belongs to the fold-family of small globular knottins. The CTD, containing the three disulfide bridges, is the biologically active part of the molecule affecting food intake. Pssm-ID: 439357 Cd Length: 41 Bit Score: 80.56 E-value: 1.06e-21
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Name | Accession | Description | Interval | E-value | ||
CART | pfam06373 | Cocaine and amphetamine regulated transcript protein (CART); This family consists of several ... |
48-116 | 2.28e-42 | ||
Cocaine and amphetamine regulated transcript protein (CART); This family consists of several cocaine and amphetamine regulated transcript type I protein (CART) sequences. Cocaine and amphetamine regulated transcript (CART) peptide has been shown to be an anorectic peptide that inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. The C-terminal part containing the three disulfide bridges is the biologically active part of the molecule affecting food intake. The solution structure of the active part of CART has a fold equivalent to other functionally distinct small proteins. CART consists mainly of turns and loops spanned by a compact framework composed by a few small stretches of antiparallel beta-sheet common to cystine knots. Pssm-ID: 461888 Cd Length: 70 Bit Score: 133.66 E-value: 2.28e-42
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CART_CTD-like | cd22741 | C-terminal domain of cocaine-and amphetamine-regulated transcript protein (CART) and similar ... |
76-116 | 1.06e-21 | ||
C-terminal domain of cocaine-and amphetamine-regulated transcript protein (CART) and similar proteins; Cocaine and amphetamine regulated transcript (CART) protein is a satiety factor closely associated with the actions of leptin and neuropeptide Y. It is an anorectic peptide that inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y. It is regulated by leptin in the hypothalamus. CART has been shown to promote neuronal development and survival in vitro. This model corresponds to the C-terminal domain (CTD) of CART, which belongs to the fold-family of small globular knottins. The CTD, containing the three disulfide bridges, is the biologically active part of the molecule affecting food intake. Pssm-ID: 439357 Cd Length: 41 Bit Score: 80.56 E-value: 1.06e-21
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