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Database: UniProt
Entry: A0A2R9CTL2_PANPA
LinkDB: A0A2R9CTL2_PANPA
Original site: A0A2R9CTL2_PANPA 
ID   A0A2R9CTL2_PANPA        Unreviewed;       443 AA.
AC   A0A2R9CTL2;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Corticotropin-releasing factor receptor 1 {ECO:0000256|ARBA:ARBA00021828};
GN   Name=CRHR1 {ECO:0000313|Ensembl:ENSPPAP00000043152.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000043152.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000043152.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000043152.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing
CC       factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand
CC       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       Inhibits the activity of the calcium channel CACNA1H. Required for
CC       normal embryonic development of the adrenal gland and for normal
CC       hormonal responses to stress. Plays a role in the response to
CC       anxiogenic stimuli. {ECO:0000256|ARBA:ARBA00001996}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000256|ARBA:ARBA00005314}.
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DR   EMBL; AJFE02012273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02012274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02012275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02012276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9CTL2; -.
DR   STRING; 9597.ENSPPAP00000043152; -.
DR   Ensembl; ENSPPAT00000066087.1; ENSPPAP00000043152.1; ENSPPAG00000044112.1.
DR   GeneTree; ENSGT00940000158410; -.
DR   OMA; NTTSQWS; -.
DR   Proteomes; UP000240080; Chromosome 17.
DR   Bgee; ENSPPAG00000044112; Expressed in cerebellum and 3 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; IEA:Ensembl.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd15445; 7tmB1_CRF-R1; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR003052; GPCR_2_CRF1_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   PANTHER; PTHR45620:SF2; CORTICOTROPIN-RELEASING FACTOR RECEPTOR 1; 1.
DR   PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF02793; HRM; 1.
DR   PRINTS; PR01279; CRFRECEPTOR.
DR   PRINTS; PR01280; CRFRECEPTOR1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00008; HormR; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 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   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603051-50};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..443
FT                   /note="Corticotropin-releasing factor receptor 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015339414"
FT   TRANSMEM        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..106
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          119..395
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   DISULFID        30..54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
FT   DISULFID        44..87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
FT   DISULFID        68..102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
FT   DISULFID        216..286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
SQ   SEQUENCE   443 AA;  50632 MW;  C89D9B2643F9EDFB CRC64;
     MGRHPQLRLV KALLLLGLNP VSASLQDQHC ESLSLASNIS GLQCNASVDL IGTCWPRSPA
     GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS ECQEILNEEK KSKVHYHVAV
     IINYLGHCIS LVALLVAFVL FLRLRPGCTH WGDQADGALE VGAPSGAPFQ VRRSIRCLRN
     IIHWNLISAF ILRNATWFVV QLTMSPEVHQ SNVGWCRLVT AAYNYFHVTN FFWMFGEGCY
     LHTAIVLTYS TDRLRKWMFI CIGWGVPFPI IVAWAIGKLY YDNEKCWFGK RPGVYTDYIY
     QGPMILVLLI NFIFLFNIVR ILMTKLRAST TSETIQYRKA VKATLVLLPL LGITYMLFFV
     NPGEDEVSRV VFIYFNSFLE SFQGFFVSVF YCFLNSEVRS AIRKRWHRWQ DKHSIRARVA
     RAMSIPTSPT RVSFHSIKQS TAV
//
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