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P34998

- CRFR1_HUMAN

UniProt

P34998 - CRFR1_HUMAN

Protein

Corticotropin-releasing factor receptor 1

Gene

CRHR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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
    4. protein binding Source: IntAct

    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 hypoxia Source: Ensembl
    30. response to immobilization stress Source: Ensembl
    31. visual learning Source: Ensembl

    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

    Organism-specific databases

    HGNCiHGNC:2357. CRHR1.

    Subcellular locationi

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

    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

    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

    ArrayExpressiP34998.
    BgeeiP34998.
    CleanExiHS_CRHR1.
    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
    Helixi28 – 325
    Beta strandi49 – 524
    Beta strandi62 – 676
    Beta strandi70 – 745
    Beta strandi81 – 877
    Turni89 – 913
    Beta strandi93 – 986
    Helixi99 – 1013
    Helixi103 – 1075
    Helixi116 – 14328
    Helixi175 – 1773
    Helixi179 – 20527
    Helixi207 – 2126
    Helixi215 – 23723
    Helixi239 – 24810
    Helixi250 – 2534
    Helixi257 – 2593
    Helixi270 – 29627
    Helixi304 – 33128
    Helixi339 – 36729
    Helixi374 – 3829
    Helixi384 – 39512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 11188ExtracellularAdd
    BLAST
    Topological domaini143 – 17836CytoplasmicAdd
    BLAST
    Topological domaini204 – 21815ExtracellularAdd
    BLAST
    Topological domaini248 – 2547Cytoplasmic
    Topological domaini283 – 29816ExtracellularAdd
    BLAST
    Topological domaini325 – 33511CytoplasmicAdd
    BLAST
    Topological domaini361 – 3677Extracellular
    Topological domaini398 – 44447CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei112 – 14231Helical; Name=1Add
    BLAST
    Transmembranei179 – 20325Helical; Name=2Add
    BLAST
    Transmembranei219 – 24729Helical; Name=3Add
    BLAST
    Transmembranei255 – 28228Helical; Name=4Add
    BLAST
    Transmembranei299 – 32426Helical; Name=5Add
    BLAST
    Transmembranei336 – 36025Helical; Name=6Add
    BLAST
    Transmembranei368 – 39730Helical; Name=7Add
    BLAST

    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.
    HOGENOMiHOG000230719.
    HOVERGENiHBG106921.
    KOiK04578.
    OMAiVGWCRLV.
    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

    MGGHPQLRLV KALLLLGLNP VSASLQDQHC ESLSLASNIS GLQCNASVDL    50
    IGTCWPRSPA GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS 100
    ECQEILNEEK KSKVHYHVAV IINYLGHCIS LVALLVAFVL FLRLRPGCTH 150
    WGDQADGALE VGAPWSGAPF QVRRSIRCLR NIIHWNLISA FILRNATWFV 200
    VQLTMSPEVH QSNVGWCRLV TAAYNYFHVT NFFWMFGEGC YLHTAIVLTY 250
    STDRLRKWMF ICIGWGVPFP IIVAWAIGKL YYDNEKCWFG KRPGVYTDYI 300
    YQGPMILVLL INFIFLFNIV RILMTKLRAS TTSETIQYRK AVKATLVLLP 350
    LLGITYMLFF VNPGEDEVSR VVFIYFNSFL ESFQGFFVSV FYCFLNSEVR 400
    SAIRKRWHRW QDKHSIRARV ARAMSIPTSP TRVSFHSIKQ STAV 444
    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:
    EMBL
    GenBank
    DDBJ
    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]
    CCDS58556.1. [P34998-5]
    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

    EnsembliENST00000293493; ENSP00000293493; ENSG00000120088. [P34998-5]
    ENST00000314537; ENSP00000326060; ENSG00000120088. [P34998-2]
    ENST00000352855; ENSP00000344068; ENSG00000120088. [P34998-3]
    ENST00000398285; ENSP00000381333; ENSG00000120088. [P34998-1]
    ENST00000577353; ENSP00000462016; ENSG00000120088. [P34998-4]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS42350.1. [P34998-2 ]
    CCDS45712.1. [P34998-1 ]
    CCDS45713.1. [P34998-4 ]
    CCDS45714.1. [P34998-3 ]
    CCDS58556.1. [P34998-5 ]
    PIRi I38879.
    I60975. A48260.
    RefSeqi NP_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 ]
    UniGenei Hs.417628.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L27 NMR - A 25-108 [» ]
    3EHS X-ray 2.76 A 24-119 [» ]
    3EHT X-ray 3.40 A 24-119 [» ]
    3EHU X-ray 1.96 A/B 24-119 [» ]
    4K5Y X-ray 2.98 A/B/C 104-373 [» ]
    ProteinModelPortali P34998.
    SMRi P34998. Positions 24-108, 117-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107784. 8 interactions.
    IntActi P34998. 2 interactions.
    MINTi MINT-1217325.
    STRINGi 9606.ENSP00000381333.

    Chemistry

    BindingDBi P34998.
    ChEMBLi CHEMBL1800.
    GuidetoPHARMACOLOGYi 212.

    Protein family/group databases

    TCDBi 9.A.14.4.3. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei P34998.

    Polymorphism databases

    DMDMi 461836.

    Proteomic databases

    PaxDbi P34998.
    PRIDEi P34998.

    Protocols and materials databases

    DNASUi 1394.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293493 ; ENSP00000293493 ; ENSG00000120088 . [P34998-5 ]
    ENST00000314537 ; ENSP00000326060 ; ENSG00000120088 . [P34998-2 ]
    ENST00000352855 ; ENSP00000344068 ; ENSG00000120088 . [P34998-3 ]
    ENST00000398285 ; ENSP00000381333 ; ENSG00000120088 . [P34998-1 ]
    ENST00000577353 ; ENSP00000462016 ; ENSG00000120088 . [P34998-4 ]
    GeneIDi 1394.
    KEGGi hsa:1394.
    UCSCi uc002ijm.3. human. [P34998-2 ]
    uc002ijn.3. human. [P34998-3 ]
    uc002ijo.2. human. [P34998-1 ]
    uc010dar.3. human. [P34998-4 ]

    Organism-specific databases

    CTDi 1394.
    GeneCardsi GC17P043704.
    HGNCi HGNC:2357. CRHR1.
    MIMi 122561. gene.
    neXtProti NX_P34998.
    PharmGKBi PA26874.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295825.
    HOGENOMi HOG000230719.
    HOVERGENi HBG106921.
    KOi K04578.
    OMAi VGWCRLV.
    PhylomeDBi P34998.
    TreeFami TF315710.

    Enzyme and pathway databases

    Reactomei REACT_18372. Class B/2 (Secretin family receptors).
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P34998.
    GeneWikii Corticotropin_releasing_hormone_receptor_1.
    GenomeRNAii 1394.
    NextBioi 5703.
    PROi P34998.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P34998.
    Bgeei P34998.
    CleanExi HS_CRHR1.
    Genevestigatori P34998.

    Family and domain databases

    InterProi IPR017981. 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 ]
    Pfami PF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view ]
    PRINTSi PR01279. CRFRECEPTOR.
    PR01280. CRFRECEPTOR1.
    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

    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: October 1, 2014
    This is version 146 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