GHRL_PIG
ID GHRL_PIG Reviewed; 118 AA.
AC Q9GKY5; A5X8W4; Q2I0G0; Q9BDG8; Q9GKY4;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Appetite-regulating hormone;
DE AltName: Full=Growth hormone secretagogue;
DE AltName: Full=Growth hormone-releasing peptide;
DE AltName: Full=Motilin-related peptide;
DE Contains:
DE RecName: Full=Ghrelin;
DE Contains:
DE RecName: Full=Obestatin;
DE Flags: Precursor;
GN Name=GHRL;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Kojima M.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Stomach;
RA Rousselle J., Lacroix D., Dubreuil P.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ying M., Yang Z.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ying M., Yang Z., Yang W.;
RT "Sequencing and chromosome mapping of pig ghrelin and motilin genes.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Ghrelin]: Ghrelin is the ligand for growth hormone
CC secretagogue receptor type 1 (GHSR). Induces the release of growth
CC hormone from the pituitary. Has an appetite-stimulating effect, induces
CC adiposity and stimulates gastric acid secretion. Involved in growth
CC regulation (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Obestatin]: Obestatin may be the ligand for GPR39. May have
CC an appetite-reducing effect resulting in decreased food intake. May
CC reduce gastric emptying activity and jejunal motility (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ghrelin;
CC IsoId=Q9GKY5-1; Sequence=Displayed;
CC Name=2; Synonyms=des-Gln14-ghrelin;
CC IsoId=Q9GKY5-2; Sequence=VSP_003247;
CC -!- PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation is
CC essential for ghrelin activity. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9EQX0}.
CC -!- PTM: Amidation of Leu-99 is essential for obestatin activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66 of
CC January 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/066";
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DR EMBL; AB035703; BAB19048.1; -; mRNA.
DR EMBL; AB035704; BAB19049.1; -; mRNA.
DR EMBL; AF308930; AAK19243.1; -; mRNA.
DR EMBL; AY028942; AAK30002.1; -; mRNA.
DR EMBL; DQ355969; ABC94728.1; -; mRNA.
DR EMBL; DQ663493; ABG23100.1; -; Genomic_DNA.
DR RefSeq; NP_998972.1; NM_213807.2. [Q9GKY5-1]
DR RefSeq; XP_013837377.1; XM_013981923.1.
DR AlphaFoldDB; Q9GKY5; -.
DR SMR; Q9GKY5; -.
DR STRING; 9823.ENSSSCP00000012327; -.
DR PaxDb; Q9GKY5; -.
DR PRIDE; Q9GKY5; -.
DR Ensembl; ENSSSCT00035110353; ENSSSCP00035048127; ENSSSCG00035080494. [Q9GKY5-1]
DR Ensembl; ENSSSCT00055014509; ENSSSCP00055011407; ENSSSCG00055007434. [Q9GKY5-1]
DR Ensembl; ENSSSCT00065066089; ENSSSCP00065028624; ENSSSCG00065048307. [Q9GKY5-1]
DR GeneID; 396728; -.
DR KEGG; ssc:396728; -.
DR CTD; 51738; -.
DR eggNOG; ENOG502SFY3; Eukaryota.
DR InParanoid; Q9GKY5; -.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR Reactome; R-SSC-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031768; F:ghrelin receptor binding; ISS:UniProtKB.
DR GO; GO:0016608; F:growth hormone-releasing hormone activity; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISS:UniProtKB.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0046697; P:decidualization; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR GO; GO:0001696; P:gastric acid secretion; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IBA:GO_Central.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0032097; P:positive regulation of response to food; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
DR InterPro; IPR006737; Motilin_assoc.
DR InterPro; IPR006738; Motilin_ghrelin.
DR InterPro; IPR005441; Preproghrelin.
DR PANTHER; PTHR14122; PTHR14122; 1.
DR Pfam; PF04643; Motilin_assoc; 1.
DR Pfam; PF04644; Motilin_ghrelin; 1.
DR PRINTS; PR01624; GHRELIN.
PE 3: Inferred from homology;
KW Alternative splicing; Amidation; Hormone; Lipoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT PEPTIDE 25..52
FT /note="Ghrelin"
FT /id="PRO_0000019207"
FT PROPEP 53..76
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019208"
FT PEPTIDE 77..99
FT /note="Obestatin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045144"
FT PROPEP 100..118
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045145"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT LIPID 27
FT /note="O-decanoyl serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT LIPID 27
FT /note="O-hexanoyl serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT LIPID 27
FT /note="O-octanoyl serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT VAR_SEQ 38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.2"
FT /id="VSP_003247"
FT CONFLICT 17
FT /note="L -> P (in Ref. 2; AAK30002)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="K -> E (in Ref. 2; AAK30002)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> N (in Ref. 3; ABC94728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 12786 MW; 856D3E1D6DAB1A76 CRC64;
MPSTGTICSL LLLSVLLMAD LAMAGSSFLS PEHQKVQQRK ESKKPAAKLK PRALEGWLGP
EDSGEVEGTE DKLEIRFNAP CDVGIKLSGA QSDQHGQPLG KFLQDILWEE VTEAPADK
