CALRL_DANRE
ID CALRL_DANRE Reviewed; 470 AA.
AC Q68EK2; A1L211; B0S6C2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Calcitonin gene-related peptide type 1 receptor;
DE Short=CGRP type 1 receptor;
DE AltName: Full=Calcitonin receptor-like receptor;
DE Flags: Precursor;
GN Name=calcrla; Synonyms=calcrl; ORFNames=si:dkey-249o24.2, zgc:100872;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) (By
CC similarity). Receptor specificity may be modulated by accessory
CC proteins. The activity of this receptor is mediated by G proteins which
CC activate adenylyl cyclase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAQ13571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX470245; CAQ13571.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC080226; AAH80226.1; -; mRNA.
DR EMBL; BC129300; AAI29301.1; -; mRNA.
DR RefSeq; NP_001004010.1; NM_001004010.1.
DR AlphaFoldDB; Q68EK2; -.
DR SMR; Q68EK2; -.
DR STRING; 7955.ENSDARP00000111592; -.
DR PaxDb; Q68EK2; -.
DR GeneID; 445508; -.
DR KEGG; dre:445508; -.
DR CTD; 445508; -.
DR ZFIN; ZDB-GENE-040822-26; calcrla.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q68EK2; -.
DR OrthoDB; 1005634at2759; -.
DR PhylomeDB; Q68EK2; -.
DR TreeFam; TF315710; -.
DR Reactome; R-DRE-418555; G alpha (s) signalling events.
DR Reactome; R-DRE-419812; Calcitonin-like ligand receptors.
DR PRO; PR:Q68EK2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001605; F:adrenomedullin receptor activity; IBA:GO_Central.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:InterPro.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0048844; P:artery morphogenesis; IMP:ZFIN.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0055064; P:chloride ion homeostasis; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IGI:ZFIN.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003289; GPCR_2_CGRP1_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; PR01351; CGRPRECEPTOR.
DR PRINTS; PR01350; CTRFAMILY.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..470
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373833"
FT TOPO_DOM 24..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..174
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..201
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..244
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..281
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..321
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..362
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..396
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
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 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..82
FT /evidence="ECO:0000250"
FT DISULFID 73..113
FT /evidence="ECO:0000250"
FT DISULFID 96..135
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="C -> R (in Ref. 2; AAI29301)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="C -> R (in Ref. 2; AAI29301)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Y -> F (in Ref. 2; AAI29301)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="K -> E (in Ref. 1; CAQ13571 and 2; AAI29301)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="F -> L (in Ref. 1; CAQ13571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 54102 MW; 7CB0C91BF7AE4921 CRC64;
MTASCWTICL FLLGSVTEFI VLASPEVNES QQQHPQNVYH DIGVTRNKIV TAQFECYQKI
MKDNSQDRRG PVCNRTWDGW LCWDDTEAGI TSEQHCPDYF QDFDPTEMVT KICTESGQWF
LHPESNRTWT NFTRCNLHTT EGRRTAMNLF YLALIGHGLS LTSLFISLGI FFHFKSLSCQ
RITLHKNLFF SFVLNSIITI IWLTAVANNQ ELVQQNPISC KISQFIHLYI FGCNYFWMLC
EGIYLHTLIV VAVFAEKQHL MWYYLLGWGF PLIPATIHAV ARSYYYNDNC WISSNTSLLY
IIHGPICAAM LVNLFFLLNI VRVLITKLKV THQAKSSLYM KAVRATLILV PLLGIQYVLL
PYKPSGRVSA EIYDYIMHIL MHYQGLLVAT IFCFFNGEVQ AVLRRHWNQY RIQFGSTITQ
SDALRSASYT ASSITEVQGC YSIDGHTEHL NGKNYHDFDN AIIKPENPFA
