Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pro-thyrotropin-releasing hormone

Gene

Trh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems.

GO - Molecular functioni

  • thyrotropin-releasing hormone activity Source: RGD

GO - Biological processi

  • adult walking behavior Source: Ensembl
  • eating behavior Source: RGD
  • histamine metabolic process Source: RGD
  • hormone-mediated signaling pathway Source: InterPro
  • negative regulation of feeding behavior Source: RGD
  • negative regulation of glutamate secretion Source: RGD
  • positive regulation of gamma-aminobutyric acid secretion Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • response to cold Source: RGD
  • response to corticosterone Source: RGD
  • response to ethanol Source: RGD
  • response to glucose Source: RGD
  • response to hypoxia Source: RGD
  • response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiR-RNO-375276. Peptide ligand-binding receptors.
R-RNO-416476. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-thyrotropin-releasing hormone
Short name:
Pro-TRH
Alternative name(s):
Prothyroliberin
Cleaved into the following chain:
Alternative name(s):
Protirelin
TSH-releasing factor
Thyroliberin
Thyrotropin-releasing factor
Short name:
TRF
Gene namesi
Name:Trh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi3903. Trh.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular region Source: UniProtKB-SubCell
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 255231Pro-thyrotropin-releasing hormonePRO_0000022522Add
BLAST
Peptidei77 – 793Thyrotropin-releasing hormonePRO_0000022523
Peptidei109 – 1113Thyrotropin-releasing hormonePRO_0000022524
Peptidei154 – 1563Thyrotropin-releasing hormonePRO_0000022525
Peptidei172 – 1743Thyrotropin-releasing hormonePRO_0000022526
Peptidei202 – 2043Thyrotropin-releasing hormonePRO_0000022527

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791Proline amideBy similarity
Modified residuei111 – 1111Proline amideBy similarity
Modified residuei154 – 1541Pyrrolidone carboxylic acid1 Publication
Modified residuei156 – 1561Proline amideBy similarity
Modified residuei172 – 1721Pyrrolidone carboxylic acid1 Publication
Modified residuei174 – 1741Proline amideBy similarity
Modified residuei204 – 2041Proline amideBy similarity

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP01150.
PRIDEiP01150.

Miscellaneous databases

PMAP-CutDBP01150.

Expressioni

Gene expression databases

ExpressionAtlasiP01150. baseline and differential.
GenevisibleiP01150. RN.

Interactioni

GO - Molecular functioni

  • thyrotropin-releasing hormone activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015944.

Chemistry

BindingDBiP01150.

Family & Domainsi

Sequence similaritiesi

Belongs to the TRH family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IXZK. Eukaryota.
ENOG4111JXZ. LUCA.
GeneTreeiENSGT00390000016951.
HOGENOMiHOG000054194.
HOVERGENiHBG083494.
InParanoidiP01150.
KOiK05253.
OMAiGRRANQD.
OrthoDBiEOG70PBZR.
PhylomeDBiP01150.
TreeFamiTF332073.

Family and domain databases

InterProiIPR008857. TRH.
[Graphical view]
PANTHERiPTHR17530. PTHR17530. 1 hit.
PfamiPF05438. TRH. 1 hit.
[Graphical view]
PIRSFiPIRSF001795. TRH. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P01150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGPWLLLAL ALIFTLTGIP ESCALPEAAQ EEGAVTPDLP GLENVQVRPE
60 70 80 90 100
RRFLWKDLQR VRGDLGAALD SWITKRQHPG KREEEEKDIE AEERGDLGEG
110 120 130 140 150
GAWRLHKRQH PGRRANQDKY SWADEEDSDW MPRSWLPDFF LDSWFSDVPQ
160 170 180 190 200
VKRQHPGRRS FPWMESDVTK RQHPGRRFID PELQRSWEEK EGEGVLMPEK
210 220 230 240 250
RQHPGKRALG HPCGPQGTCG QTGLLQLLGD LSRGQETLVK QSPQVEPWDK

EPLEE
Length:255
Mass (Da):29,284
Last modified:July 21, 1986 - v1
Checksum:i440DCCEADC0A22EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12138 mRNA. Translation: AAA42275.1.
M23632, M23643 Genomic DNA. Translation: AAA65750.2.
M27465, M27464 Genomic DNA. Translation: AAA42239.1.
M36317 mRNA. Translation: AAA42276.1.
PIRiA31773. RHRTT.
RefSeqiNP_037178.1. NM_013046.3.
XP_006236961.1. XM_006236899.2.
UniGeneiRn.22.

Genome annotation databases

EnsembliENSRNOT00000015944; ENSRNOP00000015944; ENSRNOG00000011824.
GeneIDi25569.
KEGGirno:25569.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12138 mRNA. Translation: AAA42275.1.
M23632, M23643 Genomic DNA. Translation: AAA65750.2.
M27465, M27464 Genomic DNA. Translation: AAA42239.1.
M36317 mRNA. Translation: AAA42276.1.
PIRiA31773. RHRTT.
RefSeqiNP_037178.1. NM_013046.3.
XP_006236961.1. XM_006236899.2.
UniGeneiRn.22.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015944.

Chemistry

BindingDBiP01150.

Proteomic databases

PaxDbiP01150.
PRIDEiP01150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015944; ENSRNOP00000015944; ENSRNOG00000011824.
GeneIDi25569.
KEGGirno:25569.

Organism-specific databases

CTDi7200.
RGDi3903. Trh.

Phylogenomic databases

eggNOGiENOG410IXZK. Eukaryota.
ENOG4111JXZ. LUCA.
GeneTreeiENSGT00390000016951.
HOGENOMiHOG000054194.
HOVERGENiHBG083494.
InParanoidiP01150.
KOiK05253.
OMAiGRRANQD.
OrthoDBiEOG70PBZR.
PhylomeDBiP01150.
TreeFamiTF332073.

Enzyme and pathway databases

ReactomeiR-RNO-375276. Peptide ligand-binding receptors.
R-RNO-416476. G alpha (q) signalling events.

Miscellaneous databases

NextBioi607181.
PMAP-CutDBP01150.
PROiP01150.

Gene expression databases

ExpressionAtlasiP01150. baseline and differential.
GenevisibleiP01150. RN.

Family and domain databases

InterProiIPR008857. TRH.
[Graphical view]
PANTHERiPTHR17530. PTHR17530. 1 hit.
PfamiPF05438. TRH. 1 hit.
[Graphical view]
PIRSFiPIRSF001795. TRH. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Thyrotropin-releasing hormone precursor: characterization in rat brain."
    Lechan R.M., Wu P., Jackson I.M.D., Wolf H., Cooperman S., Mandel G., Goodman R.H.
    Science 231:159-161(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the gene encoding rat thyrotropin releasing hormone."
    Lee S.L., Stewart K., Goodman R.H.
    J. Biol. Chem. 263:16604-16609(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterization and expression of the gene-encoding rat thyrotropin-releasing hormone (TRH)."
    Lee S.L., Sevarino K., Roos B.A., Goodman R.H.
    Ann. N. Y. Acad. Sci. 553:14-28(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Using the brain to screen cloned genes."
    Mandel G., Goodman R.H.
    Trends Neurosci. 10:101-104(1987)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Processing of thyrotropin-releasing hormone (TRH) prohormone in the rat olfactory bulb generates novel TRH-related peptides."
    Bulant M., Beauvillain J.-C., Delfour A., Vaudry H., Nicolas P.
    Endocrinology 127:1978-1985(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, PYROGLUTAMATE FORMATION AT GLN-154 AND GLN-172.

Entry informationi

Entry nameiTRH_RAT
AccessioniPrimary (citable) accession number: P01150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 120 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

Complete proteome, Reference proteome

Documents

  1. 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.