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Protein

Somatotropin

Gene

GH1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461ZincBy similarity
Metal bindingi199 – 1991ZincBy similarity

GO - Molecular functioni

  • growth hormone receptor binding Source: AgBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell proliferation Source: AgBase
  • cellular response to insulin stimulus Source: Ensembl
  • insulin secretion Source: AgBase
  • negative regulation of apoptotic process Source: AgBase
  • negative regulation of fatty acid biosynthetic process Source: AgBase
  • negative regulation of gene expression Source: AgBase
  • negative regulation of plasminogen activation Source: AgBase
  • negative regulation of protein acetylation Source: AgBase
  • negative regulation of testosterone secretion Source: AgBase
  • negative regulation of urine volume Source: AgBase
  • positive regulation of aldosterone secretion Source: AgBase
  • positive regulation of cholesterol biosynthetic process Source: AgBase
  • positive regulation of cytoplasmic translation Source: AgBase
  • positive regulation of diacylglycerol biosynthetic process Source: AgBase
  • positive regulation of fatty acid biosynthetic process Source: AgBase
  • positive regulation of feeding behavior Source: AgBase
  • positive regulation of gene expression Source: AgBase
  • positive regulation of lactation Source: AgBase
  • positive regulation of lipid catabolic process Source: AgBase
  • positive regulation of MAPK cascade Source: AgBase
  • positive regulation of multicellular organism growth Source: Ensembl
  • positive regulation of peptidyl-threonine phosphorylation Source: AgBase
  • positive regulation of peptidyl-tyrosine phosphorylation Source: AgBase
  • positive regulation of phospholipid biosynthetic process Source: AgBase
  • positive regulation of steroid hormone secretion Source: AgBase
  • positive regulation of TOR signaling Source: AgBase
  • positive regulation of triglyceride biosynthetic process Source: AgBase
  • protein secretion Source: AgBase
  • regulation of intracellular steroid hormone receptor signaling pathway Source: MGI
  • renal sodium ion absorption Source: AgBase
  • response to food Source: AgBase
  • response to L-arginine Source: AgBase
  • response to nutrient levels Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-1170546. Prolactin receptor signaling.
R-BTA-422085. Synthesis, secretion, and deacylation of Ghrelin.
R-BTA-982772. Growth hormone receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Somatotropin
Alternative name(s):
Growth hormone
Gene namesi
Name:GH1
Synonyms:GH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 217191SomatotropinPRO_0000032974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi79 ↔ 1901 Publication
Modified residuei132 – 1321PhosphoserineBy similarity
Disulfide bondi207 ↔ 2151 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP01246.
PRIDEiP01246.

Expressioni

Gene expression databases

ExpressionAtlasiP01246. baseline.

Interactioni

GO - Molecular functioni

  • growth hormone receptor binding Source: AgBase

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022885.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BSTmodel-A27-217[»]
ProteinModelPortaliP01246.
SMRiP01246. Positions 28-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the somatotropin/prolactin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFR6. Eukaryota.
ENOG4111HU8. LUCA.
GeneTreeiENSGT00730000111012.
HOGENOMiHOG000068443.
HOVERGENiHBG011318.
InParanoidiP01246.
KOiK05438.
OMAiTYLRVMK.
OrthoDBiEOG7F7W9X.
TreeFamiTF332592.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERiPTHR11417. PTHR11417. 1 hit.
PfamiPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSiPR00836. SOMATOTROPIN.
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01246-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAAGPRTSL LLAFALLCLP WTQVVGAFPA MSLSGLFANA VLRAQHLHQL
60 70 80 90 100
AADTFKEFER TYIPEGQRYS IQNTQVAFCF SETIPAPTGK NEAQQKSDLE
110 120 130 140 150
LLRISLLLIQ SWLGPLQFLS RVFTNSLVFG TSDRVYEKLK DLEEGILALM
160 170 180 190 200
RELEDGTPRA GQILKQTYDK FDTNMRSDDA LLKNYGLLSC FRKDLHKTET
210
YLRVMKCRRF GEASCAF
Length:217
Mass (Da):24,558
Last modified:July 21, 1986 - v1
Checksum:i99ED8D01B852EF89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951Q → E AA sequence (PubMed:4580883).Curated
Sequence conflicti110 – 12011QSWLGPLQFLS → SQWLQPGFL AA sequence (PubMed:4580883).CuratedAdd
BLAST
Sequence conflicti194 – 1941D → N AA sequence (PubMed:4580883).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531L → V in 30% of the molecules. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00111 mRNA. Translation: CAA23445.1.
J00008 Genomic DNA. Translation: AAA30542.1.
M27325 mRNA. Translation: AAA30543.1.
M57764 Genomic DNA. Translation: AAA30544.1.
M23813 mRNA. Translation: AAA30556.1.
AF034386 mRNA. Translation: AAB92549.1.
DQ184480 mRNA. Translation: ABA26924.1.
EF451795 mRNA. Translation: ABO21739.1.
EF451796 mRNA. Translation: ABO21740.1.
M11558 mRNA. Translation: AAA30545.1.
PIRiI45900. STBO.
RefSeqiNP_851339.1. NM_180996.1.
UniGeneiBt.28019.

Genome annotation databases

EnsembliENSBTAT00000022885; ENSBTAP00000022885; ENSBTAG00000017220.
GeneIDi280804.
KEGGibta:280804.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00111 mRNA. Translation: CAA23445.1.
J00008 Genomic DNA. Translation: AAA30542.1.
M27325 mRNA. Translation: AAA30543.1.
M57764 Genomic DNA. Translation: AAA30544.1.
M23813 mRNA. Translation: AAA30556.1.
AF034386 mRNA. Translation: AAB92549.1.
DQ184480 mRNA. Translation: ABA26924.1.
EF451795 mRNA. Translation: ABO21739.1.
EF451796 mRNA. Translation: ABO21740.1.
M11558 mRNA. Translation: AAA30545.1.
PIRiI45900. STBO.
RefSeqiNP_851339.1. NM_180996.1.
UniGeneiBt.28019.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BSTmodel-A27-217[»]
ProteinModelPortaliP01246.
SMRiP01246. Positions 28-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022885.

Proteomic databases

PaxDbiP01246.
PRIDEiP01246.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022885; ENSBTAP00000022885; ENSBTAG00000017220.
GeneIDi280804.
KEGGibta:280804.

Organism-specific databases

CTDi2688.

Phylogenomic databases

eggNOGiENOG410IFR6. Eukaryota.
ENOG4111HU8. LUCA.
GeneTreeiENSGT00730000111012.
HOGENOMiHOG000068443.
HOVERGENiHBG011318.
InParanoidiP01246.
KOiK05438.
OMAiTYLRVMK.
OrthoDBiEOG7F7W9X.
TreeFamiTF332592.

Enzyme and pathway databases

ReactomeiR-BTA-1170546. Prolactin receptor signaling.
R-BTA-422085. Synthesis, secretion, and deacylation of Ghrelin.
R-BTA-982772. Growth hormone receptor signaling.

Gene expression databases

ExpressionAtlasiP01246. baseline.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERiPTHR11417. PTHR11417. 1 hit.
PfamiPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSiPR00836. SOMATOTROPIN.
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of DNA complementary to bovine growth hormone mRNA."
    Miller W.L., Martial J.A., Baxter J.D.
    J. Biol. Chem. 255:7521-7524(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and nucleotide sequencing of the bovine growth hormone gene."
    Woychik R.P., Camper S.A., Lyons R.H., Horowitz S., Goodwin E.C., Rottman F.M.
    Nucleic Acids Res. 10:7197-7210(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Efficient bacterial expression of bovine and porcine growth hormones."
    Seeburg P.H., Sias S., Adelman J., de Boer H.A., Hayflick J., Jhurani P., Goeddel D.V., Heyneker H.L.
    DNA 2:37-45(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Nucleotide sequence of the bovine growth hormone chromosomal gene."
    Gordon D.F., Quick D.P., Erwin C.R., Donelson J.E., Maurer R.A.
    Mol. Cell. Endocrinol. 33:81-95(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  5. "Genetic engineering of peptide hormones."
    Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S., Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V., Zhvirblis G.S., Skryabin K.G., Baev A.A.
    Mol. Biol. (Mosk.) 19:226-235(1985)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "The complete sequence of a cDNA encoding the bovine growth hormone."
    Mauro S.M.Z., Ferro M.I.T., Macari M., Ferro J.A.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Nelore.
    Tissue: Pituitary.
  7. "Cloning the cDNA of bovine growth hormone gene in E. coli."
    Javadmanesh A., Nassiry M., Eftekhari Shahrudi F., Basami M.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.
  8. "Cloning and sequencing of the growth hormone gene of Pakistani cow breeds (Bos taurus)."
    Mahmood S.F., Awan I.N., Khan M.J., Shahzad M.I., Khanum A.
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Shiwal and Tharri malir.
    Tissue: Pituitary.
  9. "The primary structure of bovine growth hormone."
    Wallis M.
    FEBS Lett. 35:11-14(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-217, VARIANT VAL-153.
  10. Cited for: PROTEIN SEQUENCE OF 27-217.
  11. "High-level expression in Escherichia coli of biologically active bovine growth hormone."
    George H.J., L'Italien J.J., Pilacinski W.P., Glassman D.L., Krzyzek R.A.
    DNA 4:273-281(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-49.
  12. "On the primary structure of pituitary bovine growth hormone."
    Graf L., Li C.H.
    Biochem. Biophys. Res. Commun. 56:168-176(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 91-96 AND 104-121.
  13. Cited for: EVIDENCE FOR TWO ALLELIC CHAINS.
  14. "Studies on the common active site of growth hormone. Revision of the amino acid sequence of an active fragment of bovine growth hormone."
    Yamasaki N., Shimanaka J., Sonenburg M.
    J. Biol. Chem. 250:2510-2514(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  15. "A heuristic approach to predicting the tertiary structure of bovine somatotropin."
    Carlacci L., Chou K.-C., Maggiora G.M.
    Biochemistry 30:4389-4398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiSOMA_BOVIN
AccessioniPrimary (citable) accession number: P01246
Secondary accession number(s): A4GX96, Q28117, Q3LS73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 132 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.