ID GHRL_HUMAN Reviewed; 117 AA. AC Q9UBU3; A8CF34; A8CF38; A8CF42; A8DN29; A8DN30; Q86YP8; Q8TAT9; AC Q9H3R3; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 09-DEC-2015, entry version 158. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT 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., RA Staub A., Alexander G., Chenard M.-P., Rio M.-C.; RT "Identification and characterization of a novel gastric peptide RT hormone: 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 RP AT 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 RT identification of novel exons, alternative splice variants and natural RT antisense 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., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics 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., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA 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., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RP 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 RT project: 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 RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [12] 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 RT hormone secretagogue receptor."; RL Trends Endocrinol. Metab. 12:118-122(2001). CC -!- FUNCTION: Ghrelin is the ligand for growth hormone secretagogue CC receptor type 1 (GHSR). Induces the release of growth hormone from CC the pituitary. Has an appetite-stimulating effect, induces CC adiposity and stimulates gastric acid secretion. Involved in CC growth regulation. CC -!- FUNCTION: Obestatin may be the ligand for GPR39. May have an CC appetite-reducing effect resulting in decreased food intake. May CC reduce gastric emptying activity and jejunal motility (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-10319458, EBI-741480; CC Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-10319458, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Secreted. 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 CC in 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-octanoylation or O-decanoylation is essential for ghrelin CC activity. The O-decanoylated forms Ghrelin-27-C10 and Ghrelin-28- CC C10 differ in the length of the carbon backbone of the carboxylic CC acid bound to Ser-26. A small fraction of ghrelin, ghrelin-28- CC C10:1, may be modified with a singly unsaturated carboxylic acid CC (PubMed:10604470). {ECO:0000269|PubMed:10604470}. CC -!- PTM: Amidation of Leu-98 is essential for obestatin activity. CC {ECO:0000250}. CC -!- MASS SPECTROMETRY: Mass=3398.9; Mass_error=0.3; CC Method=Electrospray; Range=24-51; Note=Ghrelin-28-C10, O- CC decanoylated form.; Evidence={ECO:0000269|PubMed:12414809}; CC -!- MASS SPECTROMETRY: Mass=3397.2; Mass_error=0.5; CC Method=Electrospray; Range=24-51; Note=Ghrelin-28-C10:1, O- CC decenoylated form.; Evidence={ECO:0000269|PubMed:12414809}; CC -!- MASS SPECTROMETRY: Mass=3371.3; Mass_error=0.1; CC Method=Electrospray; Range=24-51; Note=Ghrelin-28-C8, O- CC octanoylated form.; Evidence={ECO:0000269|PubMed:12414809}; CC -!- MASS SPECTROMETRY: Mass=3243.6; Mass_error=0.4; CC Method=Electrospray; Range=24-50; Note=Ghrelin-27-C10, O- CC decanoylated form.; Evidence={ECO:0000269|PubMed:12414809}; CC -!- MASS SPECTROMETRY: Mass=3214.6; Mass_error=0.6; CC Method=Electrospray; Range=24-50; Note=Ghrelin-27-C8, O- CC octanoylated form.; Evidence={ECO:0000269|PubMed:12414809}; CC -!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/GhrelinID327.html"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66 CC of January 2006; CC URL="http://web.expasy.org/spotlight/back_issues/066"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ghrelin entry; CC URL="https://en.wikipedia.org/wiki/Ghrelin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001134941.2. [Q9UBU3-2] DR RefSeq; NP_001128416.1; NM_001134944.1. [Q9UBU3-3] DR RefSeq; NP_001128417.1; NM_001134945.1. [Q9UBU3-4] DR RefSeq; NP_001128418.1; NM_001134946.1. [Q9UBU3-5] DR RefSeq; NP_001289750.1; NM_001302821.1. [Q9UBU3-1] DR RefSeq; NP_001289751.1; NM_001302822.1. [Q9UBU3-1] DR RefSeq; NP_001289752.1; NM_001302823.1. [Q9UBU3-2] DR RefSeq; NP_001289753.1; NM_001302824.1. [Q9UBU3-1] DR RefSeq; NP_001289754.1; NM_001302825.1. [Q9UBU3-1] DR RefSeq; NP_057446.1; NM_016362.4. [Q9UBU3-1] DR UniGene; Hs.590080; -. DR UniGene; Hs.672979; -. DR PDB; 1P7X; Model; -; A=1-117. DR PDBsum; 1P7X; -. DR ProteinModelPortal; Q9UBU3; -. DR BioGrid; 119706; 5. DR IntAct; Q9UBU3; 1. DR STRING; 9606.ENSP00000335074; -. DR BindingDB; Q9UBU3; -. DR ChEMBL; CHEMBL1921664; -. DR PhosphoSite; Q9UBU3; -. DR BioMuta; GHRL; -. DR DMDM; 17865471; -. DR PaxDb; Q9UBU3; -. DR PRIDE; Q9UBU3; -. DR DNASU; 51738; -. DR Ensembl; ENST00000287656; ENSP00000287656; ENSG00000157017. [Q9UBU3-2] DR Ensembl; ENST00000335542; ENSP00000335074; ENSG00000157017. [Q9UBU3-1] DR Ensembl; ENST00000422159; ENSP00000405464; ENSG00000157017. [Q9UBU3-6] DR Ensembl; ENST00000429122; ENSP00000414819; ENSG00000157017. [Q9UBU3-1] DR Ensembl; ENST00000430179; ENSP00000399922; ENSG00000157017. [Q9UBU3-2] DR Ensembl; ENST00000437422; ENSP00000416768; ENSG00000157017. [Q9UBU3-3] DR Ensembl; ENST00000439975; ENSP00000403725; ENSG00000157017. [Q9UBU3-5] DR Ensembl; ENST00000449238; ENSP00000388145; ENSG00000157017. [Q9UBU3-4] DR Ensembl; ENST00000457360; ENSP00000391406; ENSG00000157017. [Q9UBU3-1] DR GeneID; 51738; -. DR KEGG; hsa:51738; -. DR UCSC; uc003bvj.1; human. DR UCSC; uc010hdc.2; human. [Q9UBU3-5] DR UCSC; uc010hde.2; human. [Q9UBU3-2] DR UCSC; uc010hdf.2; human. [Q9UBU3-1] DR UCSC; uc010hdj.2; human. [Q9UBU3-3] DR UCSC; uc010hdk.2; human. [Q9UBU3-4] DR CTD; 51738; -. DR GeneCards; GHRL; -. DR HGNC; HGNC:18129; GHRL. DR HPA; CAB022731; -. DR HPA; HPA014246; -. DR MalaCards; GHRL; -. DR MIM; 605353; gene. DR neXtProt; NX_Q9UBU3; -. DR PharmGKB; PA142671740; -. DR eggNOG; ENOG410IZYV; Eukaryota. DR eggNOG; ENOG410ZG1B; LUCA. DR GeneTree; ENSGT00390000004064; -. DR HOGENOM; HOG000146466; -. DR HOVERGEN; HBG018522; -. DR InParanoid; Q9UBU3; -. DR KO; K05254; -. DR OMA; EIQFNAP; -. DR OrthoDB; EOG741Z4K; -. DR PhylomeDB; Q9UBU3; -. DR TreeFam; TF336219; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin. DR GeneWiki; Ghrelin; -. DR GenomeRNAi; 51738; -. DR NextBio; 55808; -. DR PMAP-CutDB; Q9UBU3; -. DR PRO; PR:Q9UBU3; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; Q9UBU3; -. DR CleanEx; HS_GHRL; -. DR ExpressionAtlas; Q9UBU3; baseline and differential. DR Genevisible; Q9UBU3; HS. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:GOC. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0001664; F:G-protein coupled receptor binding; ISS: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:0030296; F:protein tyrosine kinase activator activity; IMP:UniProtKB. DR GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB. DR GO; GO:0000187; P:activation of MAPK activity; IMP:UniProtKB. DR GO; GO:0008343; P:adult feeding behavior; ISS:HGNC. DR GO; GO:0051216; P:cartilage development; NAS:UniProtKB. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. 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. DR GO; GO:0009755; P:hormone-mediated signaling pathway; TAS:HGNC. 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:0046676; P:negative regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:UniProtKB. DR GO; GO:0045409; P:negative regulation of interleukin-6 biosynthetic process; IDA:UniProtKB. DR GO; GO:0042536; P:negative regulation of tumor necrosis factor biosynthetic process; IDA:UniProtKB. DR GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC. DR GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IDA:BHF-UCL. 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: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:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IC:HGNC. DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:GOC. DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IDA:UniProtKB. DR GO; GO:0032095; P:regulation of response to food; IBA:GO_Central. 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; PTHR14122; 1. DR Pfam; PF04643; Motilin_assoc; 1. DR Pfam; PF04644; Motilin_ghrelin; 1. DR PRINTS; PR01624; GHRELIN. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Amidation; Complete proteome; KW Direct protein sequencing; Hormone; Lipoprotein; Polymorphism; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000269|PubMed:10930375, FT ECO:0000269|PubMed:15340161}. FT PEPTIDE 24 51 Ghrelin-28. FT /FTId=PRO_0000019202. FT PEPTIDE 24 50 Ghrelin-27. FT /FTId=PRO_0000019203. FT PROPEP 52 75 Removed in mature form. FT /FTId=PRO_0000019204. FT PEPTIDE 76 98 Obestatin. {ECO:0000250}. FT /FTId=PRO_0000045140. FT PROPEP 99 117 Removed in mature form. {ECO:0000250}. FT /FTId=PRO_0000045141. FT MOD_RES 98 98 Leucine amide. {ECO:0000250}. FT LIPID 26 26 O-decanoyl serine; alternate. FT {ECO:0000269|PubMed:10604470, FT ECO:0000269|PubMed:12414809}. FT LIPID 26 26 O-octanoyl serine; alternate. FT {ECO:0000269|PubMed:10604470, FT ECO:0000269|PubMed:12414809}. FT VAR_SEQ 1 75 MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQQRKES FT KKPPAKLQPRALAGWLRPEDGGQAEGAEDELEVR -> MFT FT CWWSYLRSTLAAVPGEASRVQ (in isoform 5). FT {ECO:0000303|PubMed:17727735}. FT /FTId=VSP_041438. FT VAR_SEQ 1 36 MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQ -> M FT FTCWWSYLRSTLAAVPGEASRVQ (in isoform 3 and FT isoform 4). FT {ECO:0000303|PubMed:17727735}. FT /FTId=VSP_041437. FT VAR_SEQ 37 37 Missing (in isoform 2 and isoform 4). FT {ECO:0000303|PubMed:12414809, FT ECO:0000303|PubMed:17727735}. FT /FTId=VSP_003245. FT VAR_SEQ 76 117 FNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPAD FT K -> RPQPTSDRPQALLTSL (in isoform 6). FT {ECO:0000303|Ref.6}. FT /FTId=VSP_047642. FT VARIANT 72 72 L -> M (in dbSNP:rs696217). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_050095. FT VARIANT 90 90 Q -> L (in dbSNP:rs4684677). FT /FTId=VAR_029135. SQ SEQUENCE 117 AA; 12911 MW; 39C0572EBECA2755 CRC64; MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRVQQRKE SKKPPAKLQP RALAGWLRPE DGGQAEGAED ELEVRFNAPF DVGIKLSGVQ YQQHSQALGK FLQDILWEEA KEAPADK //