Summary: Neurohypophysial hormones, C-terminal Domain
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This is the Wikipedia entry entitled "Neurohypophysial hormone". More...
Neurohypophysial hormone
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| crystal structure analysis of deamino-oxytocin. conformational flexibility and receptor binding | |||||||||
| Identifiers | |||||||||
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| Symbol | Hormone_4 | ||||||||
| Pfam | PF00220 | ||||||||
| InterPro | IPR022423 | ||||||||
| PROSITE | PDOC00237 | ||||||||
| SCOP | 1xy1 | ||||||||
| SUPERFAMILY | 1xy1 | ||||||||
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| solution structure of the monomeric form of a mutant unliganded bovine neurophysin, minimized average structure | |||||||||
| Identifiers | |||||||||
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| Symbol | Hormone_5 | ||||||||
| Pfam | PF00184 | ||||||||
| InterPro | IPR000981 | ||||||||
| PROSITE | PDOC00237 | ||||||||
| SCOP | 1xy2 | ||||||||
| SUPERFAMILY | 1xy2 | ||||||||
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Neurohypophysial hormones is a family of structurally and functionally related peptide hormones that includes oxytocin and vasopressin.
Hypophysis refers to the pituitary gland.
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.[1] 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).[2]
[edit] References
- ^ 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.
- ^ 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. PMID 7591488.
This article incorporates text from the public domain Pfam and InterPro IPR000981
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Neurohypophysial hormones, C-terminal Domain
N-terminal Domain is in hormone5
External database links
| PANDIT: | PF00184 |
| PROSITE: | PDOC00237 |
| Pseudofam: | PF00184 |
| SCOP: | 1xy2 |
| SYSTERS: | Hormone_5 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000981
Oxytocin 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].Gene Ontology
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) |
Domain organisation
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Alignments
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
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Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | hormone5; |
| Type: | Family |
| Author: | Finn RD |
| Number in seed: | 36 |
| Number in full: | 145 |
| Average length of the domain: | 76.60 aa |
| Average identity of full alignment: | 62 % |
| Average coverage of the sequence by the domain: | 55.76 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 79 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
Archea
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Unclassified sequence
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Interactions
There is 1 interaction for this family. More...
Hormone_5Structures
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 3 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence