MouseMine: Keyword Search

Publication

First Author:	Symes AJ
Year:	1995
Journal:	J Neurochem
Title:	Differences in nuclear signaling by leukemia inhibitory factor and interferon-gamma: the role of STAT proteins in regulating vasoactive intestinal peptide gene expression.
Volume:	65
Issue:	5
Pages:	1926-33

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Publication

8662697 | J:33244

First Author:	Couvineau A
Year:	1996
Journal:	J Biol Chem
Title:	Vasoactive intestinal peptide (VIP)1 receptor. Three nonadjacent amino acids are responsible for species selectivity with respect to recognition of peptide histidine isoleucineamide.
Volume:	271
Issue:	22
Pages:	12795-800

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Publication

8938447 | J:36735

First Author:	Mackay M
Year:	1996
Journal:	Genomics
Title:	Chromosomal localization in mouse and human of the vasoactive intestinal peptide receptor type 2 gene: a possible contributor to the holoprosencephaly 3 phenotype.
Volume:	37
Issue:	3
Pages:	345-53

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Publication

16709822 | J:131802

First Author:	Huang MC
Year:	2006
Journal:	J Immunol
Title:	Differential signaling of T cell generation of IL-4 by wild-type and short-deletion variant of type 2 G protein-coupled receptor for vasoactive intestinal peptide (VPAC2).
Volume:	176
Issue:	11
Pages:	6640-6

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Publication

22895780 | J:189806

First Author:	de Heuvel E
Year:	2012
Journal:	Am J Physiol Endocrinol Metab
Title:	Glucagon-like peptide 2 induces vasoactive intestinal polypeptide expression in enteric neurons via phophatidylinositol 3-kinase-γ signaling.
Volume:	303
Issue:	8
Pages:	E994-1005

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Publication

16236773 | J:195109

First Author:	Aubé AC
Year:	2006
Journal:	Gut
Title:	Changes in enteric neurone phenotype and intestinal functions in a transgenic mouse model of enteric glia disruption.
Volume:	55
Issue:	5
Pages:	630-7

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Publication

37946684 | J:354326

First Author:	Kozlova EV
Year:	2023
Journal:	J Neuroendocrinol
Title:	Gene deletion of the PACAP/VIP receptor, VPAC2R, alters glycemic responses during metabolic and psychogenic stress in adult female mice.
Volume:	35
Issue:	11
Pages:	e13354

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Publication

23849776 | J:206687

First Author:	Jiang YH
Year:	2013
Journal:	Am J Hum Genet
Title:	Detection of clinically relevant genetic variants in autism spectrum disorder by whole-genome sequencing.
Volume:	93
Issue:	2
Pages:	249-63

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Publication

38048352 | J:346284

First Author:	Hunyara JL
Year:	2023
Journal:	PLoS Biol
Title:	Teneurin-3 regulates the generation of non-image-forming visual circuitry and responsiveness to light in the suprachiasmatic nucleus.
Volume:	21
Issue:	12
Pages:	e3002412

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Publication

25501546 | J:223849

First Author:	Morampudi V
Year:	2015
Journal:	Am J Physiol Gastrointest Liver Physiol
Title:	Vasoactive intestinal peptide prevents PKCε-induced intestinal epithelial barrier disruption during EPEC infection.
Volume:	308
Issue:	5
Pages:	G389-402

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Publication

29408536 | J:260910

First Author:	Wang J
Year:	2018
Journal:	Exp Cell Res
Title:	Vasoactive intestinal peptide inhibits airway smooth muscle cell proliferation in a mouse model of asthma via the ERK1/2 signaling pathway.
Volume:	364
Issue:	2
Pages:	168-174

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Publication

30097165 | J:266422

First Author:	Satitpitakul V
Year:	2018
Journal:	Am J Pathol
Title:	Vasoactive Intestinal Peptide Promotes Corneal Allograft Survival.
Volume:	188
Issue:	9
Pages:	2016-2024

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Publication

32679229 | J:297480

First Author:	García-Posadas L
Year:	2020
Journal:	Am J Pathol
Title:	Lacrimal Gland Myoepithelial Cells Are Altered in a Mouse Model of Dry Eye Disease.
Volume:	190
Issue:	10
Pages:	2067-2079

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Publication

34658884 | J:312655

First Author:	Ma Y
Year:	2021
Journal:	Front Pharmacol
Title:	Resveratrol on the Metabolic Reprogramming in Liver: Implications for Advanced Atherosclerosis.
Volume:	12

Pages:	747625

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Publication

36423894 | J:334386

First Author:	Gallino L
Year:	2023
Journal:	Biochim Biophys Acta Mol Basis Dis
Title:	Vasoactive intestinal peptide deficiency promotes ovarian dysfunction associated to a proinflammatory microenvironment reminiscent of premature aging.
Volume:	1869
Issue:	2
Pages:	166585

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Publication

36453284 | J:334561

First Author:	Tasaka GI
Year:	2023
Journal:	J Comp Neurol
Title:	The local and long-range input landscape of inhibitory neurons in mouse auditory cortex.
Volume:	531
Issue:	4
Pages:	502-514

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Protein

P97751

Organism:	Mus musculus/domesticus
Length:	459
Fragment?:	false

•

Protein

P41588

Organism:	Mus musculus/domesticus
Length:	437
Fragment?:	false

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Protein

A0A286YDJ3

Organism:	Mus musculus/domesticus
Length:	28
Fragment?:	true

•

Protein

Q546Q8

Organism:	Mus musculus/domesticus
Length:	437
Fragment?:	false

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Publication

10704721 | -

First Author:	Charpin-Elhamri G
Year:	2000
Journal:	Peptides
Title:	Inhibitory effect of sorbin on pepsin secretion in conscious cats and rabbits.
Volume:	21
Issue:	1
Pages:	65-72

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Publication

11481476 | -

First Author:	Kimura A
Year:	2001
Journal:	Proc Natl Acad Sci U S A
Title:	The sorbin homology domain: a motif for the targeting of proteins to lipid rafts.
Volume:	98
Issue:	16
Pages:	9098-103

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Publication

15949647 | -

First Author:	Hand D
Year:	2005
Journal:	Peptides
Title:	Human sorbin is generated via splicing of an alternative transcript from the ArgBP2 gene locus.
Volume:	26
Issue:	7
Pages:	1278-82

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Protein Domain

IPR003127 | SoHo_dom

Type:

Domain

Description:

Sorbin is an active peptide present in the digestive tract, where it has pro-absorptive and anti-secretory effects in different parts of the intestine, including the ability to decrease VIP (vasoactive intestinal peptide) and cholera toxin-induced secretion. It is expressed in some intestinal and pancreatic endocrine tumours in humans [].Sorbin-homology (SoHo) domains are found in adaptor proteins such as vinexin, CAP/ponsin and argBP2, which regulate various cellular functions, including cell adhesion, cytoskeletal organisation, and growth factor signalling []. In addition to the sorbin domain, these proteins contain three SH3 (src homology 3) domains. The sorbin homology domain mediates the interaction of vinexin and CAP with flotillin, which is crucial for the localisation of SH3-binding proteins to the lipid raft, a region of the plasma membrane rich in cholesterol and sphingolipids that acts to concentrate certain signalling molecules. The sorbin homology domain of adaptor proteins may mediate interactions with the lipid raft that are crucial to intracellular communication [].Human sorbin is generated via splicing of an alternative transcript from the ArgBP2 gene locus [].

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Protein

P70205

Organism:	Mus musculus/domesticus
Length:	496
Fragment?:	false

•

Protein

Q8BGA4

Organism:	Mus musculus/domesticus
Length:	459
Fragment?:	true

•

Protein

E9Q3E8

Organism:	Mus musculus/domesticus
Length:	447
Fragment?:	false

•

Protein

E9Q4B3

Organism:	Mus musculus/domesticus
Length:	496
Fragment?:	false

•

Protein

Q8BLT3

Organism:	Mus musculus/domesticus
Length:	496
Fragment?:	false

•

Protein

E9PVE8

Organism:	Mus musculus/domesticus
Length:	524
Fragment?:	false

•

Protein

E9Q968

Organism:	Mus musculus/domesticus
Length:	495
Fragment?:	false

•

Protein

Q6NXJ9

Organism:	Mus musculus/domesticus
Length:	468
Fragment?:	false

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Publication

17204498 | J:140842

First Author:	Ianowski JP
Year:	2007
Journal:	J Physiol
Title:	Mucus secretion by single tracheal submucosal glands from normal and cystic fibrosis transmembrane conductance regulator knockout mice.
Volume:	580
Issue:	Pt 1
Pages:	301-14

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Publication

12860111 | J:119037

First Author:	Miller R
Year:	2003
Journal:	Neuropeptides
Title:	Selective roles for the PC2 processing enzyme in the regulation of peptide neurotransmitter levels in brain and peripheral neuroendocrine tissues of PC2 deficient mice.
Volume:	37
Issue:	3
Pages:	140-8

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Publication

9073449 | J:110705

First Author:	Francis NJ
Year:	1997
Journal:	Dev Biol
Title:	CNTF and LIF are not required for the target-directed acquisition of cholinergic and peptidergic properties by sympathetic neurons in vivo.
Volume:	182
Issue:	1
Pages:	76-87

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Publication

26903947 | J:309708

First Author:	Miller AV
Year:	2016
Journal:	Front Endocrinol (Lausanne)
Title:	Disruption of the Suprachiasmatic Nucleus in Fibroblast Growth Factor Signaling-Deficient Mice.
Volume:	7

Pages:	11

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Publication

30016349 | J:264100

First Author:	Schmahl MJ
Year:	2018
Journal:	PLoS One
Title:	NMR-based metabolic profiling of urine, serum, fecal, and pancreatic tissue samples from the Ptf1a-Cre; LSL-KrasG12D transgenic mouse model of pancreatic cancer.
Volume:	13
Issue:	7
Pages:	e0200658

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Publication

22754499 | J:247457

First Author:	Perrenoud Q
Year:	2012
Journal:	Front Neural Circuits
Title:	Characterization of Type I and Type II nNOS-Expressing Interneurons in the Barrel Cortex of Mouse.
Volume:	6

Pages:	36

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Publication

37887038 | J:350134

First Author:	Wu CY
Year:	2023
Journal:	Biology (Basel)
Title:	Klotho Null Mutation Indirectly Leads to Age-Related Lacrimal Gland Degeneration in Mutant Mice.
Volume:	12
Issue:	10

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Publication

16641377 | J:135747

First Author:	Lee SH
Year:	2006
Journal:	J Neurophysiol
Title:	Excitatory actions of vasoactive intestinal peptide on mouse thalamocortical neurons are mediated by VPAC2 receptors.
Volume:	96
Issue:	2
Pages:	858-71

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Publication

12542655 | J:97141

First Author:	Cutler DJ
Year:	2003
Journal:	Eur J Neurosci
Title:	The mouse VPAC2 receptor confers suprachiasmatic nuclei cellular rhythmicity and responsiveness to vasoactive intestinal polypeptide in vitro.
Volume:	17
Issue:	2
Pages:	197-204

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Publication

32581681 | J:341319

First Author:	Takeuchi S
Year:	2020
Journal:	Front Neurosci
Title:	Activation of the VPAC2 Receptor Impairs Axon Outgrowth and Decreases Dendritic Arborization in Mouse Cortical Neurons by a PKA-Dependent Mechanism.
Volume:	14

Pages:	521

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Publication

21878358 | J:307335

First Author:	Vomhof-DeKrey EE
Year:	2011
Journal:	Peptides
Title:	Radical reversal of vasoactive intestinal peptide (VIP) receptors during early lymphopoiesis.
Volume:	32
Issue:	10
Pages:	2058-66

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Publication

34915098 | J:319668

First Author:	Mansano NDS
Year:	2022
Journal:	Mol Cell Endocrinol
Title:	Vasoactive intestinal peptide exerts an excitatory effect on hypothalamic kisspeptin neurons during estrogen negative feedback.
Volume:	542

Pages:	111532

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Publication

33679297 | J:331673

First Author:	Alamilla J
Year:	2021
Journal:	Front Neurosci
Title:	Altered Light Sensitivity of Circadian Clock in Shank3(+/-) Mouse.
Volume:	15

Pages:	604165

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Publication

11319166 | J:69033

First Author:	Kansaku N
Year:	2001
Journal:	Biol Reprod
Title:	Molecular cloning of chicken vasoactive intestinal polypeptide receptor complementary DNA, tissue distribution and chromosomal localization.
Volume:	64
Issue:	5
Pages:	1575-81

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Publication

14605001 | J:88690

First Author:	Vlotides G
Year:	2004
Journal:	Endocrinology
Title:	Expression of novel neurotrophin-1/B-cell stimulating factor-3 (NNT-1/BSF-3) in murine pituitary folliculostellate TtT/GF cells: pituitary adenylate cyclase-activating polypeptide and vasoactive intestinal peptide-induced stimulation of NNT-1/BSF-3 is mediated by protein kinase A, protein kinase C, and extracellular-signal-regulated kinase1/2 pathways.
Volume:	145
Issue:	2
Pages:	716-27

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Publication

1646711 | -

First Author:	Ishihara T
Year:	1991
Journal:	EMBO J
Title:	Molecular cloning and expression of a cDNA encoding the secretin receptor.
Volume:	10
Issue:	7
Pages:	1635-41

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Publication

1314625 | -

First Author:	Ishihara T
Year:	1992
Journal:	Neuron
Title:	Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.
Volume:	8
Issue:	4
Pages:	811-9

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Publication

1658940 | -

First Author:	Lin HY
Year:	1991
Journal:	Science
Title:	Expression cloning of an adenylate cyclase-coupled calcitonin receptor.
Volume:	254
Issue:	5034
Pages:	1022-4

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Publication

1658941 | -

First Author:	Jüppner H
Year:	1991
Journal:	Science
Title:	A G protein-linked receptor for parathyroid hormone and parathyroid hormone-related peptide.
Volume:	254
Issue:	5034
Pages:	1024-6

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Protein Domain

IPR003290 | GPCR_2_GLP1/glucagon_rcpt

Type:

Family

Description:

G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. The glucagon receptor (GR) plays a central role in regulating the level of blood glucose by controlling the rate ofhepatic glucose production and insulin secretion []. GR is expressed predominantly in liver, kidney, adrenal, lung and stomach, with lower levels of expression detected in brown and white adipose tissue, cerebellum, duodenum and heart []. Their role in the control of blood glucose concentrations makes glucagon and GR especially important to studies of diabetes, in which the loss of control over blood glucose concentrations clinically defines the disease []. GR is similar to the secretin-like receptor superfamily. It can transduce signals leading to the accumulation of two different second messengers - i.e., both cAMP and calcium [].Glucagon-like peptide-1 (GLP-1), which is encoded by the glucagon gene and released from the gut in response to nutrients, is a potent stimulator of glucose-induced insulin secretion and proinsulin gene expression of pancreatic beta-cells [, ]. In humans, GLP-I exerts its physiological effect as an incretin. Patients with insulinoma tumors show uncontrolled insulin hypersecretion []. The GLP-I receptor binds GLP-1 with high affinity and couples to activation of adenylate cyclase []. The receptor specifically binds GLP-1 and not peptides of related structure and function, such as glucagon, gastric inhibitory peptide, VIP or secretin []. It is thought that GLP-I might have effects beyond the pancreas, including the cardiovascular and central nervous systems, where a receptor with the same ligand-binding specificity is found [].

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Protein Domain

IPR003292 | GPCR_2_GLP1_rcpt

Type:

Family

Description:

G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Glucagon-like peptide-1 (GLP-1), which is encoded by the glucagon gene and released from the gut in response to nutrients, is a potent stimulator of glucose-induced insulin secretion and proinsulin gene expression of pancreatic beta-cells [, ]. In humans, GLP-I exerts its physiological effect as an incretin. Patients with insulinoma tumors show uncontrolled insulin hypersecretion []. The GLP-I receptor binds GLP-1 with high affinity and couples to activation of adenylate cyclase []. The receptor specifically binds GLP-1 and not peptides of related structure and function, such as glucagon, gastric inhibitory peptide, VIP or secretin []. It is thought that GLP-I might have effects beyond the pancreas, including the cardiovascular and central nervous systems, where a receptor with the same ligand-binding specificity is found [].

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Publication

22837050 | J:187390

First Author:	Prömel S
Year:	2012
Journal:	Dev Dyn
Title:	Characterization and functional study of a cluster of four highly conserved orphan adhesion-GPCR in mouse.
Volume:	241
Issue:	10
Pages:	1591-602

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Protein

F6ZWT0

Organism:	Mus musculus/domesticus
Length:	186
Fragment?:	true

•

Protein

A0A1B0GRC3

Organism:	Mus musculus/domesticus
Length:	274
Fragment?:	false

•

Protein

D3Z203

Organism:	Mus musculus/domesticus
Length:	212
Fragment?:	true

•

Protein

A0A0R4J1X5

Organism:	Mus musculus/domesticus
Length:	532
Fragment?:	true

•

Publication

7517895 | -

First Author:	van Eyll B
Year:	1994
Journal:	FEBS Lett
Title:	Signal transduction of the GLP-1-receptor cloned from a human insulinoma.
Volume:	348
Issue:	1
Pages:	7-13

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Publication

7843404 | -

First Author:	Wei Y
Year:	1995
Journal:	FEBS Lett
Title:	Tissue-specific expression of the human receptor for glucagon-like peptide-I: brain, heart and pancreatic forms have the same deduced amino acid sequences.
Volume:	358
Issue:	3
Pages:	219-24

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Publication

1326760 | -

First Author:	Thorens B
Year:	1992
Journal:	Proc Natl Acad Sci U S A
Title:	Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1.
Volume:	89
Issue:	18
Pages:	8641-5

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Publication

10391944 | -

First Author:	Abe J
Year:	1999
Journal:	J Biol Chem
Title:	Ig-hepta, a novel member of the G protein-coupled hepta-helical receptor (GPCR) family that has immunoglobulin-like repeats in a long N-terminal extracellular domain and defines a new subfamily of GPCRs.
Volume:	274
Issue:	28
Pages:	19957-64

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Publication

25778400 | J:222167

First Author:	Ariestanti DM
Year:	2015
Journal:	J Biol Chem
Title:	Targeted Disruption of Ig-Hepta/Gpr116 Causes Emphysema-like Symptoms That Are Associated with Alveolar Macrophage Activation.
Volume:	290
Issue:	17
Pages:	11032-40

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Protein Domain

IPR008078 | GPCR_2_Ig-hepta-like_rcpt

Type:

Family

Description:

Ig-Hepta/GPR116 is a member of the G protein-coupled receptor family. It has been named Ig-hepta due to the presence of two immunoglobulin-like repeatsin its large extracellular domain. The receptor is expressedpredominantly in the lung, this expression being strongly inducepostnatally. Biochemical analysis indicates that Ig-hepta/GPR116 is heavilyglycosylated and exists as a disulphide-linked dimer. The receptor appearsto be localised in alveolar walls of the lungs and intercalated cells of thekidney collecting ducts, suggesting a role in regulation of acid-basebalance []. Ig-Hepta/GPR116 is likely to negatively regulate macrophage function and inflammation in the alveoli [].This entry also includes GPR110 and GPR115. Loss of GPR110 and GPR115 function does not result in detectable defects, indicating that genes of this GPCR group might function redundantly [].The secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in amanner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products.

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Publication

10844519 | J:62304

First Author:	Qian BF
Year:	2000
Journal:	Clin Exp Immunol
Title:	Neuroendocrine changes in colon of mice with a disrupted IL-2 gene.
Volume:	120
Issue:	3
Pages:	424-33

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Publication

9681497 | J:48791

First Author:	Wong AO
Year:	1998
Journal:	Endocrinology
Title:	Hypophysiotropic action of pituitary adenylate cyclase-activating polypeptide (PACAP) in the goldfish: immunohistochemical demonstration of PACAP in the pituitary, PACAP stimulation of growth hormone release from pituitary cells, and molecular cloning of pituitary type I PACAP receptor.
Volume:	139
Issue:	8
Pages:	3465-79

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Publication

28385693 | J:253774

First Author:	Jayawardena D
Year:	2017
Journal:	Am J Physiol Gastrointest Liver Physiol
Title:	Expression and localization of VPAC1, the major receptor of vasoactive intestinal peptide along the length of the intestine.
Volume:	313
Issue:	1
Pages:	G16-G25

•

Protein

Q9R1W5

Organism:	Mus musculus/domesticus
Length:	463
Fragment?:	false

•

Protein

A2AR99

Organism:	Mus musculus/domesticus
Length:	463
Fragment?:	false

•

Protein

Q8C4G9

Organism:	Mus musculus/domesticus
Length:	578
Fragment?:	false

•

Publication

7590348 | J:29637

First Author:	Burcelin R
Year:	1995
Journal:	Gene
Title:	Cloning and sequence analysis of the murine glucagon receptor-encoding gene.
Volume:	164
Issue:	2
Pages:	305-10

•

Protein

Q8VHV2

Organism:	Mus musculus/domesticus
Length:	64
Fragment?:	true

•

Protein

D3YV95

Organism:	Mus musculus/domesticus
Length:	174
Fragment?:	true

•

Protein

Q3UNS7

Organism:	Mus musculus/domesticus
Length:	216
Fragment?:	false

•

Protein

A0A0A6YX12

Organism:	Mus musculus/domesticus
Length:	472
Fragment?:	true

•

Protein

Q8BL11

Organism:	Mus musculus/domesticus
Length:	642
Fragment?:	false

•

Protein

Q3UQ38

Organism:	Mus musculus/domesticus
Length:	503
Fragment?:	false

•

Protein

A0A668KM90

Organism:	Mus musculus/domesticus
Length:	673
Fragment?:	false

•

Protein

A0A087WQZ5

Organism:	Mus musculus/domesticus
Length:	112
Fragment?:	true

•

Protein

A0A0G2JG89

Organism:	Mus musculus/domesticus
Length:	197
Fragment?:	true

•

Protein

A0A087WRZ4

Organism:	Mus musculus/domesticus
Length:	136
Fragment?:	true

•

Protein

Q52KJ6

Organism:	Mus musculus/domesticus
Length:	469
Fragment?:	true

•

Protein

Q8BUM8

Organism:	Mus musculus/domesticus
Length:	237
Fragment?:	true

•

Protein

Q6PHM3

Organism:	Mus musculus/domesticus
Length:	618
Fragment?:	false

•

Protein

Q76JQ1

Organism:	Mus musculus/domesticus
Length:	587
Fragment?:	true

•

Protein

O70440

Organism:	Mus musculus/domesticus
Length:	130
Fragment?:	true

•

Protein

A0A0G2JE85

Organism:	Mus musculus/domesticus
Length:	198
Fragment?:	true

•

Protein

A0A087WS42

Organism:	Mus musculus/domesticus
Length:	147
Fragment?:	true

•

Protein

Q6PB68

Organism:	Mus musculus/domesticus
Length:	524
Fragment?:	true

•

Protein

E9Q4H5

Organism:	Mus musculus/domesticus
Length:	642
Fragment?:	false

•

Publication

8384375 | -

First Author:	Jelinek LJ
Year:	1993
Journal:	Science
Title:	Expression cloning and signaling properties of the rat glucagon receptor.
Volume:	259
Issue:	5101
Pages:	1614-6

•

Protein

Q5IXF8

Organism:	Mus musculus/domesticus
Length:	512
Fragment?:	false

•

Protein

Q91V95

Organism:	Mus musculus/domesticus
Length:	546
Fragment?:	false

•

Protein

Q8BJ13

Organism:	Mus musculus/domesticus
Length:	652
Fragment?:	false

•

Protein

Q80T59

Organism:	Mus musculus/domesticus
Length:	127
Fragment?:	true

•

Protein

Q80UD7

Organism:	Mus musculus/domesticus
Length:	106
Fragment?:	true

•

Protein

Q9JIY4

Organism:	Mus musculus/domesticus
Length:	48
Fragment?:	true

•

Protein

F6Y0G3

Organism:	Mus musculus/domesticus
Length:	205
Fragment?:	true

•

Protein

Q0VGH2

Organism:	Mus musculus/domesticus
Length:	210
Fragment?:	false

•

Protein

Q80UB5

Organism:	Mus musculus/domesticus
Length:	151
Fragment?:	true

•

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