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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_HUMAN             Reviewed;         444 AA.
P34998; B4DIE9; Q13008; Q4QRJ1; Q9UK64;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 180.
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=CRFR, CRFR1, CRHR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRF-R1 AND CRF-R2).
TISSUE=Pituitary;
PubMed=7692441; DOI=10.1073/pnas.90.19.8967;
Chen R., Lewis K.A., Perrin M.H., Vale W.W.;
"Expression cloning of a human corticotropin-releasing-factor
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 90:8967-8971(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF-R2), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8243652; DOI=10.1016/0014-5793(93)80427-V;
Vita N., Laurent P., Lefort S., Chalon P., Lelias J.-M., Kaghad M.,
le Fur G., Caput D., Ferrara P.;
"Primary structure and functional expression of mouse pituitary and
human brain corticotrophin releasing factor receptors.";
FEBS Lett. 335:1-5(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9757017; DOI=10.1016/S0378-1119(98)00322-9;
Sakai K., Yamada M., Horiba N., Wakui M., Demura H., Suda T.;
"The genomic organization of the human corticotropin-releasing factor
type-1 receptor.";
Gene 219:125-130(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF-R3).
TISSUE=Hippocampus;
PubMed=7811272; DOI=10.1006/bbrc.1994.2884;
Ross P.C., Kostas C.M., Ramabhadran T.V.;
"A variant of the human corticotropin-releasing factor (CRF) receptor:
cloning, expression and pharmacology.";
Biochem. Biophys. Res. Commun. 205:1836-1842(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF-R4).
PubMed=10598591; DOI=10.1210/mend.13.12.0391;
Grammatopoulos D.K., Dai Y., Randeva H.S., Levine M.A., Karteris E.,
Easton A.J., Hillhouse E.W.;
"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.";
Mol. Endocrinol. 13:2189-2202(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Sherrin T., Murthy S.R., Spiess J.;
"A novel CRF1 splice isoform involved in neurodegenerative and stress
disorders.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF-R2).
TISSUE=Brain;
King M.M., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF-R2).
PubMed=19054851; DOI=10.1038/nmeth.1273;
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.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF-R2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 24-31, AND DISULFIDE BONDS.
PubMed=11425856; DOI=10.1074/jbc.M101838200;
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.;
"Expression, purification, and characterization of a soluble form of
the first extracellular domain of the human type 1 corticotropin
releasing factor receptor.";
J. Biol. Chem. 276:31528-31534(2001).
[14]
PHOSPHORYLATION AT SER-330.
PubMed=14657255; DOI=10.1210/me.2003-0365;
Papadopoulou N., Chen J., Randeva H.S., Levine M.A., Hillhouse E.W.,
Grammatopoulos D.K.;
"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.";
Mol. Endocrinol. 18:624-639(2004).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18292205; DOI=10.1124/mol.107.043612;
Tao J., Hildebrand M.E., Liao P., Liang M.C., Tan G., Li S.,
Snutch T.P., Soong T.W.;
"Activation of corticotropin-releasing factor receptor 1 selectively
inhibits CaV3.2 T-type calcium channels.";
Mol. Pharmacol. 73:1596-1609(2008).
[16]
INTERACTION WITH CRF AND UCN.
PubMed=20966082; DOI=10.1074/jbc.M110.186072;
Pal K., Swaminathan K., Xu H.E., Pioszak A.A.;
"Structural basis for hormone recognition by the Human CRFR2{alpha} G
protein-coupled receptor.";
J. Biol. Chem. 285:40351-40361(2010).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DLG1.
PubMed=23576434; DOI=10.1074/jbc.M113.473660;
Dunn H.A., Walther C., Godin C.M., Hall R.A., Ferguson S.S.;
"Role of SAP97 protein in the regulation of corticotropin-releasing
factor receptor 1 endocytosis and extracellular signal-regulated
kinase 1/2 signaling.";
J. Biol. Chem. 288:15023-15034(2013).
[18]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 24-119 IN COMPLEX WITH CRH,
FUNCTION, AND DISULFIDE BONDS.
PubMed=18801728; DOI=10.1074/jbc.M805749200;
Pioszak A.A., Parker N.R., Suino-Powell K., Xu H.E.;
"Molecular recognition of corticotropin-releasing factor by its G-
protein-coupled receptor CRFR1.";
J. Biol. Chem. 283:32900-32912(2008).
[19]
STRUCTURE BY NMR OF 25-109 IN COMPLEX WITH SYNTHETIC CRH ANALOG.
PubMed=20843795; DOI=10.1074/jbc.M110.121897;
Grace C.R., Perrin M.H., Gulyas J., Rivier J.E., Vale W.W., Riek R.;
"NMR structure of the first extracellular domain of corticotropin-
releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high
affinity agonist.";
J. Biol. Chem. 285:38580-38589(2010).
[20]
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, AND
MUTAGENESIS OF PHE-232; MET-235; LEU-309; ASN-312; PHE-313; LEU-316;
ILE-319; TYR-356 AND GLN-384.
PubMed=23863939; DOI=10.1038/nature12357;
Hollenstein K., Kean J., Bortolato A., Cheng R.K., Dore A.S.,
Jazayeri A., Cooke R.M., Weir M., Marshall F.H.;
"Structure of class B GPCR corticotropin-releasing factor receptor
1.";
Nature 499:438-443(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:18292205, ECO:0000269|PubMed:18801728,
ECO:0000269|PubMed:23576434, ECO:0000269|PubMed:23863939}.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:18801728,
ECO:0000269|PubMed:20843795, ECO:0000269|PubMed:20966082,
ECO:0000269|PubMed:23576434, ECO:0000269|PubMed:23863939}.
-!- INTERACTION:
P06850:CRH; NbExp=2; IntAct=EBI-3870393, EBI-3870390;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endosome. Note=Agonist-binding promotes endocytosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=CRF-R1;
IsoId=P34998-1; Sequence=Displayed;
Name=CRF-R2;
IsoId=P34998-2; Sequence=VSP_001997;
Note=Major isoform.;
Name=CRF-R3;
IsoId=P34998-3; Sequence=VSP_001996, VSP_001997;
Note=Does not bind to CRF with high affinity.;
Name=CRF-R4; Synonyms=1D;
IsoId=P34998-4; Sequence=VSP_001997, VSP_001998;
Name=5;
IsoId=P34998-5; Sequence=VSP_045434;
-!- TISSUE SPECIFICITY: Predominantly expressed in the cerebellum,
pituitary, cerebral cortex and olfactory lobe.
{ECO:0000269|PubMed:8243652}.
-!- DOMAIN: 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.
-!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
{ECO:0000269|PubMed:14657255}.
-!- PTM: Phosphorylation at Ser-330 by PKA prevents maximal coupling
to Gq-protein, and thereby negatively regulates downstream
signaling. {ECO:0000269|PubMed:14657255}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; L23333; AAA35719.1; -; mRNA.
EMBL; L23332; AAA35718.1; -; mRNA.
EMBL; X72304; CAA51052.1; -; mRNA.
EMBL; AF039523; AAC69993.1; -; Genomic_DNA.
EMBL; AF039510; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039511; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039512; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039513; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039514; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039515; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039516; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039517; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039518; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039519; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039520; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039521; AAC69993.1; JOINED; Genomic_DNA.
EMBL; AF039522; AAC69993.1; JOINED; Genomic_DNA.
EMBL; U16273; AAC50073.1; -; mRNA.
EMBL; AF180301; AAD52688.1; -; mRNA.
EMBL; FJ543100; ACU68591.1; -; mRNA.
EMBL; AY457172; AAR19768.1; -; mRNA.
EMBL; AB451466; BAG70280.1; -; mRNA.
EMBL; AK295559; BAG58461.1; -; mRNA.
EMBL; AC126544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC225613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471233; EAW93557.1; -; Genomic_DNA.
EMBL; BC096836; AAH96836.1; -; mRNA.
CCDS; CCDS42350.1; -. [P34998-2]
CCDS; CCDS45712.1; -. [P34998-1]
CCDS; CCDS45713.1; -. [P34998-4]
CCDS; CCDS45714.1; -. [P34998-3]
CCDS; CCDS58556.1; -. [P34998-5]
PIR; I38879; I38879.
PIR; I60975; A48260.
RefSeq; NP_001138618.1; NM_001145146.1. [P34998-1]
RefSeq; NP_001138619.1; NM_001145147.1. [P34998-3]
RefSeq; NP_001138620.1; NM_001145148.1. [P34998-4]
RefSeq; NP_001243228.1; NM_001256299.2. [P34998-5]
RefSeq; NP_001289945.1; NM_001303016.1.
RefSeq; NP_001289947.1; NM_001303018.1. [P34998-5]
RefSeq; NP_004373.2; NM_004382.4. [P34998-2]
UniGene; Hs.417628; -.
PDB; 2L27; NMR; -; A=25-108.
PDB; 3EHS; X-ray; 2.76 A; A=24-119.
PDB; 3EHT; X-ray; 3.40 A; A=24-119.
PDB; 3EHU; X-ray; 1.96 A; A/B=24-119.
PDB; 4K5Y; X-ray; 2.98 A; A/B/C=104-373.
PDB; 4Z9G; X-ray; 3.18 A; A/B/C=104-249, A/B/C=252-401.
PDBsum; 2L27; -.
PDBsum; 3EHS; -.
PDBsum; 3EHT; -.
PDBsum; 3EHU; -.
PDBsum; 4K5Y; -.
PDBsum; 4Z9G; -.
ProteinModelPortal; P34998; -.
SMR; P34998; -.
BioGrid; 107784; 8.
IntAct; P34998; 2.
MINT; MINT-1217325; -.
STRING; 9606.ENSP00000381333; -.
BindingDB; P34998; -.
ChEMBL; CHEMBL1800; -.
DrugBank; DB09067; Corticorelin ovine triflutate.
GuidetoPHARMACOLOGY; 212; -.
TCDB; 9.A.14.4.3; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P34998; -.
PhosphoSitePlus; P34998; -.
BioMuta; CRHR1; -.
DMDM; 461836; -.
PaxDb; P34998; -.
PeptideAtlas; P34998; -.
PRIDE; P34998; -.
DNASU; 1394; -.
Ensembl; ENST00000314537; ENSP00000326060; ENSG00000120088. [P34998-2]
Ensembl; ENST00000352855; ENSP00000344068; ENSG00000120088. [P34998-3]
Ensembl; ENST00000398285; ENSP00000381333; ENSG00000120088. [P34998-1]
Ensembl; ENST00000577353; ENSP00000462016; ENSG00000120088. [P34998-4]
Ensembl; ENST00000613260; ENSP00000484387; ENSG00000278232. [P34998-1]
Ensembl; ENST00000615345; ENSP00000480752; ENSG00000278232. [P34998-3]
Ensembl; ENST00000616274; ENSP00000480396; ENSG00000276191. [P34998-1]
Ensembl; ENST00000616748; ENSP00000478177; ENSG00000276191. [P34998-3]
Ensembl; ENST00000617905; ENSP00000483802; ENSG00000276191. [P34998-2]
Ensembl; ENST00000618382; ENSP00000477786; ENSG00000278232. [P34998-2]
Ensembl; ENST00000633723; ENSP00000488342; ENSG00000276191. [P34998-4]
GeneID; 104909134; -.
GeneID; 1394; -.
KEGG; hsa:104909134; -.
KEGG; hsa:1394; -.
UCSC; uc002ijm.4; human. [P34998-1]
CTD; 104909134; -.
CTD; 1394; -.
DisGeNET; 104909134; -.
DisGeNET; 1394; -.
EuPathDB; HostDB:ENSG00000120088.14; -.
GeneCards; CRHR1; -.
HGNC; HGNC:2357; CRHR1.
MIM; 122561; gene.
neXtProt; NX_P34998; -.
OpenTargets; ENSG00000120088; -.
OpenTargets; ENSG00000263715; -.
PharmGKB; PA26874; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00900000140884; -.
HOGENOM; HOG000230719; -.
HOVERGEN; HBG106921; -.
InParanoid; P34998; -.
KO; K04578; -.
OMA; FICIGWC; -.
OrthoDB; EOG091G0BBY; -.
PhylomeDB; P34998; -.
TreeFam; TF315710; -.
Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
Reactome; R-HSA-418555; G alpha (s) signalling events.
SIGNOR; P34998; -.
ChiTaRS; CRHR1; human.
EvolutionaryTrace; P34998; -.
GeneWiki; Corticotropin_releasing_hormone_receptor_1; -.
PRO; PR:P34998; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000120088; -.
CleanEx; HS_CRHR1; -.
ExpressionAtlas; P34998; baseline and differential.
Genevisible; P34998; HS.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; IDA:UniProtKB.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; IDA:UniProtKB.
GO; GO:0051458; P:corticotropin secretion; ISS:UniProtKB.
GO; GO:0007565; P:female pregnancy; NAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0007567; P:parturition; TAS:ProtInc.
GO; GO:0010579; P:positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0010578; P:regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:2000852; P:regulation of corticosterone secretion; ISS:UniProtKB.
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; IPR036445; GPCR_2_extracell_dom_sf.
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;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000269|PubMed:11425856}.
CHAIN 24 444 Corticotropin-releasing factor receptor
1.
/FTId=PRO_0000012814.
TOPO_DOM 24 111 Extracellular.
TRANSMEM 112 142 Helical; Name=1.
TOPO_DOM 143 178 Cytoplasmic.
TRANSMEM 179 203 Helical; Name=2.
TOPO_DOM 204 218 Extracellular.
TRANSMEM 219 247 Helical; Name=3.
TOPO_DOM 248 254 Cytoplasmic.
TRANSMEM 255 282 Helical; Name=4.
TOPO_DOM 283 298 Extracellular.
TRANSMEM 299 324 Helical; Name=5.
TOPO_DOM 325 335 Cytoplasmic.
TRANSMEM 336 360 Helical; Name=6.
TOPO_DOM 361 367 Extracellular.
TRANSMEM 368 397 Helical; Name=7.
TOPO_DOM 398 444 Cytoplasmic.
REGION 99 108 Important for peptide agonist binding.
REGION 309 319 Important for antagonist binding.
MOD_RES 330 330 Phosphoserine; by PKA.
{ECO:0000269|PubMed:14657255}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 54
DISULFID 44 87
DISULFID 68 102
DISULFID 217 287
VAR_SEQ 1 204 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_045434.
VAR_SEQ 41 81 GLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTN
-> D (in isoform CRF-R3).
{ECO:0000303|PubMed:7811272}.
/FTId=VSP_001996.
VAR_SEQ 146 174 Missing (in isoform CRF-R2, isoform CRF-
R3 and isoform CRF-R4).
{ECO:0000303|PubMed:10598591,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:7692441,
ECO:0000303|PubMed:7811272,
ECO:0000303|PubMed:8243652,
ECO:0000303|Ref.7}.
/FTId=VSP_001997.
VAR_SEQ 385 398 Missing (in isoform CRF-R4).
{ECO:0000303|PubMed:10598591}.
/FTId=VSP_001998.
MUTAGEN 232 232 F->A: Nearly abolishes antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 235 235 M->A: Strongly reduces antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 309 309 L->A: Nearly abolishes antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 312 312 N->A: Nearly abolishes antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 313 313 F->A: Slightly reduces antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 316 316 L->A: Strongly reduces antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 319 319 I->A: Strongly reduces antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 356 356 Y->A: Strongly reduces antagonist
binding. {ECO:0000269|PubMed:23863939}.
MUTAGEN 384 384 Q->A: Increases antagonist binding.
{ECO:0000269|PubMed:23863939}.
TURN 25 27 {ECO:0000244|PDB:3EHT}.
HELIX 28 32 {ECO:0000244|PDB:3EHU}.
STRAND 49 52 {ECO:0000244|PDB:2L27}.
STRAND 62 67 {ECO:0000244|PDB:3EHU}.
STRAND 70 74 {ECO:0000244|PDB:3EHU}.
STRAND 81 87 {ECO:0000244|PDB:3EHU}.
TURN 89 91 {ECO:0000244|PDB:2L27}.
STRAND 93 98 {ECO:0000244|PDB:3EHS}.
HELIX 99 101 {ECO:0000244|PDB:2L27}.
HELIX 103 107 {ECO:0000244|PDB:3EHS}.
HELIX 116 143 {ECO:0000244|PDB:4K5Y}.
HELIX 175 177 {ECO:0000244|PDB:4K5Y}.
HELIX 179 205 {ECO:0000244|PDB:4K5Y}.
HELIX 207 212 {ECO:0000244|PDB:4K5Y}.
HELIX 215 236 {ECO:0000244|PDB:4K5Y}.
HELIX 238 253 {ECO:0000244|PDB:4K5Y}.
HELIX 257 259 {ECO:0000244|PDB:4K5Y}.
HELIX 270 296 {ECO:0000244|PDB:4K5Y}.
HELIX 300 326 {ECO:0000244|PDB:4K5Y}.
HELIX 334 337 {ECO:0000244|PDB:4K5Y}.
HELIX 339 367 {ECO:0000244|PDB:4K5Y}.
HELIX 369 382 {ECO:0000244|PDB:4Z9G}.
HELIX 384 398 {ECO:0000244|PDB:4Z9G}.
SEQUENCE 444 AA; 50719 MW; 7221AEFB0E7AA8ED CRC64;
MGGHPQLRLV KALLLLGLNP VSASLQDQHC ESLSLASNIS GLQCNASVDL IGTCWPRSPA
GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS ECQEILNEEK KSKVHYHVAV
IINYLGHCIS LVALLVAFVL FLRLRPGCTH WGDQADGALE VGAPWSGAPF QVRRSIRCLR
NIIHWNLISA FILRNATWFV VQLTMSPEVH QSNVGWCRLV TAAYNYFHVT NFFWMFGEGC
YLHTAIVLTY STDRLRKWMF ICIGWGVPFP IIVAWAIGKL YYDNEKCWFG KRPGVYTDYI
YQGPMILVLL INFIFLFNIV RILMTKLRAS TTSETIQYRK AVKATLVLLP LLGITYMLFF
VNPGEDEVSR VVFIYFNSFL ESFQGFFVSV FYCFLNSEVR SAIRKRWHRW QDKHSIRARV
ARAMSIPTSP TRVSFHSIKQ STAV


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