CRFR2_HUMAN
ID CRFR2_HUMAN Reviewed; 411 AA.
AC Q13324; B2R967; B3SXS6; B3SXS7; B3SXS8; B3SXT0; F8WA81; O43461; Q4QRJ4;
AC Q99431;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Corticotropin-releasing factor receptor 2;
DE Short=CRF-R-2;
DE Short=CRF-R2;
DE Short=CRFR-2;
DE AltName: Full=Corticotropin-releasing hormone receptor 2;
DE Short=CRH-R-2;
DE Short=CRH-R2;
GN Name=CRHR2; Synonyms=CRF2R, CRH2R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-ALPHA).
RX PubMed=8536644; DOI=10.1210/endo.137.1.8536644;
RA Liaw C.W., Lovenberg T.W., Barry G., Oltersdorf T., Grigoriadis D.E.,
RA de Souza E.B.;
RT "Cloning and characterization of the human corticotropin-releasing factor-2
RT receptor complementary deoxyribonucleic acid.";
RL Endocrinology 137:72-77(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-BETA).
RC TISSUE=Amygdala;
RA Kostich W.A., Chen A., Sperle K., Horlick R.A., Patterson J., Hyde T.M.,
RA Largent B.L.;
RT "Molecular cloning of the human CRH2B receptor isoform: divergence from the
RT rodent isoform in sequence and expression pattern.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRF2-GAMMA).
RC TISSUE=Amygdala;
RX PubMed=9717834; DOI=10.1210/mend.12.8.0145;
RA Kostich W.A., Chen A., Sperle K., Largent B.L.;
RT "Molecular identification and analysis of a novel human corticotropin-
RT releasing factor (CRF) receptor: the CRF2gamma receptor.";
RL Mol. Endocrinol. 12:1077-1085(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CRF2-ALPHA).
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF2-ALPHA).
RC TISSUE=Brain;
RA King M.M., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; E; F AND DESQ), AND ALTERNATIVE
RP SPLICING.
RA Wu S.V., Yuan P.-Q., Lai J., Tache Y.;
RT "Identification and characterization of novel CRF receptor type 2 isoforms
RT in human.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF2-ALPHA).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRF2-ALPHA).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-88 (ISOFORM CRF2-BETA).
RC TISSUE=Skeletal muscle;
RX PubMed=9199241; DOI=10.1016/s0167-4781(97)00047-x;
RA Valdenaire O., Giller T., Breu V., Gottowik J., Kilpatrick G.;
RT "A new functional isoform of the human CRF2 receptor for corticotropin-
RT releasing factor.";
RL Biochim. Biophys. Acta 1352:129-132(1997).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND NON-CLEAVABLE SIGNAL SEQUENCE.
RX PubMed=22689579; DOI=10.1074/jbc.m112.360594;
RA Teichmann A., Rutz C., Kreuchwig A., Krause G., Wiesner B., Schulein R.;
RT "The Pseudo signal peptide of the corticotropin-releasing factor receptor
RT type 2A prevents receptor oligomerization.";
RL J. Biol. Chem. 287:27265-27274(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-104 IN COMPLEXES WITH UCN; UCN2
RP AND UCN3, INTERACTION WITH CRF; UCN; UCN2 AND UCN3, AND DISULFIDE BONDS.
RX PubMed=20966082; DOI=10.1074/jbc.m110.186072;
RA Pal K., Swaminathan K., Xu H.E., Pioszak A.A.;
RT "Structural basis for hormone recognition by the Human CRFR2{alpha} G
RT protein-coupled receptor.";
RL J. Biol. Chem. 285:40351-40361(2010).
CC -!- FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing
CC factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN.
CC Ligand binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and down-stream
CC effectors, such as adenylate cyclase. Promotes the activation of
CC adenylate cyclase, leading to increased intracellular cAMP levels.
CC -!- SUBUNIT: Monomer. Interacts (via N-terminal extracellular domain) with
CC CRF, UCN, UCN2 and UCN3. Has highest affinity for UCN, and considerably
CC lower affinity for CRF, UNC2 and UCN3. {ECO:0000269|PubMed:20966082,
CC ECO:0000269|PubMed:22689579}.
CC -!- INTERACTION:
CC Q13324-1; P06850: CRH; NbExp=4; IntAct=EBI-26585317, EBI-3870390;
CC Q13324-1; Q969E3: UCN3; NbExp=2; IntAct=EBI-26585317, EBI-26585468;
CC Q13324-2; Q13021: MALL; NbExp=3; IntAct=EBI-23865243, EBI-750078;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22689579};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22689579}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=CRF2-alpha;
CC IsoId=Q13324-1; Sequence=Displayed;
CC Name=CRF2-beta;
CC IsoId=Q13324-2; Sequence=VSP_001999;
CC Name=CRF2-gamma;
CC IsoId=Q13324-3; Sequence=VSP_002000;
CC Name=D;
CC IsoId=Q13324-4; Sequence=VSP_053565;
CC Name=E;
CC IsoId=Q13324-5; Sequence=VSP_053566;
CC Name=F;
CC IsoId=Q13324-6; Sequence=VSP_053567;
CC Name=desQ;
CC IsoId=Q13324-7; Sequence=VSP_053564;
CC -!- DOMAIN: The transmembrane domain is composed of seven transmembrane
CC helices that are arranged in V-shape. Transmembrane helix 7 assumes a
CC sharply kinked structure (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The uncleaved pseudo signal peptide prevents receptor's
CC oligomerization and coupling to G(i) subunits. It is also responsible
CC for the rather low receptor localization at the plasma membrane
CC (PubMed:22689579). {ECO:0000269|PubMed:22689579}.
CC -!- PTM: A N-glycosylation site within the signal peptide impedes its
CC proper cleavage and function. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; U34587; AAA91320.1; -; mRNA.
DR EMBL; AF011406; AAB94503.1; -; mRNA.
DR EMBL; AF019381; AAB94562.1; -; mRNA.
DR EMBL; AB065699; BAC05922.1; -; Genomic_DNA.
DR EMBL; AY449734; AAR18078.1; -; mRNA.
DR EMBL; EU012439; ABV59313.1; -; mRNA.
DR EMBL; EU012440; ABV59314.1; -; mRNA.
DR EMBL; EU012441; ABV59315.1; -; mRNA.
DR EMBL; EU012443; ABV59317.1; -; mRNA.
DR EMBL; AK313661; BAG36414.1; -; mRNA.
DR EMBL; AC004976; AAC71653.1; -; Genomic_DNA.
DR EMBL; AC004976; AAC71654.1; -; Genomic_DNA.
DR EMBL; BC096830; AAH96830.1; -; mRNA.
DR EMBL; Y10151; CAA71235.1; -; mRNA.
DR CCDS; CCDS5429.1; -. [Q13324-1]
DR CCDS; CCDS56477.1; -. [Q13324-3]
DR CCDS; CCDS56478.1; -. [Q13324-2]
DR CCDS; CCDS75576.1; -. [Q13324-4]
DR RefSeq; NP_001189404.1; NM_001202475.1. [Q13324-2]
DR RefSeq; NP_001189410.1; NM_001202481.1. [Q13324-3]
DR RefSeq; NP_001189411.1; NM_001202482.1. [Q13324-7]
DR RefSeq; NP_001189412.1; NM_001202483.1. [Q13324-4]
DR RefSeq; NP_001874.2; NM_001883.4. [Q13324-1]
DR RefSeq; XP_011513430.1; XM_011515128.2.
DR RefSeq; XP_011513431.1; XM_011515129.2.
DR RefSeq; XP_016867241.1; XM_017011752.1. [Q13324-3]
DR PDB; 3N93; X-ray; 2.50 A; A/B=3-104.
DR PDB; 3N95; X-ray; 2.72 A; A/B/C/D=3-104.
DR PDB; 3N96; X-ray; 2.75 A; A/B/C/D=3-104.
DR PDB; 6PB1; EM; 2.80 A; P=2-388.
DR PDBsum; 3N93; -.
DR PDBsum; 3N95; -.
DR PDBsum; 3N96; -.
DR PDBsum; 6PB1; -.
DR AlphaFoldDB; Q13324; -.
DR SMR; Q13324; -.
DR BioGRID; 107785; 5.
DR IntAct; Q13324; 6.
DR MINT; Q13324; -.
DR STRING; 9606.ENSP00000340943; -.
DR BindingDB; Q13324; -.
DR ChEMBL; CHEMBL4069; -.
DR DrugCentral; Q13324; -.
DR GuidetoPHARMACOLOGY; 213; -.
DR GlyGen; Q13324; 5 sites.
DR PhosphoSitePlus; Q13324; -.
DR BioMuta; CRHR2; -.
DR DMDM; 6226847; -.
DR PaxDb; Q13324; -.
DR PeptideAtlas; Q13324; -.
DR PRIDE; Q13324; -.
DR ProteomicsDB; 30449; -.
DR ProteomicsDB; 59312; -. [Q13324-1]
DR ProteomicsDB; 59313; -. [Q13324-2]
DR ProteomicsDB; 59314; -. [Q13324-3]
DR Antibodypedia; 12618; 657 antibodies from 36 providers.
DR DNASU; 1395; -.
DR Ensembl; ENST00000341843.8; ENSP00000344304.4; ENSG00000106113.19. [Q13324-3]
DR Ensembl; ENST00000348438.8; ENSP00000340943.4; ENSG00000106113.19. [Q13324-2]
DR Ensembl; ENST00000471646.6; ENSP00000418722.1; ENSG00000106113.19. [Q13324-1]
DR Ensembl; ENST00000506074.6; ENSP00000426498.3; ENSG00000106113.19. [Q13324-4]
DR GeneID; 1395; -.
DR KEGG; hsa:1395; -.
DR MANE-Select; ENST00000471646.6; ENSP00000418722.1; NM_001883.5; NP_001874.2.
DR UCSC; uc003tbn.4; human. [Q13324-1]
DR CTD; 1395; -.
DR DisGeNET; 1395; -.
DR GeneCards; CRHR2; -.
DR HGNC; HGNC:2358; CRHR2.
DR HPA; ENSG00000106113; Tissue enhanced (brain, choroid plexus).
DR MIM; 602034; gene.
DR neXtProt; NX_Q13324; -.
DR OpenTargets; ENSG00000106113; -.
DR PharmGKB; PA26875; -.
DR VEuPathDB; HostDB:ENSG00000106113; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000156795; -.
DR HOGENOM; CLU_002753_4_1_1; -.
DR InParanoid; Q13324; -.
DR OMA; RINYSHC; -.
DR OrthoDB; 1163977at2759; -.
DR PhylomeDB; Q13324; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; Q13324; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q13324; -.
DR SIGNOR; Q13324; -.
DR BioGRID-ORCS; 1395; 13 hits in 1063 CRISPR screens.
DR ChiTaRS; CRHR2; human.
DR EvolutionaryTrace; Q13324; -.
DR GeneWiki; Corticotropin_releasing_hormone_receptor_2; -.
DR GenomeRNAi; 1395; -.
DR Pharos; Q13324; Tchem.
DR PRO; PR:Q13324; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q13324; protein.
DR Bgee; ENSG00000106113; Expressed in ganglionic eminence and 92 other tissues.
DR ExpressionAtlas; Q13324; baseline and differential.
DR Genevisible; Q13324; HS.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; IBA:GO_Central.
DR GO; GO:0043404; F:corticotropin-releasing hormone receptor activity; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003053; GPCR_2_CRF2_rcpt.
DR InterPro; IPR003051; GPCR_2_CRF_rcpt.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01279; CRFRECEPTOR.
DR PRINTS; PR01281; CRFRECEPTOR2.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Corticotropin-releasing factor receptor 2"
FT /id="PRO_0000012820"
FT SIGNAL 1..19
FT /note="Not cleaved"
FT TOPO_DOM 1..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..139
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 147..171
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 172..185
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..214
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 215..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 222..249
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 250..265
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 266..291
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 292..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 303..327
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 328..334
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 335..364
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 365..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 14..50
FT /evidence="ECO:0000269|PubMed:20966082"
FT DISULFID 40..83
FT /evidence="ECO:0000269|PubMed:20966082"
FT DISULFID 64..98
FT /evidence="ECO:0000269|PubMed:20966082"
FT DISULFID 184..254
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..34
FT /note="MDAALLHSLLEANCSLALAEELLLDGWGPPLDPE -> MRGPSGPPGLLYVP
FT HLLLCLLCLLPPPLQYAAGQSQMPKDQPLWALLEQYCHTIMTLTNLS (in isoform
FT CRF2-beta)"
FT /evidence="ECO:0000303|PubMed:9199241, ECO:0000303|Ref.2"
FT /id="VSP_001999"
FT VAR_SEQ 1..34
FT /note="MDAALLHSLLEANCSLALAEELLLDGWGPPLDPE -> MGREPWPEDRDLGF
FT PQLFCQ (in isoform CRF2-gamma)"
FT /evidence="ECO:0000303|PubMed:9717834"
FT /id="VSP_002000"
FT VAR_SEQ 106
FT /note="Missing (in isoform desQ)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_053564"
FT VAR_SEQ 366..411
FT /note="VRSAVRKRWHRWQDHHSLRVPMARAMSIPTSPTRISFHSIKQTAAV -> SW
FT VSKEAQAAGPHGREKPEQRW (in isoform D)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_053565"
FT VAR_SEQ 366..411
FT /note="VRSAVRKRWHRWQDHHSLRVPMARAMSIPTSPTRISFHSIKQTAAV -> GL
FT EPV (in isoform E)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_053566"
FT VAR_SEQ 367..411
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_053567"
FT VARIANT 220
FT /note="E -> D (in dbSNP:rs34625936)"
FT /id="VAR_049455"
FT CONFLICT 185
FT /note="R -> H (in Ref. 1; AAA91320 and 6; ABV59313/
FT ABV59314/ABV59315/ABV59317)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="W -> R (in Ref. 7; BAG36414)"
FT /evidence="ECO:0000305"
FT HELIX 3..27
FT /evidence="ECO:0007829|PDB:3N93"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3N93"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3N93"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3N93"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3N93"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3N96"
FT HELIX 111..140
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 147..170
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 182..213
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:6PB1"
FT TURN 232..236
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 266..297
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 301..315
FT /evidence="ECO:0007829|PDB:6PB1"
FT TURN 316..320
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 334..349
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:6PB1"
FT HELIX 364..381
FT /evidence="ECO:0007829|PDB:6PB1"
FT DISULFID Q13324-2:51..77
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 47688 MW; 96B99A93594CF07F CRC64;
MDAALLHSLL EANCSLALAE ELLLDGWGPP LDPEGPYSYC NTTLDQIGTC WPRSAAGALV
ERPCPEYFNG VKYNTTRNAY RECLENGTWA SKINYSQCEP ILDDKQRKYD LHYRIALVVN
YLGHCVSVAA LVAAFLLFLA LRSIRCLRNV IHWNLITTFI LRNVMWFLLQ LVDHEVHESN
EVWCRCITTI FNYFVVTNFF WMFVEGCYLH TAIVMTYSTE RLRKCLFLFI GWCIPFPIIV
AWAIGKLYYE NEQCWFGKEP GDLVDYIYQG PIILVLLINF VFLFNIVRIL MTKLRASTTS
ETIQYRKAVK ATLVLLPLLG ITYMLFFVNP GEDDLSQIMF IYFNSFLQSF QGFFVSVFYC
FFNGEVRSAV RKRWHRWQDH HSLRVPMARA MSIPTSPTRI SFHSIKQTAA V
