ID   GHRL_HUMAN              Reviewed;         117 AA.
AC   Q9UBU3; A8CF34; A8CF38; A8CF42; A8DN29; A8DN30; Q86YP8; Q8TAT9; Q9H3R3;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 217.
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   AltName: Full=Protein M46;
DE   Contains:
DE     RecName: Full=Ghrelin-27;
DE   Contains:
DE     RecName: Full=Ghrelin-28;
DE              Short=Ghrelin;
DE   Contains:
DE     RecName: Full=Obestatin;
DE   Flags: Precursor;
GN   Name=GHRL; Synonyms=MTLRP; ORFNames=UNQ524/PRO1066;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ACYLATION AT SER-26.
RC   TISSUE=Stomach;
RX   PubMed=10604470; DOI=10.1038/45230;
RA   Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K.;
RT   "Ghrelin is a growth-hormone-releasing acylated peptide from stomach.";
RL   Nature 402:656-660(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 24-33.
RC   TISSUE=Stomach;
RX   PubMed=10930375; DOI=10.1053/gast.2000.9371;
RA   Tomasetto C., Karam S.M., Ribieras S., Masson R., Lefebvre O., Staub A.,
RA   Alexander G., Chenard M.-P., Rio M.-C.;
RT   "Identification and characterization of a novel gastric peptide hormone:
RT   the motilin-related peptide.";
RL   Gastroenterology 119:395-405(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wajnrajch M.P., Ten I.S., Gertner J.M., Leibel R.L.;
RT   "Genomic organization of the human Ghrelin gene.";
RL   J. Endocr. Genet. 1:231-233(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, ACYLATION AT
RP   SER-26, AND MASS SPECTROMETRY.
RC   TISSUE=Stomach;
RX   PubMed=12414809; DOI=10.1074/jbc.m205366200;
RA   Hosoda H., Kojima M., Mizushima T., Shimizu S., Kangawa K.;
RT   "Structural divergence of human ghrelin. Identification of multiple
RT   ghrelin-derived molecules produced by post-translational processing.";
RL   J. Biol. Chem. 278:64-70(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC   TISSUE=Heart, Kidney, Placenta, and Stomach;
RX   PubMed=17727735; DOI=10.1186/1471-2164-8-298;
RA   Seim I., Collet C., Herington A.C., Chopin L.K.;
RT   "Revised genomic structure of the human ghrelin gene and identification of
RT   novel exons, alternative splice variants and natural antisense
RT   transcripts.";
RL   BMC Genomics 8:298-298(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RA   Jeffery P.L., Herington A.C., Chopin L.K.;
RT   "Identification and expression pattern of an exon 3-deleted proghrelin
RT   variant in the prostate.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-72.
RC   TISSUE=Blood;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PROTEIN SEQUENCE OF 24-38.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [12]
RP   FUNCTION.
RX   PubMed=11739476; DOI=10.1210/jcem.86.12.8111;
RA   Wren A.M., Seal L.J., Cohen M.A., Brynes A.E., Frost G.S., Murphy K.G.,
RA   Dhillo W.S., Ghatei M.A., Bloom S.R.;
RT   "Ghrelin enhances appetite and increases food intake in humans.";
RL   J. Clin. Endocrinol. Metab. 86:5992-5992(2001).
RN   [13]
RP   MASS SPECTROMETRY, AND ACYLATION AT SER-26.
RC   TISSUE=Thyroid carcinoma;
RX   PubMed=18443287; DOI=10.1073/pnas.0800708105;
RA   Gutierrez J.A., Solenberg P.J., Perkins D.R., Willency J.A., Knierman M.D.,
RA   Jin Z., Witcher D.R., Luo S., Onyia J.E., Hale J.E.;
RT   "Ghrelin octanoylation mediated by an orphan lipid transferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:6320-6325(2008).
RN   [14]
RP   REVIEW.
RX   PubMed=11306336; DOI=10.1016/s1043-2760(00)00362-3;
RA   Kojima M., Hosoda H., Matsuo H., Kangawa K.;
RT   "Ghrelin: discovery of the natural endogenous ligand for the growth hormone
RT   secretagogue receptor.";
RL   Trends Endocrinol. Metab. 12:118-122(2001).
RN   [15] {ECO:0007744|PDB:7W2Z}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 24-39, FUNCTION, AND
RP   OCTANOYLATION.
RX   PubMed=35027551; DOI=10.1038/s41467-022-27975-9;
RA   Qin J., Cai Y., Xu Z., Ming Q., Ji S.Y., Wu C., Zhang H., Mao C.,
RA   Shen D.D., Hirata K., Ma Y., Yan W., Zhang Y., Shao Z.;
RT   "Molecular mechanism of agonism and inverse agonism in ghrelin receptor.";
RL   Nat. Commun. 13:300-300(2022).
CC   -!- FUNCTION: Precursor of the appetite-regulating peptide ghrelin,
CC       including ghrelin-27 and ghrelin-28. {ECO:0000269|PubMed:11306336,
CC       ECO:0000269|PubMed:35027551}.
CC   -!- FUNCTION: [Ghrelin-27]: Ghrelin is the ligand for growth hormone
CC       secretagogue receptor type 1 (GHSR) (PubMed:10604470, PubMed:35027551).
CC       Induces the release of growth hormone from the pituitary
CC       (PubMed:10604470). Has an appetite-stimulating effect, induces
CC       adiposity and stimulates gastric acid secretion (PubMed:11739476).
CC       Involved in growth regulation (PubMed:10604470).
CC       {ECO:0000269|PubMed:10604470, ECO:0000269|PubMed:11739476,
CC       ECO:0000269|PubMed:35027551}.
CC   -!- FUNCTION: [Ghrelin-28]: Ghrelin is the ligand for growth hormone
CC       secretagogue receptor type 1 (GHSR) (PubMed:10604470, PubMed:35027551).
CC       Octanoylated ghrelin-28 is the most commonly found ghrelin and
CC       octanoylation is essential for the activation of the growth hormone
CC       secretagogue receptor type 1 (GHSR) (PubMed:11306336, PubMed:35027551).
CC       Induces the release of growth hormone from the pituitary
CC       (PubMed:10604470). Has an appetite-stimulating effect, induces
CC       adiposity and stimulates gastric acid secretion (PubMed:11739476).
CC       Involved in growth regulation (PubMed:10604470).
CC       {ECO:0000269|PubMed:10604470, ECO:0000269|PubMed:11306336,
CC       ECO:0000269|PubMed:11739476, ECO:0000269|PubMed:35027551}.
CC   -!- FUNCTION: [Obestatin]: May have an appetite-reducing effect resulting
CC       in decreased food intake (By similarity). May reduce gastric emptying
CC       activity and jejunal motility (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QYH7}.
CC   -!- INTERACTION:
CC       Q9UBU3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10319458, EBI-741480;
CC       Q9UBU3; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10319458, EBI-10173939;
CC       Q9UBU3; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10319458, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9EQX0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Ghrelin;
CC         IsoId=Q9UBU3-1; Sequence=Displayed;
CC       Name=2; Synonyms=des-Gln14-ghrelin;
CC         IsoId=Q9UBU3-2; Sequence=VSP_003245;
CC       Name=3;
CC         IsoId=Q9UBU3-3; Sequence=VSP_041437;
CC       Name=4;
CC         IsoId=Q9UBU3-4; Sequence=VSP_041437, VSP_003245;
CC       Name=5;
CC         IsoId=Q9UBU3-5; Sequence=VSP_041438;
CC       Name=6;
CC         IsoId=Q9UBU3-6; Sequence=VSP_047642;
CC   -!- TISSUE SPECIFICITY: Highest level in stomach. All forms are found in
CC       serum as well. Other tissues compensate for the loss of ghrelin
CC       synthesis in the stomach following gastrectomy.
CC       {ECO:0000269|PubMed:12414809}.
CC   -!- PTM: O-octanoylated by GOAT/MBOAT4 (PubMed:18443287). O-octanoylation
CC       or O-decanoylation is essential for ghrelin activity (PubMed:10604470,
CC       PubMed:35027551). The O-decanoylated forms Ghrelin-27-C10 and Ghrelin-
CC       28-C10 differ in the length of the carbon backbone of the carboxylic
CC       acid bound to Ser-26 (PubMed:10604470). A small fraction of ghrelin,
CC       ghrelin-28-C10:1, may be modified with a singly unsaturated carboxylic
CC       acid (PubMed:10604470). Also O-acetylated and O-butyrylated on Ser-26
CC       to minor levels (PubMed:18443287). {ECO:0000269|PubMed:10604470,
CC       ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:35027551}.
CC   -!- PTM: Amidation of Leu-98 is essential for obestatin activity.
CC       {ECO:0000250|UniProtKB:Q9QYH7}.
CC   -!- MASS SPECTROMETRY: [Ghrelin-28]: Mass=3398.9; Mass_error=0.3;
CC       Method=Electrospray; Note=Ghrelin-28-C10, O-decanoylated form.;
CC       Evidence={ECO:0000269|PubMed:12414809};
CC   -!- MASS SPECTROMETRY: [Ghrelin-28]: Mass=3397.2; Mass_error=0.5;
CC       Method=Electrospray; Note=Ghrelin-28-C10:1, O-decenoylated form.;
CC       Evidence={ECO:0000269|PubMed:12414809};
CC   -!- MASS SPECTROMETRY: [Ghrelin-28]: Mass=3371.3; Mass_error=0.1;
CC       Method=Electrospray; Note=Ghrelin-28-C8, O-octanoylated form.;
CC       Evidence={ECO:0000269|PubMed:12414809};
CC   -!- MASS SPECTROMETRY: [Ghrelin-27]: Mass=3243.6; Mass_error=0.4;
CC       Method=Electrospray; Note=Ghrelin-27-C10, O-decanoylated form.;
CC       Evidence={ECO:0000269|PubMed:12414809};
CC   -!- MASS SPECTROMETRY: [Ghrelin-27]: Mass=3214.6; Mass_error=0.6;
CC       Method=Electrospray; Note=Ghrelin-27-C8, O-octanoylated form.;
CC       Evidence={ECO:0000269|PubMed:12414809};
CC   -!- MASS SPECTROMETRY: [Ghrelin-27]: Mass=3214; Method=MALDI; Note=Ghrelin-
CC       27-C8, O-octanoylated form.; Evidence={ECO:0000269|PubMed:18443287};
CC   -!- MASS SPECTROMETRY: [Ghrelin-28]: Mass=3370; Method=MALDI; Note=Ghrelin-
CC       28-C8, O-octanoylated form.; Evidence={ECO:0000269|PubMed:18443287};
CC   -!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/327/Ghrelin";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66 of
CC       January 2006;
CC       URL="https://www.proteinspotlight.org/back_issues/066";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Ghrelin entry;
CC       URL="https://en.wikipedia.org/wiki/Ghrelin";
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DR   EMBL; AB029434; BAA89371.1; -; mRNA.
DR   EMBL; AJ252278; CAB65733.1; -; mRNA.
DR   EMBL; AF296558; AAG10300.1; -; Genomic_DNA.
DR   EMBL; EU072086; ABV55189.1; -; mRNA.
DR   EMBL; EF549569; ABQ40357.1; -; mRNA.
DR   EMBL; EF549571; ABQ40358.1; -; mRNA.
DR   EMBL; EF549572; ABQ40359.1; -; mRNA.
DR   EMBL; EF549573; ABQ40360.1; -; mRNA.
DR   EMBL; EF549574; ABQ40361.1; -; mRNA.
DR   EMBL; EF549575; ABQ40362.1; -; mRNA.
DR   EMBL; EU072083; ABV55186.1; -; mRNA.
DR   EMBL; EU072084; ABV55187.1; -; mRNA.
DR   EMBL; EU072085; ABV55188.1; -; mRNA.
DR   EMBL; EU072087; ABV55190.1; -; mRNA.
DR   EMBL; AY184207; AAO27351.1; -; mRNA.
DR   EMBL; AY359053; AAQ89412.1; -; mRNA.
DR   EMBL; AC022384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64074.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW64075.1; -; Genomic_DNA.
DR   EMBL; BC025791; AAH25791.1; -; mRNA.
DR   EMBL; AB035700; BAB19045.1; -; mRNA.
DR   CCDS; CCDS33700.1; -. [Q9UBU3-1]
DR   CCDS; CCDS46747.1; -. [Q9UBU3-5]
DR   CCDS; CCDS46748.1; -. [Q9UBU3-3]
DR   CCDS; CCDS46749.1; -. [Q9UBU3-4]
DR   CCDS; CCDS46750.1; -. [Q9UBU3-2]
DR   PIR; A59316; A59316.
DR   RefSeq; NP_001128413.1; NM_001134941.3. [Q9UBU3-2]
DR   RefSeq; NP_001128416.1; NM_001134944.2. [Q9UBU3-3]
DR   RefSeq; NP_001128417.1; NM_001134945.2. [Q9UBU3-4]
DR   RefSeq; NP_001128418.1; NM_001134946.2. [Q9UBU3-5]
DR   RefSeq; NP_001289750.1; NM_001302821.2. [Q9UBU3-1]
DR   RefSeq; NP_001289751.1; NM_001302822.2. [Q9UBU3-1]
DR   RefSeq; NP_001289752.1; NM_001302823.2. [Q9UBU3-2]
DR   RefSeq; NP_001289753.1; NM_001302824.2. [Q9UBU3-1]
DR   RefSeq; NP_001289754.1; NM_001302825.2. [Q9UBU3-1]
DR   RefSeq; NP_057446.1; NM_016362.5. [Q9UBU3-1]
DR   PDB; 6H3E; NMR; -; A=24-41.
DR   PDB; 7F9Y; EM; 2.90 A; C=24-51.
DR   PDB; 7NA7; EM; 2.70 A; L=24-35.
DR   PDB; 7W2Z; EM; 2.80 A; L=24-39.
DR   AlphaFoldDB; Q9UBU3; -.
DR   BMRB; Q9UBU3; -.
DR   EMDB; EMD-24267; -.
DR   EMDB; EMD-31500; -.
DR   EMDB; EMD-32268; -.
DR   SMR; Q9UBU3; -.
DR   BioGRID; 119706; 18.
DR   FunCoup; Q9UBU3; 596.
DR   IntAct; Q9UBU3; 13.
DR   NDEx; IQUERY-CP-GHRL; 6 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000335074; -.
DR   BindingDB; Q9UBU3; -.
DR   ChEMBL; CHEMBL1921664; -.
DR   iPTMnet; Q9UBU3; -.
DR   PhosphoSitePlus; Q9UBU3; -.
DR   BioMuta; GHRL; -.
DR   DMDM; 17865471; -.
DR   MassIVE; Q9UBU3; -.
DR   PaxDb; 9606-ENSP00000335074; -.
DR   PeptideAtlas; Q9UBU3; -.
DR   ProteomicsDB; 84065; -. [Q9UBU3-1]
DR   ProteomicsDB; 84066; -. [Q9UBU3-2]
DR   ProteomicsDB; 84067; -. [Q9UBU3-3]
DR   ProteomicsDB; 84068; -. [Q9UBU3-4]
DR   ProteomicsDB; 84069; -. [Q9UBU3-5]
DR   ABCD; Q9UBU3; 20 sequenced antibodies.
DR   Antibodypedia; 2526; 932 antibodies from 44 providers.
DR   DNASU; 51738; -.
DR   Ensembl; ENST00000287656.11; ENSP00000287656.7; ENSG00000157017.17. [Q9UBU3-2]
DR   Ensembl; ENST00000335542.13; ENSP00000335074.8; ENSG00000157017.17. [Q9UBU3-1]
DR   Ensembl; ENST00000422159.5; ENSP00000405464.1; ENSG00000157017.17. [Q9UBU3-6]
DR   Ensembl; ENST00000429122.1; ENSP00000414819.1; ENSG00000157017.17. [Q9UBU3-1]
DR   Ensembl; ENST00000430179.5; ENSP00000399922.1; ENSG00000157017.17. [Q9UBU3-2]
DR   Ensembl; ENST00000437422.6; ENSP00000416768.2; ENSG00000157017.17. [Q9UBU3-3]
DR   Ensembl; ENST00000439975.6; ENSP00000403725.2; ENSG00000157017.17. [Q9UBU3-5]
DR   Ensembl; ENST00000449238.6; ENSP00000388145.2; ENSG00000157017.17. [Q9UBU3-4]
DR   Ensembl; ENST00000457360.5; ENSP00000391406.1; ENSG00000157017.17. [Q9UBU3-1]
DR   Ensembl; ENST00000910666.1; ENSP00000580725.1; ENSG00000157017.17. [Q9UBU3-1]
DR   Ensembl; ENST00000910668.1; ENSP00000580727.1; ENSG00000157017.17. [Q9UBU3-1]
DR   Ensembl; ENST00000910670.1; ENSP00000580728.1; ENSG00000157017.17. [Q9UBU3-1]
DR   Ensembl; ENST00000910671.1; ENSP00000580730.1; ENSG00000157017.17. [Q9UBU3-1]
DR   GeneID; 51738; -.
DR   KEGG; hsa:51738; -.
DR   MANE-Select; ENST00000335542.13; ENSP00000335074.8; NM_016362.5; NP_057446.1.
DR   UCSC; uc003bvj.2; human. [Q9UBU3-1]
DR   AGR; HGNC:18129; -.
DR   ClinPGx; PA142671740; -.
DR   CTD; 51738; -.
DR   DisGeNET; 51738; -.
DR   GeneCards; GHRL; -.
DR   HGNC; HGNC:18129; GHRL.
DR   HPA; ENSG00000157017; Tissue enriched (stomach).
DR   MalaCards; GHRL; -.
DR   MIM; 605353; gene.
DR   OpenTargets; ENSG00000157017; -.
DR   VEuPathDB; HostDB:ENSG00000157017; -.
DR   eggNOG; ENOG502SFY3; Eukaryota.
DR   GeneTree; ENSGT00390000004064; -.
DR   HOGENOM; CLU_168380_0_0_1; -.
DR   InParanoid; Q9UBU3; -.
DR   OMA; QYQQYGR; -.
DR   OrthoDB; 9896247at2759; -.
DR   PAN-GO; Q9UBU3; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UBU3; -.
DR   PathwayCommons; Q9UBU3; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors. [Q9UBU3-1]
DR   Reactome; R-HSA-416476; G alpha (q) signalling events. [Q9UBU3-1]
DR   Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   SignaLink; Q9UBU3; -.
DR   SIGNOR; Q9UBU3; -.
DR   Agora; ENSG00000157017; -.
DR   BioGRID-ORCS; 51738; 15 hits in 1142 CRISPR screens.
DR   GeneWiki; Ghrelin; -.
DR   GenomeRNAi; 51738; -.
DR   Pharos; Q9UBU3; Tbio.
DR   PRO; PR:Q9UBU3; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9UBU3; protein.
DR   Bgee; ENSG00000157017; Expressed in cardia of stomach and 125 other cell types or tissues.
DR   ExpressionAtlas; Q9UBU3; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0099013; C:neuronal dense core vesicle lumen; IEA:Ensembl.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0031768; F:ghrelin receptor binding; ISS:UniProtKB.
DR   GO; GO:0016608; F:growth hormone-releasing hormone activity; IDA:UniProtKB.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; IMP:UniProtKB.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB.
DR   GO; GO:0008343; P:adult feeding behavior; ISS:HGNC-UCL.
DR   GO; GO:0051216; P:cartilage development; NAS:UniProtKB.
DR   GO; GO:0043400; P:cortisol secretion; NAS:UniProtKB.
DR   GO; GO:0046697; P:decidualization; IDA:UniProtKB.
DR   GO; GO:0016358; P:dendrite development; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001696; P:gastric acid secretion; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; NAS:UniProtKB.
DR   GO; GO:0030252; P:growth hormone secretion; TAS:HGNC-UCL.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; TAS:HGNC-UCL.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; NAS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0042322; P:negative regulation of circadian sleep/wake cycle, REM sleep; IDA:BHF-UCL.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:UniProtKB.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:UniProtKB.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR   GO; GO:1904179; P:positive regulation of adipose tissue development; IEA:Ensembl.
DR   GO; GO:0032100; P:positive regulation of appetite; IDA:UniProtKB.
DR   GO; GO:1903012; P:positive regulation of bone development; IEA:Ensembl.
DR   GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IDA:BHF-UCL.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0051461; P:positive regulation of corticotropin secretion; IDA:BHF-UCL.
DR   GO; GO:0051464; P:positive regulation of cortisol secretion; IDA:BHF-UCL.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:1904000; P:positive regulation of eating behavior; IEA:Ensembl.
DR   GO; GO:1904346; P:positive regulation of gastric mucosal blood circulation; IEA:Ensembl.
DR   GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; IC:BHF-UCL.
DR   GO; GO:0060124; P:positive regulation of growth hormone secretion; IDA:BHF-UCL.
DR   GO; GO:0040010; P:positive regulation of growth rate; IEA:Ensembl.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IC:HGNC-UCL.
DR   GO; GO:0120058; P:positive regulation of small intestinal transit; IEA:Ensembl.
DR   GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:1905333; P:regulation of gastric motility; IEA:Ensembl.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR   GO; GO:0032095; P:regulation of response to food; IBA:GO_Central.
DR   GO; GO:0051969; P:regulation of transmission of nerve impulse; IEA:Ensembl.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR   GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR   InterPro; IPR006737; Motilin_assoc.
DR   InterPro; IPR006738; Motilin_ghrelin.
DR   InterPro; IPR005441; Preproghrelin.
DR   PANTHER; PTHR14122:SF1; APPETITE-REGULATING HORMONE; 1.
DR   PANTHER; PTHR14122; GHRELIN PRECURSOR; 1.
DR   Pfam; PF04643; Motilin_assoc; 1.
DR   Pfam; PF04644; Motilin_ghrelin; 1.
DR   PRINTS; PR01624; GHRELIN.
DR   PDBsum; 6H3E; -.
DR   PDBsum; 7F9Y; -.
DR   PDBsum; 7NA7; -.
DR   PDBsum; 7W2Z; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Amidation; Direct protein sequencing;
KW   Hormone; Lipoprotein; Proteomics identification; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:10930375,
FT                   ECO:0000269|PubMed:15340161"
FT   PEPTIDE         24..51
FT                   /note="Ghrelin-28"
FT                   /id="PRO_0000019202"
FT   PEPTIDE         24..50
FT                   /note="Ghrelin-27"
FT                   /id="PRO_0000019203"
FT   PROPEP          52..75
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000019204"
FT   PEPTIDE         76..98
FT                   /note="Obestatin"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYH7"
FT                   /id="PRO_0000045140"
FT   PROPEP          99..117
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000045141"
FT   REGION          29..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYH7"
FT   LIPID           26
FT                   /note="O-decanoyl serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:10604470,
FT                   ECO:0000269|PubMed:12414809"
FT   LIPID           26
FT                   /note="O-hexanoyl serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT   LIPID           26
FT                   /note="O-octanoyl serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:10604470,
FT                   ECO:0000269|PubMed:12414809, ECO:0000269|PubMed:18443287"
FT   VAR_SEQ         1..75
FT                   /note="MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQQRKESKKPPAKLQPRA
FT                   LAGWLRPEDGGQAEGAEDELEVR -> MFTCWWSYLRSTLAAVPGEASRVQ (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:17727735"
FT                   /id="VSP_041438"
FT   VAR_SEQ         1..36
FT                   /note="MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQ -> MFTCWWSYLRST
FT                   LAAVPGEASRVQ (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17727735"
FT                   /id="VSP_041437"
FT   VAR_SEQ         37
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12414809,
FT                   ECO:0000303|PubMed:17727735"
FT                   /id="VSP_003245"
FT   VAR_SEQ         76..117
FT                   /note="FNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK -> RPQPTS
FT                   DRPQALLTSL (in isoform 6)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_047642"
FT   VARIANT         72
FT                   /note="L -> M (in dbSNP:rs696217)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_050095"
FT   VARIANT         90
FT                   /note="Q -> L (in dbSNP:rs4684677)"
FT                   /id="VAR_029135"
FT   HELIX           32..36
FT                   /evidence="ECO:0007829|PDB:7W2Z"
SQ   SEQUENCE   117 AA;  12911 MW;  39C0572EBECA2755 CRC64;
     MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRVQQRKE SKKPPAKLQP RALAGWLRPE
     DGGQAEGAED ELEVRFNAPF DVGIKLSGVQ YQQHSQALGK FLQDILWEEA KEAPADK
//