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Corticotropin-releasing factor receptor 2 (CRF-R-2) (CRF-R2) (CRFR-2) (Corticotropin-releasing hormone receptor 2) (CRH-R-2) (CRH-R2)

 CRFR2_RAT               Reviewed;         411 AA.
P47866; G3V948;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
22-JAN-2014, sequence version 2.
22-NOV-2017, entry version 136.
RecName: Full=Corticotropin-releasing factor receptor 2;
Short=CRF-R-2;
Short=CRF-R2;
Short=CRFR-2;
AltName: Full=Corticotropin-releasing hormone receptor 2;
Short=CRH-R-2;
Short=CRH-R2;
Name=Crhr2; Synonyms=Crf2r;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Hypothalamus, and Lung;
PubMed=7846062; DOI=10.1073/pnas.92.3.836;
Lovenberg T.W., Liaw C.W., Grigoriadis D.E., Clevenger W.,
Chalmers D.T., de Souza E.B., Oltersdorf T.;
"Cloning and characterization of a functionally distinct
corticotropin-releasing factor receptor subtype from rat brain.";
Proc. Natl. Acad. Sci. U.S.A. 92:836-840(1995).
[2]
ERRATUM.
Lovenberg T.W., Liaw C.W., Grigoriadis D.E., Clevenger W.,
Chalmers D.T., de Souza E.B., Oltersdorf T.;
Proc. Natl. Acad. Sci. U.S.A. 92:5759-5759(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
GLYCOSYLATION AT ASN-13, MUTAGENESIS OF ASN-13, NON-CLEAVABLE SIGNAL
SEQUENCE, AND SUBCELLULAR LOCATION.
PubMed=16766521; DOI=10.1074/jbc.M601554200;
Rutz C., Renner A., Alken M., Schulz K., Beyermann M., Wiesner B.,
Rosenthal W., Schulein R.;
"The corticotropin-releasing factor receptor type 2a contains an N-
terminal pseudo signal peptide.";
J. Biol. Chem. 281:24910-24921(2006).
-!- FUNCTION: G-protein coupled receptor for CRH (corticotropin-
releasing factor), UCN (urocortin), UCN2 and UCN3. Has high
affinity for UCN. Ligand binding causes a conformation change that
triggers signaling via guanine nucleotide-binding proteins (G
proteins) and down-stream effectors, such as adenylate cyclase.
Promotes the activation of adenylate cyclase, leading to increased
intracellular cAMP levels. {ECO:0000269|PubMed:7846062}.
-!- SUBUNIT: Monomer. Interacts (via N-terminal extracellular domain)
with CRF, UCN, UCN2 and UCN3 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16766521,
ECO:0000269|PubMed:7846062}; Multi-pass membrane protein
{ECO:0000269|PubMed:16766521, ECO:0000269|PubMed:7846062}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=CRF2-alpha;
IsoId=P47866-1; Sequence=Displayed;
Note=Major isoform.;
Name=CRF2-beta;
IsoId=P47866-2; Sequence=VSP_002001;
-!- TISSUE SPECIFICITY: Predominantly expressed in limbic regions of
the brain such as the lateral septum, the entorhinal cortex, the
hypothalamic ventromedial nucleus and several amygdaloid nuclei.
Also detectable in lung, kidney and heart.
{ECO:0000269|PubMed:7846062}.
-!- DOMAIN: The transmembrane domain is composed of seven
transmembrane helices that are arranged in V-shape. Transmembrane
helix 7 assumes a sharply kinked structure (By similarity).
{ECO:0000250}.
-!- DOMAIN: The uncleaved pseudo signal peptide prevents receptor's
oligomerization and coupling to G(i) subunits. It is also
responsible for the rather low receptor localization at the plasma
membrane (By similarity). {ECO:0000250}.
-!- PTM: A N-glycosylation site within the signal peptide impedes its
proper cleavage and function. {ECO:0000269|PubMed:16766521}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U16253; AAC52159.1; -; mRNA.
EMBL; AABR06031050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474011; EDL88099.1; -; Genomic_DNA.
PIR; A55610; A55610.
RefSeq; NP_073205.1; NM_022714.1.
UniGene; Rn.10023; -.
ProteinModelPortal; P47866; -.
SMR; P47866; -.
BioGrid; 249194; 7.
STRING; 10116.ENSRNOP00000014925; -.
BindingDB; P47866; -.
ChEMBL; CHEMBL3581; -.
GuidetoPHARMACOLOGY; 213; -.
iPTMnet; P47866; -.
PhosphoSitePlus; P47866; -.
PaxDb; P47866; -.
PRIDE; P47866; -.
Ensembl; ENSRNOT00000033672; ENSRNOP00000035712; ENSRNOG00000011145. [P47866-1]
GeneID; 64680; -.
KEGG; rno:64680; -.
UCSC; RGD:70547; rat. [P47866-1]
CTD; 1395; -.
RGD; 70547; Crhr2.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00900000140884; -.
HOGENOM; HOG000230719; -.
HOVERGEN; HBG106921; -.
InParanoid; P47866; -.
KO; K04579; -.
Reactome; R-RNO-373080; Class B/2 (Secretin family receptors).
Reactome; R-RNO-418555; G alpha (s) signalling events.
PRO; PR:P47866; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000011145; -.
ExpressionAtlas; P47866; baseline and differential.
Genevisible; P47866; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0070852; C:cell body fiber; IDA:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0043196; C:varicosity; IDA:RGD.
GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; ISO:RGD.
GO; GO:0043404; F:corticotropin-releasing hormone receptor activity; IDA:RGD.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:RGD.
GO; GO:0005179; F:hormone activity; ISO:RGD.
GO; GO:0017046; F:peptide hormone binding; IPI:RGD.
GO; GO:0007015; P:actin filament organization; IMP:RGD.
GO; GO:0042423; P:catecholamine biosynthetic process; IMP:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0030855; P:epithelial cell differentiation; IMP:RGD.
GO; GO:0007631; P:feeding behavior; NAS:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:RGD.
GO; GO:0035482; P:gastric motility; IMP:RGD.
GO; GO:0021854; P:hypothalamus development; IEP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
GO; GO:0090281; P:negative regulation of calcium ion import; IMP:RGD.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IDA:RGD.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISO:RGD.
GO; GO:2000293; P:negative regulation of defecation; IMP:RGD.
GO; GO:0032811; P:negative regulation of epinephrine secretion; IMP:RGD.
GO; GO:2000252; P:negative regulation of feeding behavior; IDA:RGD.
GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
GO; GO:0033685; P:negative regulation of luteinizing hormone secretion; IMP:RGD.
GO; GO:0010700; P:negative regulation of norepinephrine secretion; IMP:RGD.
GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:RGD.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; IMP:RGD.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
GO; GO:0014064; P:positive regulation of serotonin secretion; IMP:RGD.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:RGD.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
GO; GO:0048630; P:skeletal muscle tissue growth; IDA:RGD.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR003053; GPCR_2_CRF2_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; PR01281; CRFRECEPTOR2.
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;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 411 Corticotropin-releasing factor receptor
2.
/FTId=PRO_0000012822.
SIGNAL 1 19 Not cleaved.
TOPO_DOM 1 108 Extracellular. {ECO:0000250}.
TRANSMEM 109 139 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 140 146 Cytoplasmic. {ECO:0000250}.
TRANSMEM 147 171 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 172 185 Extracellular. {ECO:0000250}.
TRANSMEM 186 214 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 215 221 Cytoplasmic. {ECO:0000250}.
TRANSMEM 222 249 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 250 265 Extracellular. {ECO:0000250}.
TRANSMEM 266 291 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 292 302 Cytoplasmic. {ECO:0000250}.
TRANSMEM 303 327 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 328 334 Extracellular. {ECO:0000250}.
TRANSMEM 335 364 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 365 411 Cytoplasmic. {ECO:0000250}.
CARBOHYD 13 13 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16766521}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 14 50 {ECO:0000250}.
DISULFID 40 83 {ECO:0000250}.
DISULFID 64 98 {ECO:0000250}.
DISULFID 184 254 {ECO:0000250}.
VAR_SEQ 1 34 MDAALLLSLLEANCSLALAEELLLDGWGEPPDPE -> MGH
PGSLPSAQLLLCLYSLLPLLQVAQPGRPLQDQPLWTLLEQY
CHRTTTRNFS (in isoform CRF2-beta).
{ECO:0000305}.
/FTId=VSP_002001.
MUTAGEN 13 13 N->A,F,I: Allows cleavage of signal
peptide. {ECO:0000269|PubMed:16766521}.
CONFLICT 93 93 V -> I (in Ref. 1; AAC52159).
{ECO:0000305}.
SEQUENCE 411 AA; 47693 MW; F0BA7795F8C37AFE CRC64;
MDAALLLSLL EANCSLALAE ELLLDGWGEP PDPEGPYSYC NTTLDQIGTC WPQSAPGALV
ERPCPEYFNG IKYNTTRNAY RECLENGTWA SRVNYSHCEP ILDDKQRKYD LHYRIALIIN
YLGHCVSVVA LVAAFLLFLV LRSIRCLRNV IHWNLITTFI LRNITWFLLQ LIDHEVHEGN
EVWCRCVTTI FNYFVVTNFF WMFVEGCYLH TAIVMTYSTE HLRKWLFLFI GWCIPCPIIV
AWAVGKLYYE NEQCWFGKEP GDLVDYIYQG PIILVLLINF VFLFNIVRIL MTKLRASTTS
ETIQYRKAVK ATLVLLPLLG ITYMLFFVNP GEDDLSQIVF IYFNSFLQSF QGFFVSVFYC
FFNGEVRSAL RKRWHRWQDH HALRVPVARA MSIPTSPTRI SFHSIKQTAA V


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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