P34998 (CRFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CRHR1
Synonyms:	CRFR, CRFR1, CRHR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for corticotropin releasing factor (CRH). Shows high-affinity CRF binding. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Ref.16
Subunit structure	Interacts (via N-terminal extracellular domain) with CRF and UCN. Ref.15
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Predominantly expressed in the cerebellum, pituitary, cerebral cortex and olfactory lobe.
Post-translational modification	C-terminal Ser or Thr residues may be phosphorylated. Ref.14 Phosphorylation at Ser-330 by PKA prevents maximal coupling to Gq-protein, and thereby negatively regulates downstream signaling.
Sequence similarities	Belongs to the G-protein coupled receptor 2 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of adenylate cyclase activity Traceable author statement Ref.5. Source: ProtInc adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara adenylate cyclase-modulating G-protein coupled receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc behavioral response to cocaine Inferred from electronic annotation. Source: Compara behavioral response to pain Inferred from electronic annotation. Source: Compara eating behavior Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara epithelial cell differentiation Inferred from electronic annotation. Source: Compara female pregnancy Non-traceable author statement PubMed 7585095. Source: ProtInc hypothalamus development Inferred from electronic annotation. Source: Compara immune response Traceable author statement Ref.1. Source: ProtInc locomotory exploration behavior Inferred from electronic annotation. Source: Compara long-term synaptic potentiation Inferred from electronic annotation. Source: Compara memory Inferred from electronic annotation. Source: Compara negative regulation of appetite Inferred from electronic annotation. Source: Compara negative regulation of epinephrine secretion Inferred from electronic annotation. Source: Compara negative regulation of neuron death Inferred from electronic annotation. Source: Compara neuropeptide signaling pathway Inferred from electronic annotation. Source: Compara parturition Traceable author statement Ref.5. Source: ProtInc phospholipase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of mast cell degranulation Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to immobilization stress Inferred from electronic annotation. Source: Compara visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara axon part Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.5. Source: ProtInc multivesicular body Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara trans-Golgi network Inferred from electronic annotation. Source: Compara vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	corticotrophin-releasing factor receptor activity Traceable author statement Ref.5. Source: ProtInc corticotropin-releasing hormone binding Inferred from electronic annotation. Source: Compara corticotropin-releasing hormone receptor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRH	P06850	2	EBI-3870393,EBI-3870390

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform CRF-R1 (identifier: P34998-1)

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.

Isoform CRF-R2 (identifier: P34998-2)

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

Note: Major isoform.

Isoform CRF-R3 (identifier: P34998-3)

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.

Isoform CRF-R4 (identifier: P34998-4)

Also known as: 1D;

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

Isoform 5 (identifier: P34998-5)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.13

Chain

24 – 444

421

Corticotropin-releasing factor receptor 1

PRO_0000012814

Regions

Topological domain

24 – 121

98

Extracellular Potential

Transmembrane

122 – 142

21

Helical; Name=1; Potential

Topological domain

143 – 180

38

Cytoplasmic Potential

Transmembrane

181 – 200

20

Helical; Name=2; Potential

Topological domain

201 – 218

18

Extracellular Potential

Transmembrane

219 – 242

24

Helical; Name=3; Potential

Topological domain

243 – 256

14

Cytoplasmic Potential

Transmembrane

257 – 278

22

Helical; Name=4; Potential

Topological domain

279 – 297

19

Extracellular Potential

Transmembrane

298 – 320

23

Helical; Name=5; Potential

Topological domain

321 – 343

23

Cytoplasmic Potential

Transmembrane

344 – 363

20

Helical; Name=6; Potential

Topological domain

364 – 378

15

Extracellular Potential

Transmembrane

379 – 398

20

Helical; Name=7; Potential

Topological domain

399 – 444

46

Cytoplasmic Potential

Amino acid modifications

Modified residue

330

1

Phosphoserine; by PKA Ref.14

Glycosylation

38

1

N-linked (GlcNAc...) Potential

Glycosylation

45

1

N-linked (GlcNAc...) Potential

Glycosylation

78

1

N-linked (GlcNAc...) Potential

Glycosylation

90

1

N-linked (GlcNAc...) Potential

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Disulfide bond

30 ↔ 54

Ref.13 Ref.16

Disulfide bond

44 ↔ 87

Ref.13 Ref.16

Disulfide bond

68 ↔ 102

Ref.13 Ref.16

Natural variations

Alternative sequence

1 – 204

204

Missing in isoform 5.

VSP_045434

Alternative sequence

41 – 81

41

GLQCN…YNTTN → D in isoform CRF-R3.

VSP_001996

Alternative sequence

146 – 174

29

Missing in isoform CRF-R2, isoform CRF-R3 and isoform CRF-R4.

VSP_001997

Alternative sequence

385 – 398

14

Missing in isoform CRF-R4.

VSP_001998

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

444

Helix Strand Turn

Details...

Turn

25 – 27

3

Helix

28 – 32

5

Beta strand

49 – 52

4

Beta strand

62 – 67

6

Beta strand

70 – 74

5

Beta strand

81 – 87

7

Turn

89 – 91

3

Beta strand

93 – 98

6

Helix

99 – 101

3

Helix

103 – 107

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform CRF-R1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 7221AEFB0E7AA8ED	FASTA	444	50,719
	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
	Isoform CRF-R2 [UniParc]. Checksum: 81445283CCE34C6E	FASTA	415	47,671
	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 FLRLRSIRCL RNIIHWNLIS AFILRNATWF VVQLTMSPEV 190 200 210 220 230 240 HQSNVGWCRL VTAAYNYFHV TNFFWMFGEG CYLHTAIVLT YSTDRLRKWM FICIGWGVPF 250 260 270 280 290 300 PIIVAWAIGK LYYDNEKCWF GKRPGVYTDY IYQGPMILVL LINFIFLFNI VRILMTKLRA 310 320 330 340 350 360 STTSETIQYR KAVKATLVLL PLLGITYMLF FVNPGEDEVS RVVFIYFNSF LESFQGFFVS 370 380 390 400 410 VFYCFLNSEV RSAIRKRWHR WQDKHSIRAR VARAMSIPTS PTRVSFHSIK QSTAV
	Isoform CRF-R3 [UniParc]. Checksum: 6A2068BE9386F8B0	FASTA	375	43,331
	10 20 30 40 50 60 MGGHPQLRLV KALLLLGLNP VSASLQDQHC ESLSLASNIS DNGYRECLAN GSWAARVNYS 70 80 90 100 110 120 ECQEILNEEK KSKVHYHVAV IINYLGHCIS LVALLVAFVL FLRLRSIRCL RNIIHWNLIS 130 140 150 160 170 180 AFILRNATWF VVQLTMSPEV HQSNVGWCRL VTAAYNYFHV TNFFWMFGEG CYLHTAIVLT 190 200 210 220 230 240 YSTDRLRKWM FICIGWGVPF PIIVAWAIGK LYYDNEKCWF GKRPGVYTDY IYQGPMILVL 250 260 270 280 290 300 LINFIFLFNI VRILMTKLRA STTSETIQYR KAVKATLVLL PLLGITYMLF FVNPGEDEVS 310 320 330 340 350 360 RVVFIYFNSF LESFQGFFVS VFYCFLNSEV RSAIRKRWHR WQDKHSIRAR VARAMSIPTS 370 PTRVSFHSIK QSTAV
	Isoform CRF-R4 (1D) [UniParc]. Checksum: 3D8FF9B128810372	FASTA	401	46,030
	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 FLRLRSIRCL RNIIHWNLIS AFILRNATWF VVQLTMSPEV 190 200 210 220 230 240 HQSNVGWCRL VTAAYNYFHV TNFFWMFGEG CYLHTAIVLT YSTDRLRKWM FICIGWGVPF 250 260 270 280 290 300 PIIVAWAIGK LYYDNEKCWF GKRPGVYTDY IYQGPMILVL LINFIFLFNI VRILMTKLRA 310 320 330 340 350 360 STTSETIQYR KAVKATLVLL PLLGITYMLF FVNPGEDEVS RVVFIYFNSF LESFQVRSAI 370 380 390 400 RKRWHRWQDK HSIRARVARA MSIPTSPTRV SFHSIKQSTA V
	Isoform 5 [UniParc]. Checksum: F4465F15BF7C52E4	FASTA	240	28,122
	10 20 30 40 50 60 MSPEVHQSNV GWCRLVTAAY NYFHVTNFFW MFGEGCYLHT AIVLTYSTDR LRKWMFICIG 70 80 90 100 110 120 WGVPFPIIVA WAIGKLYYDN EKCWFGKRPG VYTDYIYQGP MILVLLINFI FLFNIVRILM 130 140 150 160 170 180 TKLRASTTSE TIQYRKAVKA TLVLLPLLGI TYMLFFVNPG EDEVSRVVFI YFNSFLESFQ 190 200 210 220 230 240 GFFVSVFYCF LNSEVRSAIR KRWHRWQDKH SIRARVARAM SIPTSPTRVS FHSIKQSTAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 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]	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 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]	"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.
[16]	"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.
[17]	"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 AGONIST.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00003083.
IPI00219267.
IPI00219268.
IPI00219269.

PIR

I38879.
A48260. I60975.

RefSeq

NP_001138618.1. NM_001145146.1.
NP_001138619.1. NM_001145147.1.
NP_001138620.1. NM_001145148.1.
NP_001243228.1. NM_001256299.1.
NP_004373.2. NM_004382.4.

UniGene

Hs.417628.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L27	NMR	-	A	25-109	[»]
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	[»]

ProteinModelPortal

P34998.

ModBase

Search...

Protein-protein interaction databases

IntAct

P34998. 1 interaction.

MINT

MINT-1217325.

STRING

9606.ENSP00000381333.

Protein family/group databases

GPCRDB

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PTM databases

PhosphoSite

P34998.

Polymorphism databases

DMDM

461836.

Proteomic databases

PaxDb

P34998.

PRIDE

P34998.

Protocols and materials databases

DNASU

1394.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000293493; ENSP00000293493; ENSG00000120088.
ENST00000314537; ENSP00000326060; ENSG00000120088.
ENST00000352855; ENSP00000344068; ENSG00000120088.
ENST00000398285; ENSP00000381333; ENSG00000120088.
ENST00000577353; ENSP00000462016; ENSG00000120088.

GeneID

1394.

KEGG

hsa:1394.

UCSC

uc002ijm.3. human.
uc002ijn.3. human.
uc010dap.3. human.
uc010dar.3. human.

Organism-specific databases

CTD

1394.

GeneCards

GC17P043699.

HGNC

HGNC:2357. CRHR1.

MIM

122561. gene.

neXtProt

NX_P34998.

PharmGKB

PA26874.

GenAtlas

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Phylogenomic databases

eggNOG

NOG295825.

HOGENOM

HOG000230719.

HOVERGEN

HBG106921.

KO

K04578.

OMA

VGWCRLV.

OrthoDB

EOG4DBTDQ.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P34998.

Bgee

P34998.

CleanEx

HS_CRHR1.

Genevestigator

P34998.

GermOnline

ENSG00000120088. Homo sapiens.

Family and domain databases

InterPro

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]

Pfam

PF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]

PRINTS

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

SMART

SM00008. HormR. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

P34998.

ChEMBL

CHEMBL1800.

EvolutionaryTrace

P34998.

GenomeRNAi

1394.

NextBio

5703.

SOURCE

Search...

Entry information

Entry name

CRFR1_HUMAN

Accession

Primary (citable) accession number: P34998
Secondary accession number(s): B4DIE9 , Q13008, Q4QRJ1, Q9UK64

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.