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Corticotropin-releasing factor receptor 1 (CRF-R-1) (CRF-R1) (CRFR-1) (Corticotropin-releasing hormone receptor 1) (CRH-R-1) (CRH-R1)

 CRFR1_RAT               Reviewed;         415 AA.
P35353;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
30-AUG-2017, entry version 141.
RecName: Full=Corticotropin-releasing factor receptor 1;
Short=CRF-R-1;
Short=CRF-R1;
Short=CRFR-1;
AltName: Full=Corticotropin-releasing hormone receptor 1;
Short=CRH-R-1;
Short=CRH-R1;
Flags: Precursor;
Name=Crhr1; Synonyms=Crhr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=8243338; DOI=10.1210/endo.133.6.8243338;
Perrin M.H., Donaldson C.J., Chen R., Lewis K.A., Vale W.W.;
"Cloning and functional expression of a rat brain corticotropin
releasing factor (CRF) receptor.";
Endocrinology 133:3058-3061(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
PubMed=8274282; DOI=10.1016/0896-6273(93)90230-O;
Chang C.P., Pearse R.V. II, O'Connell S., Rosenfeld M.G.;
"Identification of a seven transmembrane helix receptor for
corticotropin-releasing factor and sauvagine in mammalian brain.";
Neuron 11:1187-1195(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Testis;
PubMed=8662941; DOI=10.1074/jbc.271.24.14519;
Tsai-Morris C.-H., Buczko E., Geng Y., Gamboa-Pinto A., Dufau M.L.;
"The genomic structure of the rat corticotropin releasing factor
receptor. A member of the class II G protein-coupled receptors.";
J. Biol. Chem. 271:14519-14525(1996).
[4]
FUNCTION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-38; ASN-45;
ASN-78; ASN-90 AND ASN-98.
PubMed=11567096; DOI=10.1110/ps.12101;
Hofmann B.A., Sydow S., Jahn O., van Werven L., Liepold T., Eckart K.,
Spiess J.;
"Functional and protein chemical characterization of the N-terminal
domain of the rat corticotropin-releasing factor receptor 1.";
Protein Sci. 10:2050-2062(2001).
[5]
SUBUNIT.
PubMed=23300088; DOI=10.1074/jbc.M112.412478;
Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.;
"Post-synaptic density-95 (PSD-95) binding capacity of G-protein-
coupled receptor 30 (GPR30), an estrogen receptor that can be
identified in hippocampal dendritic spines.";
J. Biol. Chem. 288:6438-6450(2013).
-!- FUNCTION: G-protein coupled receptor for CRH (corticotropin-
releasing factor) and UCN (urocortin). Has high affinity for CRH
and UCN. Ligand binding causes a conformation change that triggers
signaling via guanine nucleotide-binding proteins (G proteins) and
down-stream effectors, such as adenylate cyclase. Promotes the
activation of adenylate cyclase, leading to increased
intracellular cAMP levels. Inhibits the activity of the calcium
channel CACNA1H. Required for normal embryonic development of the
adrenal gland and for normal hormonal responses to stress. Plays a
role in the response to anxiogenic stimuli.
{ECO:0000269|PubMed:11567096, ECO:0000269|PubMed:8243338,
ECO:0000269|PubMed:8274282}.
-!- SUBUNIT: Interacts (via N-terminal extracellular domain) with CRH
and UCN. Interacts with DLG1; this inhibits endocytosis of CRHR1
after agonist binding (By similarity). Heterodimer;
heterodimerizes with GPER1. {ECO:0000250,
ECO:0000269|PubMed:23300088}.
-!- INTERACTION:
P55090:Ucn; NbExp=3; IntAct=EBI-9030306, EBI-9030248;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endosome {ECO:0000250}. Note=Agonist-binding promotes endocytosis.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in brain, especially in cerebellum.
Detected in pituitary gland, and at lower levels in the olfactory
bulb. {ECO:0000269|PubMed:8274282}.
-!- DOMAIN: The transmembrane domain is composed of seven
transmembrane helices that are arranged in V-shape. Transmembrane
helix 7 assumes a sharply kinked structure (By similarity).
{ECO:0000250}.
-!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
-!- PTM: Phosphorylation at Ser-301 by PKA prevents maximal coupling
to Gq-protein, and thereby negatively regulates downstream
signaling. {ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L24096; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L25438; AAA16441.1; -; mRNA.
EMBL; U53498; AAC53519.1; -; Genomic_DNA.
EMBL; U53486; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53487; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53488; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53489; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53490; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53491; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53492; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53493; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53494; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53495; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53496; AAC53519.1; JOINED; Genomic_DNA.
EMBL; U53497; AAC53519.1; JOINED; Genomic_DNA.
PIR; I58144; I58144.
RefSeq; NP_112261.1; NM_030999.4.
UniGene; Rn.10499; -.
ProteinModelPortal; P35353; -.
SMR; P35353; -.
BioGrid; 248692; 4.
IntAct; P35353; 1.
STRING; 10116.ENSRNOP00000006764; -.
BindingDB; P35353; -.
ChEMBL; CHEMBL4649; -.
GuidetoPHARMACOLOGY; 212; -.
iPTMnet; P35353; -.
PhosphoSitePlus; P35353; -.
PaxDb; P35353; -.
Ensembl; ENSRNOT00000006764; ENSRNOP00000006764; ENSRNOG00000004900.
GeneID; 58959; -.
KEGG; rno:58959; -.
CTD; 1394; -.
RGD; 61276; Crhr1.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000230719; -.
HOVERGEN; HBG106921; -.
InParanoid; P35353; -.
KO; K04578; -.
OMA; FICIGWC; -.
OrthoDB; EOG091G0BBY; -.
PhylomeDB; P35353; -.
TreeFam; TF315710; -.
Reactome; R-RNO-373080; Class B/2 (Secretin family receptors).
Reactome; R-RNO-418555; G alpha (s) signalling events.
PRO; PR:P35353; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000004900; -.
ExpressionAtlas; P35353; baseline and differential.
Genevisible; P35353; RN.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005771; C:multivesicular body; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; ISS:UniProtKB.
GO; GO:0051424; F:corticotropin-releasing hormone binding; IDA:RGD.
GO; GO:0043404; F:corticotropin-releasing hormone receptor activity; IDA:RGD.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
GO; GO:0004930; F:G-protein coupled receptor activity; IDA:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
GO; GO:0048266; P:behavioral response to pain; IMP:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
GO; GO:0051458; P:corticotropin secretion; ISS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IMP:RGD.
GO; GO:0042596; P:fear response; IEA:Ensembl.
GO; GO:0007631; P:feeding behavior; IMP:RGD.
GO; GO:0051867; P:general adaptation syndrome, behavioral process; IEA:Ensembl.
GO; GO:0021854; P:hypothalamus development; IEP:RGD.
GO; GO:0035641; P:locomotory exploration behavior; IMP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0032811; P:negative regulation of epinephrine secretion; IMP:RGD.
GO; GO:2000252; P:negative regulation of feeding behavior; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:RGD.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0010579; P:positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
GO; GO:2000852; P:regulation of corticosterone secretion; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IMP:RGD.
GO; GO:0001666; P:response to hypoxia; IMP:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0008542; P:visual learning; IMP:RGD.
CDD; cd15445; 7tmB1_CRF-R1; 1.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR003052; GPCR_2_CRF1_rcpt.
InterPro; IPR003051; GPCR_2_CRF_rcpt.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR01279; CRFRECEPTOR.
PRINTS; PR01280; CRFRECEPTOR1.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00008; HormR; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 23
CHAIN 24 415 Corticotropin-releasing factor receptor
1.
/FTId=PRO_0000012816.
TOPO_DOM 24 111 Extracellular. {ECO:0000250}.
TRANSMEM 112 142 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 143 149 Cytoplasmic. {ECO:0000250}.
TRANSMEM 150 174 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 175 189 Extracellular. {ECO:0000250}.
TRANSMEM 190 218 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 219 225 Cytoplasmic. {ECO:0000250}.
TRANSMEM 226 253 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 254 269 Extracellular. {ECO:0000250}.
TRANSMEM 270 295 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 296 306 Cytoplasmic. {ECO:0000250}.
TRANSMEM 307 331 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 332 338 Extracellular. {ECO:0000250}.
TRANSMEM 339 368 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 369 415 Cytoplasmic. {ECO:0000250}.
REGION 99 108 Important for peptide agonist binding.
{ECO:0000250}.
REGION 280 290 Important for antagonist binding.
{ECO:0000250}.
MOD_RES 301 301 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P34998}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11567096}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11567096}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11567096}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11567096}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11567096}.
DISULFID 30 54 {ECO:0000269|PubMed:11567096}.
DISULFID 44 87 {ECO:0000269|PubMed:11567096}.
DISULFID 68 102 {ECO:0000269|PubMed:11567096}.
DISULFID 188 258 {ECO:0000250}.
SEQUENCE 415 AA; 47842 MW; 48D6704B31D4C013 CRC64;
MGRRPQLRLV KALLLLGLNP VSTSLQDQRC ENLSLTSNVS GLQCNASVDL IGTCWPRSPA
GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS ECQEILNEEK KSKVHYHVAV
IINYLGHCIS LVALLVAFVL FLRLRSIRCL RNIIHWNLIS AFILRNATWF VVQLTVSPEV
HQSNVAWCRL VTAAYNYFHV TNFFWMFGEG CYLHTAIVLT YSTDRLRKWM FVCIGWGVPF
PIIVAWAIGK LHYDNEKCWF GKRPGVYTDY IYQGPMILVL LINFIFLFNI VRILMTKLRA
STTSETIQYR KAVKATLVLL PLLGITYMLF FVNPGEDEVS RVVFIYFNSF LESFQGFFVS
VFYCFLNSEV RSAIRKRWRR WQDKHSIRAR VARAMSIPTS PTRVSFHSIK QSTAV


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