Summary: Neurohypophysial hormones, C-terminal Domain
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Neurohypophysial hormone Edit Wikipedia article
|Neurohypophysial hormones, N-terminal Domain|
crystal structure analysis of deamino-oxytocin. conformational flexibility and receptor binding
|Neurohypophysial hormones, C-terminal Domain|
solution structure of the monomeric form of a mutant unliganded bovine neurophysin, minimized average structure
The neurohypophysial hormones form a family of structurally and functionally related peptide hormones. Their main representatives are oxytocin and vasopressin. They are named for being secreted by the neurohypophysis, i.e. the posterior pituitary gland (hypophysis refers to the pituitary gland), itself a neuronal projection from the hypothalamus.
Most of the circulating oxytocin and vasopressin hormones are synthesized in magnocellular neurosecretory cells of the supraoptic nucleus and paraventricular nucleus of the hypothalamus. They are then transported in neurosecretory granules along axons within the hypothalamo-neurohypophysial tract by axoplasmic flow to axon terminals forming the pars nervosa of the posterior pituitary. There, they are stored in Herring bodies and can be released into the circulation on the basis of hormonal and synaptic signals with assistance from pituicytes.
Vasopressin and oxytocin are also synthesized in the parvocellular neurosecretory cells of the paraventricular nucleus of the hypothalamus, which project to the median eminence, where they are transported and secreted into the hypophyseal portal system to stimulate the anterior pituitary. Thus they can also be considered as hypophysiotropic hormones.
Oxytocin mediates contraction of the smooth muscle of the uterus and mammary gland, while vasopressin has antidiuretic action on the kidney, and mediates vasoconstriction of the peripheral vessels. Due to the similarity of the two hormones, there is cross-reaction: oxytocin has a slight antidiuretic function, and high levels of AVP can cause uterine contractions. In common with most active peptides, both hormones are synthesised as larger protein precursors that are enzymatically converted to their mature forms.
Members of this family are found in birds, fish, reptiles and amphibians (mesotocin, isotocin, valitocin, glumitocin, aspargtocin, vasotocin, seritocin, asvatocin, phasvatocin), in worms (annetocin, nematocin), octopi (cephalotocin), Locusta migratoria (Migratory locust) (locupressin or neuropeptide F1/F2) and in molluscs (conopressins G and S).
- Burbach JP, Luckman SM, Murphy D, Gainer H (July 2001). "Gene regulation in the magnocellular hypothalamo-neurohypophysial system". Physiol. Rev. 81 (3): 1197–267. PMID 11427695.
- Jones CW, Pickering BT (December 1972). "Intra-axonal transport and turnover of neurohypophysial hormones in the rat". J. Physiol. (Lond.) 227 (2): 553–64. PMC 1331210. PMID 4678722.
- Hatton GI (September 1988). "Pituicytes, glia and control of terminal secretion". J. Exp. Biol. 139: 67–79. PMID 3062122.
- Buma P, Nieuwenhuys R (February 1987). "Ultrastructural demonstration of oxytocin and vasopressin release sites in the neural lobe and median eminence of the rat by tannic acid and immunogold methods". Neurosci. Lett. 74 (2): 151–7. doi:10.1016/0304-3940(87)90141-8. PMID 3574755.
- Antoni FA, Kovács KJ, Dohanits J, Makara GB, Holmes MC, Mazurek MF (June 1988). "Hypophysiotrophic function of vasopressin and oxytocin". Brain Res. Bull. 20 (6): 729–36. doi:10.1016/0361-9230(88)90084-6. PMID 3409054.
- Acher R, Chauvet J (1988). "Structure, processing and evolution of the neurohypophysial hormone-neurophysin precursors". Biochimie 70 (9): 1197–1207. doi:10.1016/0300-9084(88)90185-X. PMID 3147712.
- Li C, Wang W, Summer SN, Westfall TD, Brooks DP, Falk S, Schrier RW (February 2008). "Molecular mechanisms of antidiuretic effect of oxytocin". J. Am. Soc. Nephrol. 19 (2): 225–32. doi:10.1681/ASN.2007010029. PMC 2396735. PMID 18057218.
- Joo KW, Jeon US, Kim GH, Park J, Oh YK, Kim YS, Ahn C, Kim S, Kim SY, Lee JS, Han JS (October 2004). "Antidiuretic action of oxytocin is associated with increased urinary excretion of aquaporin-2". Nephrol. Dial. Transplant. 19 (10): 2480–6. doi:10.1093/ndt/gfh413. PMID 15280526.
- Michel G, Acher R, Chauvet J, Ouedraogo Y, Chou J, Chait BT (1995). "A new neurohypophysial peptide, seritocin ([Ser5,Ile8]-oxytocin), identified in a dryness-resistant African toad, Bufo regularis". Int. J. Pept. Protein Res. 45 (5): 482–487. doi:10.1111/j.1399-3011.1995.tb01064.x. PMID 7591488.
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Neurohypophysial hormones, C-terminal Domain Provide feedback
N-terminal Domain is in hormone5
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000981Oxytocin and vasopressin are nine-residue, structurally and functionally related neurohypophysial peptide hormones. Oxytocin mediates contraction of the smooth muscle of the uterus and mammary gland, while vasopressin has antidiuretic action on the kidney, and mediates vasoconstriction of the peripheral vessels [PUBMED:3147712]. In common with most active peptides, both hormones are synthesised as larger protein precursors that are enzymatically converted to their mature forms. Members of this family are found in birds, fish, reptiles and amphibians (mesotocin, isotocin, valitocin, glumitocin, aspargtocin, vasotocin, seritocin, asvatocin, phasvatocin), in worms (annetocin), octopi (cephalotocin), Locusta migratoria (Migratory locust) (locupressin or neuropeptide F1/F2) and in molluscs (conopressins G and S) [PUBMED:7591488].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Molecular function||neurohypophyseal hormone activity (GO:0005185)|
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Number in seed:||36|
|Number in full:||207|
|Average length of the domain:||77.00 aa|
|Average identity of full alignment:||63 %|
|Average coverage of the sequence by the domain:||55.90 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Hormone_5 domain has been found. There are 29 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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