GRP_PIG
ID GRP_PIG Reviewed; 146 AA.
AC P63153; A0A287ANW4; P01294;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Gastrin-releasing peptide;
DE Short=GRP;
DE Contains:
DE RecName: Full=Neuromedin-C;
DE AltName: Full=GRP-10;
DE AltName: Full=GRP18-27 {ECO:0000250|UniProtKB:Q8R1I2};
DE Flags: Precursor;
GN Name=GRP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:AWR92766.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-50, AND FUNCTION.
RX PubMed=496973; DOI=10.1016/0006-291x(79)91614-0;
RA McDonald T.J., Joernvall H., Nilsson G., Vagne M., Ghatei M., Bloom S.R.,
RA Mutt V.;
RT "Characterization of a gastrin releasing peptide from porcine non-antral
RT gastric tissue.";
RL Biochem. Biophys. Res. Commun. 90:227-233(1979).
RN [4]
RP PROTEIN SEQUENCE OF 41-50, AND AMIDATION AT MET-50.
RX PubMed=6546686; DOI=10.1016/0006-291x(84)91611-5;
RA Minamino N., Kangawa K., Matsuo H.;
RT "Neuromedin C: a bombesin-like peptide identified in porcine spinal cord.";
RL Biochem. Biophys. Res. Commun. 119:14-20(1984).
CC -!- FUNCTION: Stimulates the release of gastrin and other gastrointestinal
CC hormones (PubMed:496973). Contributes to the perception of prurient
CC stimuli and to the transmission of itch signals in the spinal cord that
CC promote scratching behavior (By similarity). Contributes primarily to
CC nonhistaminergic itch sensation (By similarity). In one study, shown to
CC act in the amygdala as part of an inhibitory network which inhibits
CC memory specifically related to learned fear (By similarity). In another
CC study, shown to act on vasoactive intestinal peptide (VIP)-expressing
CC cells in the auditory cortex, most likely via extrasynaptic diffusion
CC from local and long-range sources, to mediate disinhibition of
CC glutamatergic cells via VIP cell-specific GRPR signaling which leads to
CC enhanced auditory fear memories (By similarity). Contributes to the
CC regulation of food intake (By similarity). Inhibits voltage-gated
CC sodium channels but enhances voltage-gated potassium channels in
CC hippocampal neurons (By similarity). Induces sighing by acting directly
CC on the pre-Botzinger complex, a cluster of several thousand neurons in
CC the ventrolateral medulla responsible for inspiration during
CC respiratory activity (By similarity). {ECO:0000250|UniProtKB:P24393,
CC ECO:0000250|UniProtKB:Q8R1I2, ECO:0000269|PubMed:496973}.
CC -!- FUNCTION: [Neuromedin-C]: Induces an itch response through activation
CC of receptors present on mast cells, triggering mast cell degranulation.
CC {ECO:0000250|UniProtKB:Q8R1I2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07492}.
CC Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000250|UniProtKB:Q863C3}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q8R1I2}. Note=In neurons of the retrotrapezoid
CC nucleus/parafacial respiratory group, expressed on neuron projections
CC which project into the pre-Botzinger complex.
CC {ECO:0000250|UniProtKB:Q8R1I2}.
CC -!- SIMILARITY: Belongs to the bombesin/neuromedin-B/ranatensin family.
CC {ECO:0000305}.
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DR EMBL; MF508701; AWR92766.1; -; mRNA.
DR EMBL; AEMK02000004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01562; RHPGA.
DR AlphaFoldDB; P63153; -.
DR STRING; 9823.ENSSSCP00000005286; -.
DR Ensembl; ENSSSCT00000040819; ENSSSCP00000045701; ENSSSCG00000037300.
DR Ensembl; ENSSSCT00025015656; ENSSSCP00025006193; ENSSSCG00025011850.
DR Ensembl; ENSSSCT00045005498; ENSSSCP00045003676; ENSSSCG00045003373.
DR Ensembl; ENSSSCT00055047955; ENSSSCP00055038276; ENSSSCG00055024334.
DR Ensembl; ENSSSCT00065035695; ENSSSCP00065014946; ENSSSCG00065026545.
DR Ensembl; ENSSSCT00070020904; ENSSSCP00070017285; ENSSSCG00070010777.
DR VGNC; VGNC:88707; GRP.
DR GeneTree; ENSGT00940000154470; -.
DR InParanoid; P63153; -.
DR OMA; KDMMDYL; -.
DR OrthoDB; 1427338at2759; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000037300; Expressed in Ammon's horn and 11 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; ISS:UniProtKB.
DR GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:1905151; P:negative regulation of voltage-gated sodium channel activity; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; ISS:UniProtKB.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IMP:UniProtKB.
DR GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; ISS:UniProtKB.
DR InterPro; IPR000874; Bombesin.
DR InterPro; IPR015674; Gastrin-RP.
DR PANTHER; PTHR16866; PTHR16866; 1.
DR PANTHER; PTHR16866:SF2; PTHR16866:SF2; 1.
DR Pfam; PF02044; Bombesin; 1.
DR PROSITE; PS00257; BOMBESIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Cell projection; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Direct protein sequencing; Mast cell degranulation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:496973"
FT PEPTIDE 24..50
FT /note="Gastrin-releasing peptide"
FT /evidence="ECO:0000269|PubMed:496973"
FT /id="PRO_0000045915"
FT PEPTIDE 41..50
FT /note="Neuromedin-C"
FT /evidence="ECO:0000269|PubMed:6546686"
FT /id="PRO_0000003038"
FT PROPEP 54..146
FT /evidence="ECO:0000269|PubMed:496973"
FT /id="PRO_0000455540"
FT REGION 95..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Methionine amide"
FT /evidence="ECO:0000269|PubMed:6546686"
SQ SEQUENCE 146 AA; 16002 MW; 3D127E5AD15B02F3 CRC64;
MRGREFPLVL LALVLCQAPR GPAAPVSVGG GTVLAKMYPR GNHWAVGHLM GKKSTGESPY
AYEGGNMKEQ LREYIRWEDA TRNLLSLLEA KGIGSHQPPQ WEPLGIRQST WDSKDGSNFK
DMGPRLKVDG LSAPGSQHEG RIPQLN
