ID   GNRR2_CLAGA             Reviewed;         379 AA.
AC   O42329;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Gonadotropin-releasing hormone II receptor;
DE            Short=GnRH II receptor;
DE            Short=GnRH-II-R;
DE   AltName: Full=Type II GnRH receptor;
OS   Clarias gariepinus (North African catfish) (Silurus gariepinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Clariidae; Clarias.
OX   NCBI_TaxID=13013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=9030732; DOI=10.1111/j.1432-1033.1997.0134a.x;
RA   Tensen C.P., Okuzawa K., Blomenroehr M., Rebers F.E.M., Leurs R.,
RA   Bogerd J., Schulz R.W., Goos H.J.T.;
RT   "Distinct efficacies for two endogenous ligands on a single cognate
RT   gonadoliberin receptor.";
RL   Eur. J. Biochem. 243:134-140(1997).
RN   [2]
RP   SEQUENCE REVISION TO 56.
RA   Bogerd J.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for gonadotropin releasing hormone II (GnRH II).
CC       This receptor mediates its action by association with G proteins that
CC       activate a phosphatidylinositol-calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated on the C-terminal cytoplasmic tail. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X97497; CAA66128.2; -; mRNA.
DR   AlphaFoldDB; O42329; -.
DR   SMR; O42329; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016500; F:protein-hormone receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001658; GphnRH_fam_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00529; GNADOTRPHINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..379
FT                   /note="Gonadotropin-releasing hormone II receptor"
FT                   /id="PRO_0000069496"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..140
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..184
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..210
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..230
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..302
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..328
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          355..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        117..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   379 AA;  42771 MW;  194430926562678D CRC64;
     MSGNTTLLLS NPTNVLDNSS VLNVSVSPPV LKWETPTFTT AARFRVAATL VLFVFAAASN
     LSVLLSVTRG RGRRLASHLR PLIASLASAD LVMTFVVMPL DAVWNVTVQW YAGDAMCKLM
     CFLKLFAMHS AAFILVVVSL DRHHAILHPL DTLDAGRRNR RMLLTAWILS LLLASPQLFI
     FRAIKAKGVD FVQCATHGSF QQHWQETAYN MFHFVTLYVF PLLVMSLCYT RILVEINRQM
     HRSKDKAGEP CLRRSGTDMI PKARMKTLKM TIIIVASFVI CWTPYYLLGI WYWFQPQMLH
     VIPDYVHHVF FVFGNLNTCC DPVIYGFFTP SFRADLSRCF CWRNQNASAK SLPHFSGHRR
     EVSGEAESDL GSGDQPSGQ