[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRF-R1 AND CRF-R2). TISSUE=Pituitary; DOI=10.1073/pnas.90.19.8967; PubMed=7692441 [NCBI, ExPASy, EBI, Israel, Japan] 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). TISSUE=Brain; DOI=10.1016/0014-5793(93)80427-V; PubMed=8243652 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1016/S0378-1119(98)00322-9; PubMed=9757017 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1006/bbrc.1994.2884; PubMed=7811272 [NCBI, ExPASy, EBI, Israel, Japan] 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). DOI=10.1210/me.13.12.2189; PubMed=10598591 [NCBI, ExPASy, EBI, Israel, Japan] 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 [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.
[7]	PROTEIN SEQUENCE OF 24-31, AND DISULFIDE BONDS. DOI=10.1074/jbc.M101838200; PubMed=11425856 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: This is a receptor for corticotropin releasing factor. Shows high-affinity CRF binding. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	CRF-R1
Isoform ID	P34998-1
This is the isoform sequence displayed in this entry.

Name	CRF-R2
Isoform ID	P34998-2
Note: Major isoform.
Features which should be applied to build the isoform sequence: VSP_001997.

Name	CRF-R3
Isoform ID	P34998-3
Note: Does not bind to CRF with high affinity.
Features which should be applied to build the isoform sequence: VSP_001996, VSP_001997.

Name	CRF-R4
Synonyms	1D
Isoform ID	P34998-4
Features which should be applied to build the isoform sequence: VSP_001997, VSP_001998.

TISSUE SPECIFICITY: Predominantly expressed in the cerebellum, pituitary, cerebral cortex and olfactory lobe.
PTM: C-terminal Ser or Thr residues may be phosphorylated.
SIMILARITY: Belongs to the G-protein coupled receptor 2 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L23333; AAA35719.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L23332; AAA35718.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X72304; CAA51052.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039523; AAC69993.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039510; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039511; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039512; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039513; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039514; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039515; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039516; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039517; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039518; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039519; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039520; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039521; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039522; AAC69993.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U16273; AAC50073.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF180301; AAD52688.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY457172; AAR19768.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00219267; -.
IPI00219268; -.
IPI00219269; -.
IPI00873090; -.

PIR

I38879; I38879.
I60975; A48260.

RefSeq

NP_001138618.1; -.
NP_001138619.1; -.
NP_001138620.1; -.
NP_004373.2; -.

UniGene

Hs.417628

3D structure databases

PDB

3EHS; X-ray; 2.76 A; A=24-119.	[ExPASy / RCSB / EBI]
3EHU; X-ray; 1.96 A; A/B=24-119.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

3EHS; -.
3EHU; -.

ModBase

P34998.

Protein family/group databases

GPCRDB

P34998; CRFR1_HUMAN.

PTM databases

PhosphoSite

P34998; -.

Organism-specific databases

GC17P041217; -.

HIX0027131; -.

HGNC:2357; CRHR1.

122561; gene. [NCBI / EBI]

PharmGKB

PA26874; -.

Gene expression databases

P34998; -.

P34998; -.

HS_CRHR1; -.

ENSG00000120088; Homo sapiens.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0015056;	Molecular function: corticotrophin-releasing factor receptor activity (traceable author statement from ProtInc).
GO:0007190;	Biological process: activation of adenylate cyclase activity (traceable author statement from ProtInc).
GO:0007565;	Biological process: female pregnancy (non-traceable author statement from ProtInc).
GO:0007188;	Biological process: G-protein signaling, coupled to cAMP nucleotide second messenger (traceable author statement from ProtInc).
GO:0006955;	Biological process: immune response (traceable author statement from ProtInc).
GO:0007567;	Biological process: parturition (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR017981; GPCR_2-like.
IPR003052; GPCR_2_CRF1_rcpt.
IPR003051; GPCR_2_CRF_rcpt.
IPR001879; GPCR_2_extracellular.
IPR000832; GPCR_2_secretin-like.
IPR017983; GPCR_2_secretin-like_CS.
Graphical view of domain structure.

PANTHER

PTHR12011:SF73; CRF_rcpt; 1.

Pfam

PF00002; 7tm_2; 1.
PF02793; HRM; 1.
Pfam graphical view of domain structure.

PRINTS

PR01279; CRFRECEPTOR.
PR01280; CRFRECEPTOR1.
PR00249; GPCRSECRETIN.

SMART

SM00008; HormR; 1.
SMART graphical view of domain structure.

PROSITE

PS00649; G_PROTEIN_RECEP_F2_1; 1.
PS00650; G_PROTEIN_RECEP_F2_2; 1.
PS50227; G_PROTEIN_RECEP_F2_3; 1.
PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P34998; -.

Genome annotation databases

Ensembl

ENSG00000120088; Homo sapiens. [Contig view]

GeneID

1394; -.

KEGG

hsa:1394; -.

Phylogenomic databases

HOVERGEN

P34998; -.

Other

5703; -.

CRHR1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cell membrane; Direct protein sequencing; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; Receptor; Signal; Transducer; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 444`	`421`	`Corticotropin-releasing factor receptor 1.`	`PRO_0000012814`
`TOPO_DOM`	`24 121`	`98`	`Extracellular (Potential).`
`TRANSMEM`	`122 142`	`21`	`1 (Potential).`
`TOPO_DOM`	`143 180`	`38`	`Cytoplasmic (Potential).`
`TRANSMEM`	`181 200`	`20`	`2 (Potential).`
`TOPO_DOM`	`201 218`	`18`	`Extracellular (Potential).`
`TRANSMEM`	`219 242`	`24`	`3 (Potential).`
`TOPO_DOM`	`243 256`	`14`	`Cytoplasmic (Potential).`
`TRANSMEM`	`257 278`	`22`	`4 (Potential).`
`TOPO_DOM`	`279 297`	`19`	`Extracellular (Potential).`
`TRANSMEM`	`298 320`	`23`	`5 (Potential).`
`TOPO_DOM`	`321 343`	`23`	`Cytoplasmic (Potential).`
`TRANSMEM`	`344 363`	`20`	`6 (Potential).`
`TOPO_DOM`	`364 378`	`15`	`Extracellular (Potential).`
`TRANSMEM`	`379 398`	`20`	`7 (Potential).`
`TOPO_DOM`	`399 444`	`46`	`Cytoplasmic (Potential).`
`CARBOHYD`	`38 38`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`45 45`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`78 78`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`90 90`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`98 98`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`30 54`
`DISULFID`	`44 87`
`DISULFID`	`68 102`
`VAR_SEQ`	`41 81`		`GLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVR` `YNTTN -> D (in isoform CRF-R3).`	`VSP_001996`
`VAR_SEQ`	`146 174`		`Missing (in isoform CRF-R2, isoform CRF-R3 and isoform CRF-R4).`	`VSP_001997`
`VAR_SEQ`	`385 398`		`Missing (in isoform CRF-R4).`	`VSP_001998`

Sequence information

Length: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 50719 Da [This is the MW of the unprocessed precursor]

CRC64: 7221AEFB0E7AA8ED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGGHPQLRLV KALLLLGLNP VSASLQDQHC ESLSLASNIS GLQCNASVDL IGTCWPRSPA 

        70         80         90        100        110        120 
GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS ECQEILNEEK KSKVHYHVAV 

       130        140        150        160        170        180 
IINYLGHCIS LVALLVAFVL FLRLRPGCTH WGDQADGALE VGAPWSGAPF QVRRSIRCLR 

       190        200        210        220        230        240 
NIIHWNLISA FILRNATWFV VQLTMSPEVH QSNVGWCRLV TAAYNYFHVT NFFWMFGEGC 

       250        260        270        280        290        300 
YLHTAIVLTY STDRLRKWMF ICIGWGVPFP IIVAWAIGKL YYDNEKCWFG KRPGVYTDYI 

       310        320        330        340        350        360 
YQGPMILVLL INFIFLFNIV RILMTKLRAS TTSETIQYRK AVKATLVLLP LLGITYMLFF 

       370        380        390        400        410        420 
VNPGEDEVSR VVFIYFNSFL ESFQGFFVSV FYCFLNSEVR SAIRKRWHRW QDKHSIRARV 

       430        440 
ARAMSIPTSP TRVSFHSIKQ STAV

P34998 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools