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Protein

Corticotropin-releasing factor receptor 1

Gene

CRHR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. corticotrophin-releasing factor receptor activity Source: UniProtKB
  2. corticotropin-releasing hormone binding Source: Ensembl
  3. corticotropin-releasing hormone receptor activity Source: Ensembl

GO - Biological processi

  1. activation of adenylate cyclase activity Source: ProtInc
  2. adrenal gland development Source: Ensembl
  3. behavioral response to cocaine Source: Ensembl
  4. behavioral response to ethanol Source: Ensembl
  5. behavioral response to pain Source: Ensembl
  6. cellular response to corticotropin-releasing hormone stimulus Source: UniProtKB
  7. corticotropin secretion Source: UniProtKB
  8. epithelial cell differentiation Source: Ensembl
  9. fear response Source: Ensembl
  10. female pregnancy Source: ProtInc
  11. general adaptation syndrome, behavioral process Source: Ensembl
  12. hypothalamus development Source: Ensembl
  13. immune response Source: ProtInc
  14. locomotory exploration behavior Source: Ensembl
  15. long-term synaptic potentiation Source: Ensembl
  16. memory Source: Ensembl
  17. negative regulation of epinephrine secretion Source: Ensembl
  18. negative regulation of feeding behavior Source: Ensembl
  19. negative regulation of neuron death Source: Ensembl
  20. negative regulation of voltage-gated calcium channel activity Source: UniProtKB
  21. neuropeptide signaling pathway Source: Ensembl
  22. parturition Source: ProtInc
  23. phospholipase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
  24. positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: UniProtKB
  25. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  26. positive regulation of mast cell degranulation Source: Ensembl
  27. regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: UniProtKB
  28. regulation of corticosterone secretion Source: UniProtKB
  29. response to electrical stimulus Source: Ensembl
  30. response to hypoxia Source: Ensembl
  31. response to immobilization stress Source: Ensembl
  32. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_18372. Class B/2 (Secretin family receptors).
REACT_19327. G alpha (s) signalling events.

Protein family/group databases

TCDBi9.A.14.4.3. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Corticotropin-releasing factor receptor 1
Short name:
CRF-R-1
Short name:
CRF-R1
Short name:
CRFR-1
Alternative name(s):
Corticotropin-releasing hormone receptor 1
Short name:
CRH-R-1
Short name:
CRH-R1
Gene namesi
Name:CRHR1
Synonyms:CRFR, CRFR1, CRHR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:2357. CRHR1.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Endosome
Note: Agonist-binding promotes endocytosis.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 11188ExtracellularAdd
BLAST
Transmembranei112 – 14231Helical; Name=1Add
BLAST
Topological domaini143 – 17836CytoplasmicAdd
BLAST
Transmembranei179 – 20325Helical; Name=2Add
BLAST
Topological domaini204 – 21815ExtracellularAdd
BLAST
Transmembranei219 – 24729Helical; Name=3Add
BLAST
Topological domaini248 – 2547Cytoplasmic
Transmembranei255 – 28228Helical; Name=4Add
BLAST
Topological domaini283 – 29816ExtracellularAdd
BLAST
Transmembranei299 – 32426Helical; Name=5Add
BLAST
Topological domaini325 – 33511CytoplasmicAdd
BLAST
Transmembranei336 – 36025Helical; Name=6Add
BLAST
Topological domaini361 – 3677Extracellular
Transmembranei368 – 39730Helical; Name=7Add
BLAST
Topological domaini398 – 44447CytoplasmicAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. dendrite Source: Ensembl
  3. integral component of membrane Source: UniProtKB
  4. integral component of plasma membrane Source: ProtInc
  5. intrinsic component of plasma membrane Source: UniProtKB
  6. multivesicular body Source: Ensembl
  7. neuronal cell body Source: Ensembl
  8. plasma membrane Source: Reactome
  9. trans-Golgi network Source: Ensembl
  10. vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2321F → A: Nearly abolishes antagonist binding. 1 Publication
Mutagenesisi235 – 2351M → A: Strongly reduces antagonist binding. 1 Publication
Mutagenesisi309 – 3091L → A: Nearly abolishes antagonist binding. 1 Publication
Mutagenesisi312 – 3121N → A: Nearly abolishes antagonist binding. 1 Publication
Mutagenesisi313 – 3131F → A: Slightly reduces antagonist binding. 1 Publication
Mutagenesisi316 – 3161L → A: Strongly reduces antagonist binding. 1 Publication
Mutagenesisi319 – 3191I → A: Strongly reduces antagonist binding. 1 Publication
Mutagenesisi356 – 3561Y → A: Strongly reduces antagonist binding. 1 Publication
Mutagenesisi384 – 3841Q → A: Increases antagonist binding. 1 Publication

Organism-specific databases

PharmGKBiPA26874.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 444421Corticotropin-releasing factor receptor 1PRO_0000012814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 54
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi44 ↔ 87
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi68 ↔ 102
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi217 ↔ 287
Modified residuei330 – 3301Phosphoserine; by PKA1 Publication

Post-translational modificationi

C-terminal Ser or Thr residues may be phosphorylated.1 Publication
Phosphorylation at Ser-330 by PKA prevents maximal coupling to Gq-protein, and thereby negatively regulates downstream signaling.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP34998.
PRIDEiP34998.

PTM databases

PhosphoSiteiP34998.

Expressioni

Tissue specificityi

Predominantly expressed in the cerebellum, pituitary, cerebral cortex and olfactory lobe.1 Publication

Gene expression databases

BgeeiP34998.
CleanExiHS_CRHR1.
ExpressionAtlasiP34998. baseline.
GenevestigatoriP34998.

Interactioni

Subunit structurei

Heterodimer; heterodimerizes with GPER1 (By similarity). Interacts (via N-terminal extracellular domain) with CRH and UCN. Interacts with DLG1; this inhibits endocytosis of CRHR1 after agonist binding.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRHP068502EBI-3870393,EBI-3870390

Protein-protein interaction databases

BioGridi107784. 8 interactions.
IntActiP34998. 2 interactions.
MINTiMINT-1217325.
STRINGi9606.ENSP00000381333.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273Combined sources
Helixi28 – 325Combined sources
Beta strandi49 – 524Combined sources
Beta strandi62 – 676Combined sources
Beta strandi70 – 745Combined sources
Beta strandi81 – 877Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 986Combined sources
Helixi99 – 1013Combined sources
Helixi103 – 1075Combined sources
Helixi116 – 14328Combined sources
Helixi175 – 1773Combined sources
Helixi179 – 20527Combined sources
Helixi207 – 2126Combined sources
Helixi215 – 23521Combined sources
Helixi238 – 25316Combined sources
Helixi257 – 2593Combined sources
Helixi270 – 29627Combined sources
Helixi304 – 33128Combined sources
Helixi339 – 36729Combined sources
Helixi375 – 39622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L27NMR-A25-108[»]
3EHSX-ray2.76A24-119[»]
3EHTX-ray3.40A24-119[»]
3EHUX-ray1.96A/B24-119[»]
4K5YX-ray2.98A/B/C104-373[»]
ProteinModelPortaliP34998.
SMRiP34998. Positions 24-108, 117-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34998.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 10810Important for peptide agonist binding
Regioni309 – 31911Important for antagonist bindingAdd
BLAST

Domaini

The transmembrane domain is composed of seven transmembrane helices that are arranged in V-shape. Transmembrane helix 7 assumes a sharply kinked structure. The antagonist CP-376395 binds at an allosteric site, far from the presumed binding site for the physiological peptide ligand.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295825.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000230719.
HOVERGENiHBG106921.
InParanoidiP34998.
KOiK04578.
OMAiTTNNVYR.
PhylomeDBiP34998.
TreeFamiTF315710.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR003052. GPCR_2_CRF1_rcpt.
IPR003051. GPCR_2_CRF_rcpt.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR01279. CRFRECEPTOR.
PR01280. CRFRECEPTOR1.
PR00249. GPCRSECRETIN.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform CRF-R1 (identifier: P34998-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MGGHPQLRLV KALLLLGLNP VSASLQDQHC ESLSLASNIS GLQCNASVDL
60 70 80 90 100
IGTCWPRSPA GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS
110 120 130 140 150
ECQEILNEEK KSKVHYHVAV IINYLGHCIS LVALLVAFVL FLRLRPGCTH
160 170 180 190 200
WGDQADGALE VGAPWSGAPF QVRRSIRCLR NIIHWNLISA FILRNATWFV
210 220 230 240 250
VQLTMSPEVH QSNVGWCRLV TAAYNYFHVT NFFWMFGEGC YLHTAIVLTY
260 270 280 290 300
STDRLRKWMF ICIGWGVPFP IIVAWAIGKL YYDNEKCWFG KRPGVYTDYI
310 320 330 340 350
YQGPMILVLL INFIFLFNIV RILMTKLRAS TTSETIQYRK AVKATLVLLP
360 370 380 390 400
LLGITYMLFF VNPGEDEVSR VVFIYFNSFL ESFQGFFVSV FYCFLNSEVR
410 420 430 440
SAIRKRWHRW QDKHSIRARV ARAMSIPTSP TRVSFHSIKQ STAV
Length:444
Mass (Da):50,719
Last modified:February 1, 1994 - v1
Checksum:i7221AEFB0E7AA8ED
GO
Isoform CRF-R2 (identifier: P34998-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     146-174: Missing.

Note: Major isoform.

Show »
Length:415
Mass (Da):47,671
Checksum:i81445283CCE34C6E
GO
Isoform CRF-R3 (identifier: P34998-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-81: GLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTN → D
     146-174: Missing.

Note: Does not bind to CRF with high affinity.

Show »
Length:375
Mass (Da):43,331
Checksum:i6A2068BE9386F8B0
GO
Isoform CRF-R4 (identifier: P34998-4) [UniParc]FASTAAdd to Basket

Also known as: 1D

The sequence of this isoform differs from the canonical sequence as follows:
     146-174: Missing.
     385-398: Missing.

Show »
Length:401
Mass (Da):46,030
Checksum:i3D8FF9B128810372
GO
Isoform 5 (identifier: P34998-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.

Show »
Length:240
Mass (Da):28,122
Checksum:iF4465F15BF7C52E4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 204204Missing in isoform 5. 2 PublicationsVSP_045434Add
BLAST
Alternative sequencei41 – 8141GLQCN…YNTTN → D in isoform CRF-R3. 1 PublicationVSP_001996Add
BLAST
Alternative sequencei146 – 17429Missing in isoform CRF-R2, isoform CRF-R3 and isoform CRF-R4. 7 PublicationsVSP_001997Add
BLAST
Alternative sequencei385 – 39814Missing in isoform CRF-R4. 1 PublicationVSP_001998Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23333 mRNA. Translation: AAA35719.1.
L23332 mRNA. Translation: AAA35718.1.
X72304 mRNA. Translation: CAA51052.1.
AF039523
, AF039510, AF039511, AF039512, AF039513, AF039514, AF039515, AF039516, AF039517, AF039518, AF039519, AF039520, AF039521, AF039522 Genomic DNA. Translation: AAC69993.1.
U16273 mRNA. Translation: AAC50073.1.
AF180301 mRNA. Translation: AAD52688.1.
FJ543100 mRNA. Translation: ACU68591.1.
AY457172 mRNA. Translation: AAR19768.1.
AB451466 mRNA. Translation: BAG70280.1.
AK295559 mRNA. Translation: BAG58461.1.
AC126544 Genomic DNA. No translation available.
AC217770 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
AC217774 Genomic DNA. No translation available.
AC225613 Genomic DNA. No translation available.
CH471233 Genomic DNA. Translation: EAW93557.1.
BC096836 mRNA. Translation: AAH96836.1.
CCDSiCCDS42350.1. [P34998-2]
CCDS45712.1. [P34998-1]
CCDS45713.1. [P34998-4]
CCDS45714.1. [P34998-3]
PIRiI38879.
I60975. A48260.
RefSeqiNP_001138618.1. NM_001145146.1. [P34998-1]
NP_001138619.1. NM_001145147.1. [P34998-3]
NP_001138620.1. NM_001145148.1. [P34998-4]
NP_001243228.1. NM_001256299.1. [P34998-5]
NP_004373.2. NM_004382.4. [P34998-2]
UniGeneiHs.417628.

Genome annotation databases

EnsembliENST00000314537; ENSP00000326060; ENSG00000120088. [P34998-2]
ENST00000352855; ENSP00000344068; ENSG00000120088. [P34998-3]
ENST00000398285; ENSP00000381333; ENSG00000120088. [P34998-1]
ENST00000577353; ENSP00000462016; ENSG00000120088. [P34998-4]
ENST00000613260; ENSP00000484387; ENSG00000278232. [P34998-1]
ENST00000615345; ENSP00000480752; ENSG00000278232. [P34998-3]
ENST00000616274; ENSP00000480396; ENSG00000276191. [P34998-1]
ENST00000616748; ENSP00000478177; ENSG00000276191. [P34998-3]
ENST00000617905; ENSP00000483802; ENSG00000276191. [P34998-2]
ENST00000618382; ENSP00000477786; ENSG00000278232. [P34998-2]
GeneIDi1394.
KEGGihsa:1394.
UCSCiuc002ijm.3. human. [P34998-2]
uc002ijn.3. human. [P34998-3]
uc002ijo.2. human. [P34998-1]
uc010dar.3. human. [P34998-4]

Polymorphism databases

DMDMi461836.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23333 mRNA. Translation: AAA35719.1.
L23332 mRNA. Translation: AAA35718.1.
X72304 mRNA. Translation: CAA51052.1.
AF039523
, AF039510, AF039511, AF039512, AF039513, AF039514, AF039515, AF039516, AF039517, AF039518, AF039519, AF039520, AF039521, AF039522 Genomic DNA. Translation: AAC69993.1.
U16273 mRNA. Translation: AAC50073.1.
AF180301 mRNA. Translation: AAD52688.1.
FJ543100 mRNA. Translation: ACU68591.1.
AY457172 mRNA. Translation: AAR19768.1.
AB451466 mRNA. Translation: BAG70280.1.
AK295559 mRNA. Translation: BAG58461.1.
AC126544 Genomic DNA. No translation available.
AC217770 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
AC217774 Genomic DNA. No translation available.
AC225613 Genomic DNA. No translation available.
CH471233 Genomic DNA. Translation: EAW93557.1.
BC096836 mRNA. Translation: AAH96836.1.
CCDSiCCDS42350.1. [P34998-2]
CCDS45712.1. [P34998-1]
CCDS45713.1. [P34998-4]
CCDS45714.1. [P34998-3]
PIRiI38879.
I60975. A48260.
RefSeqiNP_001138618.1. NM_001145146.1. [P34998-1]
NP_001138619.1. NM_001145147.1. [P34998-3]
NP_001138620.1. NM_001145148.1. [P34998-4]
NP_001243228.1. NM_001256299.1. [P34998-5]
NP_004373.2. NM_004382.4. [P34998-2]
UniGeneiHs.417628.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L27NMR-A25-108[»]
3EHSX-ray2.76A24-119[»]
3EHTX-ray3.40A24-119[»]
3EHUX-ray1.96A/B24-119[»]
4K5YX-ray2.98A/B/C104-373[»]
ProteinModelPortaliP34998.
SMRiP34998. Positions 24-108, 117-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107784. 8 interactions.
IntActiP34998. 2 interactions.
MINTiMINT-1217325.
STRINGi9606.ENSP00000381333.

Chemistry

BindingDBiP34998.
ChEMBLiCHEMBL1800.
GuidetoPHARMACOLOGYi212.

Protein family/group databases

TCDBi9.A.14.4.3. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

PTM databases

PhosphoSiteiP34998.

Polymorphism databases

DMDMi461836.

Proteomic databases

PaxDbiP34998.
PRIDEiP34998.

Protocols and materials databases

DNASUi1394.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314537; ENSP00000326060; ENSG00000120088. [P34998-2]
ENST00000352855; ENSP00000344068; ENSG00000120088. [P34998-3]
ENST00000398285; ENSP00000381333; ENSG00000120088. [P34998-1]
ENST00000577353; ENSP00000462016; ENSG00000120088. [P34998-4]
ENST00000613260; ENSP00000484387; ENSG00000278232. [P34998-1]
ENST00000615345; ENSP00000480752; ENSG00000278232. [P34998-3]
ENST00000616274; ENSP00000480396; ENSG00000276191. [P34998-1]
ENST00000616748; ENSP00000478177; ENSG00000276191. [P34998-3]
ENST00000617905; ENSP00000483802; ENSG00000276191. [P34998-2]
ENST00000618382; ENSP00000477786; ENSG00000278232. [P34998-2]
GeneIDi1394.
KEGGihsa:1394.
UCSCiuc002ijm.3. human. [P34998-2]
uc002ijn.3. human. [P34998-3]
uc002ijo.2. human. [P34998-1]
uc010dar.3. human. [P34998-4]

Organism-specific databases

CTDi1394.
GeneCardsiGC17P043733.
HGNCiHGNC:2357. CRHR1.
MIMi122561. gene.
neXtProtiNX_P34998.
PharmGKBiPA26874.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295825.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000230719.
HOVERGENiHBG106921.
InParanoidiP34998.
KOiK04578.
OMAiTTNNVYR.
PhylomeDBiP34998.
TreeFamiTF315710.

Enzyme and pathway databases

ReactomeiREACT_18372. Class B/2 (Secretin family receptors).
REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSiCRHR1. human.
EvolutionaryTraceiP34998.
GeneWikiiCorticotropin_releasing_hormone_receptor_1.
GenomeRNAii1394.
NextBioi5703.
PROiP34998.
SOURCEiSearch...

Gene expression databases

BgeeiP34998.
CleanExiHS_CRHR1.
ExpressionAtlasiP34998. baseline.
GenevestigatoriP34998.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR003052. GPCR_2_CRF1_rcpt.
IPR003051. GPCR_2_CRF_rcpt.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR01279. CRFRECEPTOR.
PR01280. CRFRECEPTOR1.
PR00249. GPCRSECRETIN.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression cloning of a human corticotropin-releasing-factor receptor."
    Chen R., Lewis K.A., Perrin M.H., Vale W.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:8967-8971(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRF-R1 AND CRF-R2).
    Tissue: Pituitary.
  2. "Primary structure and functional expression of mouse pituitary and human brain corticotrophin releasing factor receptors."
    Vita N., Laurent P., Lefort S., Chalon P., Lelias J.-M., Kaghad M., le Fur G., Caput D., Ferrara P.
    FEBS Lett. 335:1-5(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF-R2), TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "The genomic organization of the human corticotropin-releasing factor type-1 receptor."
    Sakai K., Yamada M., Horiba N., Wakui M., Demura H., Suda T.
    Gene 219:125-130(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "A variant of the human corticotropin-releasing factor (CRF) receptor: cloning, expression and pharmacology."
    Ross P.C., Kostas C.M., Ramabhadran T.V.
    Biochem. Biophys. Res. Commun. 205:1836-1842(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF-R3).
    Tissue: Hippocampus.
  5. "A novel spliced variant of the type 1 corticotropin-releasing hormone receptor with a deletion in the seventh transmembrane domain present in the human pregnant term myometrium and fetal membranes."
    Grammatopoulos D.K., Dai Y., Randeva H.S., Levine M.A., Karteris E., Easton A.J., Hillhouse E.W.
    Mol. Endocrinol. 13:2189-2202(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF-R4).
  6. "A novel CRF1 splice isoform involved in neurodegenerative and stress disorders."
    Sherrin T., Murthy S.R., Spiess J.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  7. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    King M.M., Aronstam R.S., Sharma S.V.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF-R2).
    Tissue: Brain.
  8. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF-R2).
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Hippocampus.
  10. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF-R2).
  13. "Expression, purification, and characterization of a soluble form of the first extracellular domain of the human type 1 corticotropin releasing factor receptor."
    Perrin M.H., Fischer W.H., Kunitake K.S., Craig A.G., Koerber S.C., Cervini L.A., Rivier J.E., Groppe J.C., Greenwald J., Moller Nielsen S., Vale W.W.
    J. Biol. Chem. 276:31528-31534(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-31, DISULFIDE BONDS.
  14. "Protein kinase A-induced negative regulation of the corticotropin-releasing hormone R1alpha receptor-extracellularly regulated kinase signal transduction pathway: the critical role of Ser301 for signaling switch and selectivity."
    Papadopoulou N., Chen J., Randeva H.S., Levine M.A., Hillhouse E.W., Grammatopoulos D.K.
    Mol. Endocrinol. 18:624-639(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-330.
  15. "Activation of corticotropin-releasing factor receptor 1 selectively inhibits CaV3.2 T-type calcium channels."
    Tao J., Hildebrand M.E., Liao P., Liang M.C., Tan G., Li S., Snutch T.P., Soong T.W.
    Mol. Pharmacol. 73:1596-1609(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "Structural basis for hormone recognition by the Human CRFR2{alpha} G protein-coupled receptor."
    Pal K., Swaminathan K., Xu H.E., Pioszak A.A.
    J. Biol. Chem. 285:40351-40361(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRF AND UCN.
  17. "Role of SAP97 protein in the regulation of corticotropin-releasing factor receptor 1 endocytosis and extracellular signal-regulated kinase 1/2 signaling."
    Dunn H.A., Walther C., Godin C.M., Hall R.A., Ferguson S.S.
    J. Biol. Chem. 288:15023-15034(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DLG1.
  18. "Molecular recognition of corticotropin-releasing factor by its G-protein-coupled receptor CRFR1."
    Pioszak A.A., Parker N.R., Suino-Powell K., Xu H.E.
    J. Biol. Chem. 283:32900-32912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 24-119 IN COMPLEX WITH CRH, FUNCTION, DISULFIDE BONDS.
  19. "NMR structure of the first extracellular domain of corticotropin-releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high affinity agonist."
    Grace C.R., Perrin M.H., Gulyas J., Rivier J.E., Vale W.W., Riek R.
    J. Biol. Chem. 285:38580-38589(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-109 IN COMPLEX WITH SYNTHETIC CRH ANALOG.
  20. "Structure of class B GPCR corticotropin-releasing factor receptor 1."
    Hollenstein K., Kean J., Bortolato A., Cheng R.K., Dore A.S., Jazayeri A., Cooke R.M., Weir M., Marshall F.H.
    Nature 499:438-443(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 104-373 IN COMPLEX WITH THE SYNTHETIC ANTAGONIST CP-376395, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DISULFIDE BOND, ANTAGONIST BINDING SITES, MUTAGENESIS OF PHE-232; MET-235; LEU-309; ASN-312; PHE-313; LEU-316; ILE-319; TYR-356 AND GLN-384.

Entry informationi

Entry nameiCRFR1_HUMAN
AccessioniPrimary (citable) accession number: P34998
Secondary accession number(s): B4DIE9
, Q13008, Q4QRJ1, Q9UK64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 4, 2015
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.