GRP_BOVIN
ID GRP_BOVIN Reviewed; 134 AA.
AC Q863C3; A6QQP2; Q7M2Y8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Gastrin-releasing peptide;
DE Short=GRP;
DE Contains:
DE RecName: Full=Neuromedin-C;
DE AltName: Full=GRP-(18-27);
DE AltName: Full=GRP-10;
DE AltName: Full=GRP18-27 {ECO:0000250|UniProtKB:Q8R1I2};
DE Flags: Precursor;
GN Name=GRP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-134.
RC TISSUE=Endometrium;
RA Budipitojo T., Sasaki T., Cruzana M.B.C., Kitamura N., Yamada J.;
RT "Molecular cloning of cDNA encoding an endometrial gastrin-releasing
RT peptide (GRP) of cow.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 41-50, AMIDATION AT MET-50, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Adrenal medulla;
RX PubMed=2755876; DOI=10.1016/0196-9781(89)90043-0;
RA Lemaire S., Trifaro J.-M., Chouinard L., Cecyre D., Dessureault J.,
RA Mercier P., Dumont M.;
RT "Structural identification, subcellular localization and secretion of
RT bovine adrenomedullary neuromedin C [GRP-(18-27)].";
RL Peptides 10:355-360(1989).
CC -!- FUNCTION: Stimulates the release of gastrin and other gastrointestinal
CC hormones (By similarity). 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:P63153, ECO:0000250|UniProtKB:Q8R1I2}.
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: Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000269|PubMed:2755876}. Secreted {ECO:0000305|PubMed:2755876}.
CC Cell projection, neuron projection {ECO:0000250|UniProtKB:Q8R1I2}.
CC Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory
CC group, expressed on neuron projections which project into the pre-
CC Botzinger complex. {ECO:0000250|UniProtKB:Q8R1I2}.
CC -!- TISSUE SPECIFICITY: Detected in adrenal medulla (at protein level).
CC {ECO:0000269|PubMed:2755876}.
CC -!- SIMILARITY: Belongs to the bombesin/neuromedin-B/ranatensin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP13050.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC149933; AAI49934.1; -; mRNA.
DR EMBL; AY255852; AAP13050.1; ALT_FRAME; mRNA.
DR PIR; A60647; A60647.
DR RefSeq; NP_001094709.1; NM_001101239.1.
DR AlphaFoldDB; Q863C3; -.
DR STRING; 9913.ENSBTAP00000006297; -.
DR PaxDb; Q863C3; -.
DR Ensembl; ENSBTAT00000006297; ENSBTAP00000006297; ENSBTAG00000004796.
DR GeneID; 615323; -.
DR KEGG; bta:615323; -.
DR CTD; 2922; -.
DR VEuPathDB; HostDB:ENSBTAG00000004796; -.
DR VGNC; VGNC:29664; GRP.
DR eggNOG; ENOG502S4DG; Eukaryota.
DR GeneTree; ENSGT00940000154470; -.
DR HOGENOM; CLU_144892_0_0_1; -.
DR InParanoid; Q863C3; -.
DR OrthoDB; 1427338at2759; -.
DR TreeFam; TF336391; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000004796; Expressed in oviduct epithelium and 86 other tissues.
DR ExpressionAtlas; Q863C3; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR GO; GO:0048565; P:digestive tract development; NAS:AgBase.
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; IBA:GO_Central.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; ISS:UniProtKB.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISS: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:0000250|UniProtKB:P08989"
FT PEPTIDE 24..50
FT /note="Gastrin-releasing peptide"
FT /evidence="ECO:0000250|UniProtKB:P08989"
FT /id="PRO_0000003030"
FT PEPTIDE 41..50
FT /note="Neuromedin-C"
FT /evidence="ECO:0000269|PubMed:2755876"
FT /id="PRO_0000003031"
FT PROPEP 54..134
FT /evidence="ECO:0000269|PubMed:2755876"
FT /id="PRO_0000003032"
FT REGION 95..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Methionine amide"
FT /evidence="ECO:0000269|PubMed:2755876"
FT CONFLICT 17
FT /note="L -> P (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
FT CONFLICT 22..23
FT /note="WA -> SG (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="G -> A (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="E -> ES (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..98
FT /note="ARGHQM -> PEPTRL (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..129
FT /note="PQHEGR -> SQREGG (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="N -> Y (in Ref. 2; AAP13050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 14934 MW; 581CA992A778C961 CRC64;
MRGREVPLVL LALVLCLAPR GWAAPVTAGR GGALAKMYTR GNHWAVGHLM GKKSVAESPQ
LHEEESLKEQ LREYAQWEEA TRNLLSLLQA KGARGHQMPP WEPLSIHQPA WDSEDVSNFK
DTGPQHEGRN PQLN
