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Q9EQX0

- GHRL_MOUSE

UniProt

Q9EQX0 - GHRL_MOUSE

Protein

Appetite-regulating hormone

Gene

Ghrl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
    Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility By similarity.By similarity

    GO - Molecular functioni

    1. ghrelin receptor binding Source: UniProtKB
    2. growth hormone-releasing hormone activity Source: UniProtKB
    3. hormone activity Source: UniProtKB
    4. protein tyrosine kinase activator activity Source: UniProtKB

    GO - Biological processi

    1. actin polymerization or depolymerization Source: UniProtKB
    2. activation of MAPK activity Source: UniProtKB
    3. adult feeding behavior Source: HGNC
    4. decidualization Source: UniProtKB
    5. dendrite development Source: UniProtKB
    6. gastric acid secretion Source: Ensembl
    7. G-protein coupled receptor signaling pathway Source: Ensembl
    8. negative regulation of apoptotic process Source: UniProtKB
    9. negative regulation of circadian sleep/wake cycle, REM sleep Source: Ensembl
    10. negative regulation of endothelial cell proliferation Source: UniProtKB
    11. negative regulation of inflammatory response Source: UniProtKB
    12. negative regulation of insulin secretion Source: UniProtKB
    13. negative regulation of interleukin-1 beta production Source: UniProtKB
    14. negative regulation of interleukin-6 biosynthetic process Source: UniProtKB
    15. negative regulation of locomotion Source: MGI
    16. negative regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
    17. positive regulation of appetite Source: HGNC
    18. positive regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
    19. positive regulation of corticotropin secretion Source: Ensembl
    20. positive regulation of cortisol secretion Source: Ensembl
    21. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    22. positive regulation of growth hormone secretion Source: Ensembl
    23. positive regulation of insulin secretion Source: UniProtKB
    24. positive regulation of response to food Source: UniProtKB
    25. positive regulation of synapse assembly Source: UniProtKB
    26. regulation of cell proliferation Source: UniProtKB
    27. regulation of excitatory postsynaptic membrane potential Source: MGI
    28. regulation of response to food Source: UniProtKB
    29. response to estrogen Source: UniProtKB
    30. response to hormone Source: UniProtKB

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_207651. G alpha (q) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Appetite-regulating hormone
    Alternative name(s):
    Growth hormone secretagogue
    Growth hormone-releasing peptide
    Motilin-related peptide
    Protein M46
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Ghrl
    Synonyms:Mtlrp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1930008. Ghrl.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cytoplasm Source: MGI
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Peptidei24 – 5128GhrelinPRO_0000019205Add
    BLAST
    Propeptidei52 – 7524Removed in mature formBy similarityPRO_0000019206Add
    BLAST
    Peptidei76 – 9823ObestatinPRO_0000045142Add
    BLAST
    Propeptidei99 – 11719Removed in mature formBy similarityPRO_0000045143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi26 – 261O-decanoyl serine; alternate1 Publication
    Lipidationi26 – 261O-octanoyl serine; alternate1 Publication
    Modified residuei98 – 981Leucine amide1 Publication

    Post-translational modificationi

    O-octanoylation or O-decanoylation is essential for ghrelin activity By similarity. The O-decanoylated form ghrelin-C10 differs in the length of the carbon backbone of the carboxylic acid bound to Ser-26 (PubMed:15746259).By similarity1 Publication
    Amidation of Leu-98 is essential for obestatin activity.By similarity

    Keywords - PTMi

    Amidation, Lipoprotein

    Proteomic databases

    MaxQBiQ9EQX0.
    PaxDbiQ9EQX0.
    PRIDEiQ9EQX0.

    PTM databases

    PhosphoSiteiQ9EQX0.

    Expressioni

    Tissue specificityi

    Mainly expressed in the gastrointestinal tract with higher levels in the stomach, medium levels in the duodenum, jejunum, ileum and colon. Low expression in the testis and brain. Not detected in the salivary gland, pancreas, liver and lung.1 Publication

    Developmental stagei

    Levels of n-octanoylated and n-decanoylated ghrelin drop by one third and 3-fold, respectively, between postnatal weeks 3 and 4 due to change of diet during weaning.1 Publication

    Gene expression databases

    BgeeiQ9EQX0.
    CleanExiMM_GHRL.
    GenevestigatoriQ9EQX0.

    Structurei

    Secondary structure

    1
    117
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi84 – 863
    Helixi87 – 904
    Beta strandi94 – 963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JSHNMR-A76-98[»]
    2JSINMR-A86-98[»]
    2JSJNMR-A76-98[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9EQX0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the motilin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG45924.
    GeneTreeiENSGT00390000004064.
    HOGENOMiHOG000236303.
    HOVERGENiHBG018522.
    InParanoidiQ9EQX0.
    KOiK05254.
    OMAiSLGTICS.
    OrthoDBiEOG741Z4K.
    PhylomeDBiQ9EQX0.
    TreeFamiTF336219.

    Family and domain databases

    InterProiIPR006737. Motilin_assoc.
    IPR006738. Motilin_ghrelin.
    IPR005441. Preproghrelin.
    [Graphical view]
    PANTHERiPTHR14122. PTHR14122. 1 hit.
    PfamiPF04643. Motilin_assoc. 1 hit.
    PF04644. Motilin_ghrelin. 1 hit.
    [Graphical view]
    PRINTSiPR01624. GHRELIN.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9EQX0-1) [UniParc]FASTAAdd to Basket

    Also known as: Ghrelin

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLSSGTICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP    50
    RALEGWLHPE DRGQAEETEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK 100
    FLQDILWEEV KEAPADK 117
    Length:117
    Mass (Da):13,207
    Last modified:March 1, 2001 - v1
    Checksum:iEACB49D2E3CA7203
    GO
    Isoform 2 (identifier: Q9EQX0-2) [UniParc]FASTAAdd to Basket

    Also known as: des-Gln14-ghrelin

    The sequence of this isoform differs from the canonical sequence as follows:
         37-37: Missing.

    Show »
    Length:116
    Mass (Da):13,079
    Checksum:iE00DA3D67998B6B8
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei37 – 371Missing in isoform 2. 1 PublicationVSP_003246

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ243503 mRNA. Translation: CAB46500.1.
    AB035701 mRNA. Translation: BAB19046.1.
    AB060078 Genomic DNA. Translation: BAB69857.1.
    AK008658 mRNA. Translation: BAB25814.1.
    AK008860 mRNA. Translation: BAB25934.1.
    CCDSiCCDS20432.1. [Q9EQX0-1]
    RefSeqiNP_001273333.1. NM_001286404.1. [Q9EQX0-2]
    NP_001273334.1. NM_001286405.1.
    NP_001273335.1. NM_001286406.1.
    NP_067463.2. NM_021488.5. [Q9EQX0-1]
    XP_006506509.1. XM_006506446.1. [Q9EQX0-1]
    UniGeneiMm.379095.

    Genome annotation databases

    EnsembliENSMUST00000064993; ENSMUSP00000069567; ENSMUSG00000064177. [Q9EQX0-1]
    GeneIDi58991.
    KEGGimmu:58991.
    UCSCiuc009dhj.1. mouse. [Q9EQX0-2]
    uc009dhl.1. mouse. [Q9EQX0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Gut feelings - Issue 66 of January 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ243503 mRNA. Translation: CAB46500.1 .
    AB035701 mRNA. Translation: BAB19046.1 .
    AB060078 Genomic DNA. Translation: BAB69857.1 .
    AK008658 mRNA. Translation: BAB25814.1 .
    AK008860 mRNA. Translation: BAB25934.1 .
    CCDSi CCDS20432.1. [Q9EQX0-1 ]
    RefSeqi NP_001273333.1. NM_001286404.1. [Q9EQX0-2 ]
    NP_001273334.1. NM_001286405.1.
    NP_001273335.1. NM_001286406.1.
    NP_067463.2. NM_021488.5. [Q9EQX0-1 ]
    XP_006506509.1. XM_006506446.1. [Q9EQX0-1 ]
    UniGenei Mm.379095.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JSH NMR - A 76-98 [» ]
    2JSI NMR - A 86-98 [» ]
    2JSJ NMR - A 76-98 [» ]
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9EQX0.

    Proteomic databases

    MaxQBi Q9EQX0.
    PaxDbi Q9EQX0.
    PRIDEi Q9EQX0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064993 ; ENSMUSP00000069567 ; ENSMUSG00000064177 . [Q9EQX0-1 ]
    GeneIDi 58991.
    KEGGi mmu:58991.
    UCSCi uc009dhj.1. mouse. [Q9EQX0-2 ]
    uc009dhl.1. mouse. [Q9EQX0-1 ]

    Organism-specific databases

    CTDi 51738.
    MGIi MGI:1930008. Ghrl.

    Phylogenomic databases

    eggNOGi NOG45924.
    GeneTreei ENSGT00390000004064.
    HOGENOMi HOG000236303.
    HOVERGENi HBG018522.
    InParanoidi Q9EQX0.
    KOi K05254.
    OMAi SLGTICS.
    OrthoDBi EOG741Z4K.
    PhylomeDBi Q9EQX0.
    TreeFami TF336219.

    Enzyme and pathway databases

    Reactomei REACT_207651. G alpha (q) signalling events.

    Miscellaneous databases

    ChiTaRSi GHRL. mouse.
    EvolutionaryTracei Q9EQX0.
    NextBioi 314490.
    PROi Q9EQX0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EQX0.
    CleanExi MM_GHRL.
    Genevestigatori Q9EQX0.

    Family and domain databases

    InterProi IPR006737. Motilin_assoc.
    IPR006738. Motilin_ghrelin.
    IPR005441. Preproghrelin.
    [Graphical view ]
    PANTHERi PTHR14122. PTHR14122. 1 hit.
    Pfami PF04643. Motilin_assoc. 1 hit.
    PF04644. Motilin_ghrelin. 1 hit.
    [Graphical view ]
    PRINTSi PR01624. GHRELIN.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel gastric peptide hormone: the motilin-related peptide."
      Tomasetto C., Karam S.M., Ribieras S., Masson R., Lefebvre O., Staub A., Alexander G., Chenard M.-P., Rio M.-C.
      Gastroenterology 119:395-405(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 24-30, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Stomach.
    2. "Mouse mRNA for preproghrelin."
      Kojima M.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Tanaka M., Hayashida Y., Iguchi T., Nakao N., Nakai N., Nakashima K.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Stomach.
    5. "Developmental changes in the pattern of ghrelin's acyl modification and the levels of acyl-modified ghrelins in murine stomach."
      Nishi Y., Hiejima H., Mifune H., Sato T., Kangawa K., Kojima M.
      Endocrinology 146:2709-2715(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, ACYLATION AT SER-26.
    6. "Ghrelin: discovery of the natural endogenous ligand for the growth hormone secretagogue receptor."
      Kojima M., Hosoda H., Matsuo H., Kangawa K.
      Trends Endocrinol. Metab. 12:118-122(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. "Obestatin conformational features: a strategy to unveil obestatin's biological role ?"
      Scrima M., Campiglia P., Esposito C., Gomez-Monterrey I., Novellino E., D'Ursi A.M.
      Biochem. Biophys. Res. Commun. 363:500-505(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 76-98, AMIDATION AT LEU-98.

    Entry informationi

    Entry nameiGHRL_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQX0
    Secondary accession number(s): Q9WUZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3