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Q60748

- CRFR2_MOUSE

UniProt

Q60748 - CRFR2_MOUSE

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Protein

Corticotropin-releasing factor receptor 2

Gene

Crhr2

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

Functioni

G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for 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.

GO - Molecular functioni

  1. corticotrophin-releasing factor receptor activity Source: MGI
  2. hormone activity Source: MGI

GO - Biological processi

  1. cellular response to corticotropin-releasing hormone stimulus Source: GOC
  2. G-protein coupled receptor signaling pathway Source: MGI
  3. negative regulation of angiogenesis Source: MGI
  4. negative regulation of cAMP-mediated signaling Source: MGI
  5. positive regulation of cAMP-mediated signaling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
Corticotropin-releasing factor receptor 2
Short name:
CRF-R-2
Short name:
CRF-R2
Short name:
CRFR-2
Alternative name(s):
CRF-RB
Corticotropin-releasing hormone receptor 2
Short name:
CRH-R-2
Short name:
CRH-R2
Gene namesi
Name:Crhr2
Synonyms:Crf2r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:894312. Crhr2.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: MGI
  3. Golgi apparatus Source: MGI
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451D → A: Disrupts internal salt bridge and abrogates ligand recognition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Corticotropin-releasing factor receptor 2PRO_0000012821Add
BLAST
Signal peptidei1 – 1919Not cleavedBy similarityAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi14 ↔ 50By similarity
Disulfide bondi40 ↔ 83
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi64 ↔ 98
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi184 ↔ 254By similarity

Post-translational modificationi

A N-glycosylation site within the signal peptide impedes its proper cleavage and function.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ60748.

PTM databases

PhosphoSiteiQ60748.

Expressioni

Tissue specificityi

Highly expressed in the heart. Also expressed in lungs, skeletal muscle, gastrointestinal tract, epididymis, and brain.

Gene expression databases

CleanExiMM_CRHR2.
ExpressionAtlasiQ60748. baseline and differential.
GenevestigatoriQ60748.

Interactioni

Subunit structurei

Monomer. Interacts with CRF, UCN, UCN2 and UCN3 (By similarity).By similarity

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 483
Beta strandi58 – 636
Beta strandi69 – 713
Beta strandi78 – 836
Turni85 – 873
Beta strandi97 – 993

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U34NMR-A35-113[»]
2JNCNMR-A35-113[»]
2JNDNMR-A35-113[»]
ProteinModelPortaliQ60748.
SMRiQ60748. Positions 3-113, 115-363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60748.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 108108ExtracellularBy similarityAdd
BLAST
Topological domaini140 – 1467CytoplasmicBy similarity
Topological domaini172 – 18514ExtracellularBy similarityAdd
BLAST
Topological domaini215 – 2217CytoplasmicBy similarity
Topological domaini250 – 26516ExtracellularBy similarityAdd
BLAST
Topological domaini292 – 30211CytoplasmicBy similarityAdd
BLAST
Topological domaini328 – 3347ExtracellularBy similarity
Topological domaini365 – 41147CytoplasmicBy similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei109 – 13931Helical; Name=1By similarityAdd
BLAST
Transmembranei147 – 17125Helical; Name=2By similarityAdd
BLAST
Transmembranei186 – 21429Helical; Name=3By similarityAdd
BLAST
Transmembranei222 – 24928Helical; Name=4By similarityAdd
BLAST
Transmembranei266 – 29126Helical; Name=5By similarityAdd
BLAST
Transmembranei303 – 32725Helical; Name=6By similarityAdd
BLAST
Transmembranei335 – 36430Helical; Name=7By similarityAdd
BLAST

Family & Domainsi

Domaini

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).By similarity
The uncleaved pseudo signal peptide prevents receptor's oligomerization and coupling to G(i) subunits. It is also responsible for the rather low receptor localization at the plasma membrane (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295825.
HOGENOMiHOG000230719.
HOVERGENiHBG106921.
InParanoidiQ60748.
KOiK04579.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR003053. GPCR_2_CRF2_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.
PR01281. CRFRECEPTOR2.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform CRF2-alpha (identifier: Q60748-1) [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
MDAALLLSLL EANCSLALAE ELLLDGWGVP PDPEGPYTYC NTTLDQIGTC
60 70 80 90 100
WPQSAPGALV ERPCPEYFNG IKYNTTRNAY RECLENGTWA SRVNYSHCEP
110 120 130 140 150
ILDDKQRKYD LHYRIALIVN YLGHCVSVVA LVAAFLLFLV LRSIRCLRNV
160 170 180 190 200
IHWNLITTFI LRNIAWFLLQ LIDHEVHEGN EVWCRCITTI FNYFVVTNFF
210 220 230 240 250
WMFVEGCYLH TAIVMTYSTE HLRKWLFLFI GWCIPCPIII AWAVGKLYYE
260 270 280 290 300
NEQCWFGKEA GDLVDYIYQG PVMLVLLINF VFLFNIVRIL MTKLRASTTS
310 320 330 340 350
ETIQYRKAVK ATLVLLPLLG ITYMLFFVNP GEDDLSQIVF IYFNSFLQSF
360 370 380 390 400
QGFFVSVFYC FFNGEVRAAL RKRWHRWQDH HALRVPVARA MSIPTSPTRI
410
SFHSIKQTAA V
Length:411
Mass (Da):47,623
Last modified:January 22, 2014 - v2
Checksum:iC0EAD0BC6A064683
GO
Isoform CRF2-beta (identifier: Q60748-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MDAALLLSLLEANCSLALAEELLLDGWGVPPDPE → MGTPGSLPSA...CHRTTIGNFS

Note: Contains a disulfide bond in positions 45-70.Curated

Show »
Length:431
Mass (Da):49,923
Checksum:iA6D9EDE575DB8061
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061Missing in AAC52243. (PubMed:7565810)Curated
Sequence conflicti372 – 3732KR → NG in AAC52243. (PubMed:7565810)Curated
Sequence conflicti376 – 3772RW → SG in AAC52174. (PubMed:7755719)Curated
Sequence conflicti388 – 3881A → R in AAC52174. (PubMed:7755719)Curated
Isoform CRF2-beta (identifier: Q60748-2)
Sequence conflicti3 – 53TPG → QQI in AAC52174. (PubMed:7755719)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MDAAL…PPDPE → MGTPGSLPSAQLLLCLFSLL PVLQVAQPGQAPQDQPLWTL LEQYCHRTTIGNFS in isoform CRF2-beta. 4 PublicationsVSP_053568Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17858 mRNA. Translation: AAA68026.1.
U21729 mRNA. Translation: AAC52174.1.
U19939 mRNA. Translation: AAC52243.1.
AY445512 mRNA. Translation: AAS07021.1.
BC137592 mRNA. Translation: AAI37593.1.
PIRiA56726.
I49149.
I49279.
RefSeqiNP_001275548.1. NM_001288619.1. [Q60748-1]
UniGeneiMm.236081.

Genome annotation databases

GeneIDi12922.
KEGGimmu:12922.
UCSCiuc009cal.2. mouse. [Q60748-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17858 mRNA. Translation: AAA68026.1 .
U21729 mRNA. Translation: AAC52174.1 .
U19939 mRNA. Translation: AAC52243.1 .
AY445512 mRNA. Translation: AAS07021.1 .
BC137592 mRNA. Translation: AAI37593.1 .
PIRi A56726.
I49149.
I49279.
RefSeqi NP_001275548.1. NM_001288619.1. [Q60748-1 ]
UniGenei Mm.236081.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U34 NMR - A 35-113 [» ]
2JNC NMR - A 35-113 [» ]
2JND NMR - A 35-113 [» ]
ProteinModelPortali Q60748.
SMRi Q60748. Positions 3-113, 115-363.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q60748.
ChEMBLi CHEMBL2253.
GuidetoPHARMACOLOGYi 213.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei Q60748.

Proteomic databases

PRIDEi Q60748.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 12922.
KEGGi mmu:12922.
UCSCi uc009cal.2. mouse. [Q60748-1 ]

Organism-specific databases

CTDi 1395.
MGIi MGI:894312. Crhr2.

Phylogenomic databases

eggNOGi NOG295825.
HOGENOMi HOG000230719.
HOVERGENi HBG106921.
InParanoidi Q60748.
KOi K04579.

Miscellaneous databases

EvolutionaryTracei Q60748.
PROi Q60748.
SOURCEi Search...

Gene expression databases

CleanExi MM_CRHR2.
ExpressionAtlasi Q60748. baseline and differential.
Genevestigatori Q60748.

Family and domain databases

InterProi IPR017981. GPCR_2-like.
IPR003053. GPCR_2_CRF2_rcpt.
IPR003051. GPCR_2_CRF_rcpt.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view ]
Pfami PF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view ]
PRINTSi PR01279. CRFRECEPTOR.
PR01281. CRFRECEPTOR2.
PR00249. GPCRSECRETIN.
SMARTi SM00008. HormR. 1 hit.
[Graphical view ]
PROSITEi PS00649. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a second corticotropin-releasing factor receptor gene and characterization of a cDNA expressed in heart."
    Perrin M., Donaldson C., Chen R., Blount A., Berggren T., Bilezikjian L., Sawchenko P., Vale W.
    Proc. Natl. Acad. Sci. U.S.A. 92:2969-2973(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-BETA).
    Tissue: Heart.
  2. "A sauvagine/corticotropin-releasing factor receptor expressed in heart and skeletal muscle."
    Kishimoto T., Pearse R.V. II, Lin C.R., Rosenfeld M.G.
    Proc. Natl. Acad. Sci. U.S.A. 92:1108-1112(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-BETA).
    Strain: BALB/c.
    Tissue: Heart.
  3. "Identification of a novel murine receptor for corticotropin-releasing hormone expressed in the heart."
    Stenzel P., Kesterson R., Yeung W., Cone R.D., Rittenberg M.B., Stenzel-Poore M.P.
    Mol. Endocrinol. 9:637-645(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-BETA).
    Strain: BALB/c.
    Tissue: Heart.
  4. "Mouse corticotropin-releasing factor receptor type 2alpha gene: isolation, distribution, pharmacological characterization and regulation by stress and glucocorticoids."
    Chen A., Perrin M., Brar B., Li C., Jamieson P., DiGruccio M., Lewis K., Vale W.
    Mol. Endocrinol. 19:441-458(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-ALPHA).
    Strain: C57BL/6 X 129.
  5. "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 CRF2-BETA).
    Tissue: Brain.
  6. "NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor."
    Grace C.R., Perrin M.H., DiGruccio M.R., Miller C.L., Rivier J.E., Vale W.W., Riek R.
    Proc. Natl. Acad. Sci. U.S.A. 101:12836-12841(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 39-133 (ISOFORM CRF2-BETA), DISULFIDE BONDS.
  7. "The three-dimensional structure of the N-terminal domain of corticotropin-releasing factor receptors: sushi domains and the B1 family of G protein-coupled receptors."
    Perrin M.H., Grace C.R., Riek R., Vale W.W.
    Ann. N. Y. Acad. Sci. 1070:105-119(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 39-133 (ISOFORM CRF2-BETA) IN COMPLEX WITH PEPTIDE LIGAND, DISULFIDE BONDS, MUTAGENESIS OF ASP-45.
  8. "Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand."
    Grace C.R., Perrin M.H., Gulyas J., Digruccio M.R., Cantle J.P., Rivier J.E., Vale W.W., Riek R.
    Proc. Natl. Acad. Sci. U.S.A. 104:4858-4863(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 39-133 (ISOFORM CRF2-BETA) IN COMPLEX WITH PEPTIDE LIGAND, DISULFIDE BONDS.

Entry informationi

Entry nameiCRFR2_MOUSE
AccessioniPrimary (citable) accession number: Q60748
Secondary accession number(s): B9EHB5
, Q5GL24, Q60783, Q60808
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 22, 2014
Last modified: October 29, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3